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Conserved domains on  [gi|1034661056|ref|XP_016869182|]
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adhesion G protein-coupled receptor B1 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
7tmB2_BAI_Adhesion_VII cd15251
brain-specific angiogenesis inhibitors, group VII adhesion GPCRs, member of the class B2 ...
941-1231 1.55e-157

brain-specific angiogenesis inhibitors, group VII adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediate direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


:

Pssm-ID: 320379  Cd Length: 253  Bit Score: 479.44  E-value: 1.55e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  941 ATLPSVTLIVGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFL 1020
Cdd:cd15251      1 AGSPSVTLIVGCGVSCLALLTLLAIYAAFWRYIRSERSIILINFCLSIISSNILILVGQTQTLNKGVCTMTAAFLHFFFL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1021 SSFCWVLTEAWQSYMAVTGHLRNRLIRKRFLCLGWGLPALVVAISVGFTKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVV 1100
Cdd:cd15251     81 SSFCWVLTEAWQSYMAVTGRMRTRLIRKRFLCLGWGLPALVVAVSVGFTRTKGYGTSSYCWLSLEGGLLYAFVGPAAAVV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1101 LVNMVIGILVFNKLVSKDGITDkklkeragqpsphplgralkcaecgvlsaadatsdatsNAMASLWSSCVVLPLLALTW 1180
Cdd:cd15251    161 LVNMVIGILVFNKLVSRDGISD--------------------------------------NAMASLWSSCVVLPLLALTW 202
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034661056 1181 MSAVLAVTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVKCRVVD 1231
Cdd:cd15251    203 MSAVLAMTDRRSVLFQILFAVFDSLQGFVIVMVHCILRREVQDAVKCRMGV 253
AGRB_N pfam19188
Adhesion GPCR B N-terminal region; This region is found at the N-terminus of various adhesion ...
41-216 1.69e-92

Adhesion GPCR B N-terminal region; This region is found at the N-terminus of various adhesion G-protein coupled receptor B proteins. This region contains 10 cysteine residues that probably form disulphide bonds.


:

Pssm-ID: 465991  Cd Length: 177  Bit Score: 296.70  E-value: 1.69e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056   41 EPCATLVQGKFFGYFSAAAVFPANASRCSWTLRNPDPRRYTLYMKVAKAPVPCSgPGRVRTYQFDSFLES-TRTYLGVES 119
Cdd:pfam19188    1 DPCSTLVQGVLYGSFSLRDLFPTNASGCSWTLENPDPTKYTLYLKFTKPTQSCL-PFSPRLLQFDHYLENtTRTYLGRES 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  120 FDEVLRLCDPSAPLAFLQASKQFLQMRRQQPPQHDglrPRAGPPGPTDDFSVEYLVVGNRNPSRAACQMLCRWLDACLAG 199
Cdd:pfam19188   80 FDEVVELCDASSPFSFLEFDKNFVQLCLLAEPRGD---PESVVPGPSGDFKVEVLVINNENPSQFTCGVLCRWLEECLSA 156
                          170
                   ....*....|....*..
gi 1034661056  200 SRSSHPCGIMQTPCACL 216
Cdd:pfam19188  157 STSSRPCGIMQTPCICP 173
GAIN pfam16489
GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and ...
658-856 2.84e-52

GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and beta-strands that is found in cell-adhesion GPCRs and precedes the GPS motif where the autoproteolysis occurs, family, pfam01825. The full GAIN domain, comprises the GPS and the GAIN, in cell-adhesion GPCRs, and is the functional unit for autoproteolysis. The GPS motif at the end of the GAIN domain is an ancient domain that exists in primitive ancestor organizms, and the full GAIN + GPS is conserved in all cell-adhesion GPCRs and all PKD1-related proteins.


:

Pssm-ID: 465137  Cd Length: 205  Bit Score: 182.85  E-value: 2.84e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  658 GVSEVIQTLVEISQDGTSYSGDLLSTIDVLRNMTEIFRRAYYSPTPGDVQNFVQILSNLLAEENRDKWEEAQLAGPNAKE 737
Cdd:pfam16489    1 GAKELARELRNATRHGPLYGGDVLTAVELLSQLFDLLATQDATLSNAFLENFVQTVSNLLDPENRESWEDLQQTERGTAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  738 --LFRLVEDFVDVIGFRMKDLRDAYQVTDNLVLSIHKLPAS---GATDISFPMKGWRATGdwakvpEDRVTVSKSVFStg 812
Cdd:pfam16489   81 tkLLRTLEEYALLLAQNMKYLTPFTIVTPNIVLSVDRLDTHnfkGARFPRFPMKGERPKD------EDSVKLPPKAFK-- 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034661056  813 ltEADEASVFVVGTVLYRNLGSFLALQRN-----------TTVLNSKVISVTVKP 856
Cdd:pfam16489  153 --PPDSNGTVVVVFILYRNLGSLLPPSSRydpdrrslrlpRRVVNSPVVSASVHS 205
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
412-462 5.52e-16

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 73.39  E-value: 5.52e-16
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034661056   412 WDEWSPWSLCSSTCGRGFRDRTRTC--RPPQFGGNPCEGPEKQTKFCNIALCP 462
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
522-572 2.50e-14

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 68.77  E-value: 2.50e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034661056   522 WQAWASWGSCSVTCGAGSQRRERVCSGP--FFGGAACQGPQDEYRQCGTQRCP 572
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPppQNGGGPCTGEDVETRACNEQPCP 53
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
877-935 3.50e-12

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


:

Pssm-ID: 197639  Cd Length: 49  Bit Score: 62.40  E-value: 3.50e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034661056   877 TNQTCILWDETDvpsssappqlGPWSWRGCRTVPLDALRTRCLCDRLSTFAILAQLSAD 935
Cdd:smart00303    1 FNPICVFWDESS----------GEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
359-407 7.08e-12

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 61.83  E-value: 7.08e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1034661056   359 EWSPWSVCSSTCGEGWQTRTRFCVSSSYS---TQCSGPLREQRLCNNSAvCP 407
Cdd:smart00209    3 EWSEWSPCSVTCGGGVQTRTRSCCSPPPQnggGPCTGEDVETRACNEQP-CP 53
HormR smart00008
Domain present in hormone receptors;
574-640 9.31e-11

Domain present in hormone receptors;


:

Pssm-ID: 214468  Cd Length: 70  Bit Score: 59.07  E-value: 9.31e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034661056   574 PHEICDEDNFGAVIWKETPAGEVAAVRCPRNATGL-----ILRRCELDEegiaYWEP--PTYIRCVSIDYRNIQ 640
Cdd:smart00008    1 TDLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGFsyktgASRNCTENG----GWSPpfPNYSNCTSNDYEELK 70
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
264-314 2.73e-08

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 51.43  E-value: 2.73e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1034661056   264 WKLWSLWGECTRDCGGGLQTRTRTC-LPAPGVEGGGCEGVLEEGRQCNREAC 314
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcSPPPQNGGGPCTGEDVETRACNEQPC 52
 
Name Accession Description Interval E-value
7tmB2_BAI_Adhesion_VII cd15251
brain-specific angiogenesis inhibitors, group VII adhesion GPCRs, member of the class B2 ...
941-1231 1.55e-157

brain-specific angiogenesis inhibitors, group VII adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediate direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320379  Cd Length: 253  Bit Score: 479.44  E-value: 1.55e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  941 ATLPSVTLIVGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFL 1020
Cdd:cd15251      1 AGSPSVTLIVGCGVSCLALLTLLAIYAAFWRYIRSERSIILINFCLSIISSNILILVGQTQTLNKGVCTMTAAFLHFFFL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1021 SSFCWVLTEAWQSYMAVTGHLRNRLIRKRFLCLGWGLPALVVAISVGFTKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVV 1100
Cdd:cd15251     81 SSFCWVLTEAWQSYMAVTGRMRTRLIRKRFLCLGWGLPALVVAVSVGFTRTKGYGTSSYCWLSLEGGLLYAFVGPAAAVV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1101 LVNMVIGILVFNKLVSKDGITDkklkeragqpsphplgralkcaecgvlsaadatsdatsNAMASLWSSCVVLPLLALTW 1180
Cdd:cd15251    161 LVNMVIGILVFNKLVSRDGISD--------------------------------------NAMASLWSSCVVLPLLALTW 202
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034661056 1181 MSAVLAVTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVKCRVVD 1231
Cdd:cd15251    203 MSAVLAMTDRRSVLFQILFAVFDSLQGFVIVMVHCILRREVQDAVKCRMGV 253
AGRB_N pfam19188
Adhesion GPCR B N-terminal region; This region is found at the N-terminus of various adhesion ...
41-216 1.69e-92

Adhesion GPCR B N-terminal region; This region is found at the N-terminus of various adhesion G-protein coupled receptor B proteins. This region contains 10 cysteine residues that probably form disulphide bonds.


Pssm-ID: 465991  Cd Length: 177  Bit Score: 296.70  E-value: 1.69e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056   41 EPCATLVQGKFFGYFSAAAVFPANASRCSWTLRNPDPRRYTLYMKVAKAPVPCSgPGRVRTYQFDSFLES-TRTYLGVES 119
Cdd:pfam19188    1 DPCSTLVQGVLYGSFSLRDLFPTNASGCSWTLENPDPTKYTLYLKFTKPTQSCL-PFSPRLLQFDHYLENtTRTYLGRES 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  120 FDEVLRLCDPSAPLAFLQASKQFLQMRRQQPPQHDglrPRAGPPGPTDDFSVEYLVVGNRNPSRAACQMLCRWLDACLAG 199
Cdd:pfam19188   80 FDEVVELCDASSPFSFLEFDKNFVQLCLLAEPRGD---PESVVPGPSGDFKVEVLVINNENPSQFTCGVLCRWLEECLSA 156
                          170
                   ....*....|....*..
gi 1034661056  200 SRSSHPCGIMQTPCACL 216
Cdd:pfam19188  157 STSSRPCGIMQTPCICP 173
7tm_2 pfam00002
7 transmembrane receptor (Secretin family); This family is known as Family B, the ...
941-1210 5.52e-70

7 transmembrane receptor (Secretin family); This family is known as Family B, the secretin-receptor family or family 2 of the G-protein-coupled receptors (GCPRs). They have been described in many animal species, but not in plants, fungi or prokaryotes. Three distinct sub-families are recognized. Subfamily B1 contains classical hormone receptors, such as receptors for secretin and glucagon, that are all involved in cAMP-mediated signalling pathways. Subfamily B2 contains receptors with long extracellular N-termini, such as the leukocyte cell-surface antigen CD97; calcium-independent receptors for latrotoxin, and brain-specific angiogenesis inhibitors amongst others. Subfamily B3 includes Methuselah and other Drosophila proteins. Other than the typical seven-transmembrane region, characteriztic structural features include an amino-terminal extracellular domain involved in ligand binding, and an intracellular loop (IC3) required for specific G-protein coupling.


Pssm-ID: 459625 [Multi-domain]  Cd Length: 248  Bit Score: 235.25  E-value: 5.52e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  941 ATLPSVTLIVGCGVSSLTLLMLVIIYVSVwRYIRSERSVILINFCLSIISSNALILIGQTQTRNK--------VVCTLVA 1012
Cdd:pfam00002    1 ALSLKVIYTVGYSLSLVALLLAIAIFLLF-RKLHCTRNYIHLNLFASFILRALLFLVGDAVLFNKqdldhcswVGCKVVA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1013 AFLHFFFLSSFCWVLTEAWQSYMA-VTGHLRNRLIRKRFLCLGWGLPALVVAISVGFTkAKGYSTMNYCWLSLEGGLLYA 1091
Cdd:pfam00002   80 VFLHYFFLANFFWMLVEGLYLYTLlVEVFFSERKYFWWYLLIGWGVPALVVGIWAGVD-PKGYGEDDGCWLSNENGLWWI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1092 FVGPAAAVVLVNMVIGILVFNKLVSKDGITDKKLKERAgqpsphplgralkcaecgvlsaadatsdatsNAMASLWSSCV 1171
Cdd:pfam00002  159 IRGPILLIILVNFIIFINIVRILVQKLRETNMGKSDLK-------------------------------QYRRLAKSTLL 207
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1034661056 1172 VLPLLALTWMSAVLAVTDRR--SALFQILFAVFDSLEGFVI 1210
Cdd:pfam00002  208 LLPLLGITWVFGLFAFNPENtlRVVFLYLFLILNSFQGFFV 248
GAIN pfam16489
GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and ...
658-856 2.84e-52

GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and beta-strands that is found in cell-adhesion GPCRs and precedes the GPS motif where the autoproteolysis occurs, family, pfam01825. The full GAIN domain, comprises the GPS and the GAIN, in cell-adhesion GPCRs, and is the functional unit for autoproteolysis. The GPS motif at the end of the GAIN domain is an ancient domain that exists in primitive ancestor organizms, and the full GAIN + GPS is conserved in all cell-adhesion GPCRs and all PKD1-related proteins.


Pssm-ID: 465137  Cd Length: 205  Bit Score: 182.85  E-value: 2.84e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  658 GVSEVIQTLVEISQDGTSYSGDLLSTIDVLRNMTEIFRRAYYSPTPGDVQNFVQILSNLLAEENRDKWEEAQLAGPNAKE 737
Cdd:pfam16489    1 GAKELARELRNATRHGPLYGGDVLTAVELLSQLFDLLATQDATLSNAFLENFVQTVSNLLDPENRESWEDLQQTERGTAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  738 --LFRLVEDFVDVIGFRMKDLRDAYQVTDNLVLSIHKLPAS---GATDISFPMKGWRATGdwakvpEDRVTVSKSVFStg 812
Cdd:pfam16489   81 tkLLRTLEEYALLLAQNMKYLTPFTIVTPNIVLSVDRLDTHnfkGARFPRFPMKGERPKD------EDSVKLPPKAFK-- 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034661056  813 ltEADEASVFVVGTVLYRNLGSFLALQRN-----------TTVLNSKVISVTVKP 856
Cdd:pfam16489  153 --PPDSNGTVVVVFILYRNLGSLLPPSSRydpdrrslrlpRRVVNSPVVSASVHS 205
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
412-462 5.52e-16

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 73.39  E-value: 5.52e-16
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034661056   412 WDEWSPWSLCSSTCGRGFRDRTRTC--RPPQFGGNPCEGPEKQTKFCNIALCP 462
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
522-572 2.50e-14

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 68.77  E-value: 2.50e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034661056   522 WQAWASWGSCSVTCGAGSQRRERVCSGP--FFGGAACQGPQDEYRQCGTQRCP 572
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPppQNGGGPCTGEDVETRACNEQPCP 53
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
877-935 3.50e-12

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


Pssm-ID: 197639  Cd Length: 49  Bit Score: 62.40  E-value: 3.50e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034661056   877 TNQTCILWDETDvpsssappqlGPWSWRGCRTVPLDALRTRCLCDRLSTFAILAQLSAD 935
Cdd:smart00303    1 FNPICVFWDESS----------GEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
359-407 7.08e-12

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 61.83  E-value: 7.08e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1034661056   359 EWSPWSVCSSTCGEGWQTRTRFCVSSSYS---TQCSGPLREQRLCNNSAvCP 407
Cdd:smart00209    3 EWSEWSPCSVTCGGGVQTRTRSCCSPPPQnggGPCTGEDVETRACNEQP-CP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
414-461 2.80e-11

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 59.74  E-value: 2.80e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1034661056  414 EWSPWSLCSSTCGRGFRDRTRTCRPPQFGGNPCEGPEKQTKFCNIALC 461
Cdd:pfam00090    2 PWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49
HormR smart00008
Domain present in hormone receptors;
574-640 9.31e-11

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 59.07  E-value: 9.31e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034661056   574 PHEICDEDNFGAVIWKETPAGEVAAVRCPRNATGL-----ILRRCELDEegiaYWEP--PTYIRCVSIDYRNIQ 640
Cdd:smart00008    1 TDLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGFsyktgASRNCTENG----GWSPpfPNYSNCTSNDYEELK 70
TSP_1 pfam00090
Thrombospondin type 1 domain;
525-571 4.12e-10

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 56.66  E-value: 4.12e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1034661056  525 WASWGSCSVTCGAGSQRRERVCSGPFFGGAACQGPQDEYRQCGTQRC 571
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
880-929 1.17e-09

GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for auto-proteolysis, so is thus named, GPS. The GPS motif is a conserved sequence of ~40 amino acids containing canonical cysteine and tryptophan residues, and is the most highly conserved part of the domain. In most, if not all, cell-adhesion GPCRs these undergo autoproteolysis in the GPS between a conserved aliphatic residue (usually a leucine) and a threonine, serine, or cysteine residue. In higher eukaryotes this motif is found embedded in the C-terminal beta-stranded part of a GAIN domain - GPCR-Autoproteolysis INducing (GAIN). The GAIN-GPS domain adopts a fold in which the GPS motif, at the C-terminus, forms five beta-strands that are tightly integrated into the overall GAIN domain. The GPS motif, evolutionarily conserved from tetrahymena to mammals, is the only extracellular domain shared by all human cell-adhesion GPCRs and PKD proteins, and is the locus of multiple human disease mutations. The GAIN-GPS domain is both necessary and sufficient functionally for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyze peptide bond hydrolysis. In the cell-adhesion GPCRs and PKD proteins, the GPS motif is always located at the end of their long N-terminal extracellular regions, immediately before the first transmembrane helix of the respective protein.


Pssm-ID: 460350  Cd Length: 44  Bit Score: 55.01  E-value: 1.17e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034661056  880 TCILWDETDvpsssapPQLGPWSWRGCRTVPLDALRTRCLCDRLSTFAIL 929
Cdd:pfam01825    2 QCVFWDFTN-------STTGRWSTEGCTTVSLNDTHTVCSCNHLTSFAVL 44
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
264-314 2.73e-08

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 51.43  E-value: 2.73e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1034661056   264 WKLWSLWGECTRDCGGGLQTRTRTC-LPAPGVEGGGCEGVLEEGRQCNREAC 314
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
359-401 6.63e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 50.49  E-value: 6.63e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1034661056  359 EWSPWSVCSSTCGEGWQTRTRFCVS-SSYSTQCSGPLREQRLCN 401
Cdd:pfam00090    2 PWSPWSPCSVTCGKGIQVRQRTCKSpFPGGEPCTGDDIETQACK 45
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
575-634 9.64e-07

Hormone receptor domain; This extracellular domain contains four conserved cysteines that probably for disulphide bridges. The domain is found in a variety of hormone receptors. It may be a ligand binding domain.


Pssm-ID: 397086  Cd Length: 64  Bit Score: 47.36  E-value: 9.64e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034661056  575 HEICDEDNFGAVIWKETPAGEVAAVRCPR-----NATGLILRRCelDEEGiaYWE---PPTYIRCVSI 634
Cdd:pfam02793    1 GLGCPRTWDGILCWPRTPAGETVEVPCPDyfsgfDPRGNASRNC--TEDG--TWSehpPSNYSNCTSN 64
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
267-287 5.21e-04

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 39.57  E-value: 5.21e-04
                           10        20
                   ....*....|....*....|.
gi 1034661056  267 WSLWGECTRDCGGGLQTRTRT 287
Cdd:pfam19028    6 WSEWSECSVTCGGGVQTRTRT 26
 
Name Accession Description Interval E-value
7tmB2_BAI_Adhesion_VII cd15251
brain-specific angiogenesis inhibitors, group VII adhesion GPCRs, member of the class B2 ...
941-1231 1.55e-157

brain-specific angiogenesis inhibitors, group VII adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediate direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320379  Cd Length: 253  Bit Score: 479.44  E-value: 1.55e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  941 ATLPSVTLIVGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFL 1020
Cdd:cd15251      1 AGSPSVTLIVGCGVSCLALLTLLAIYAAFWRYIRSERSIILINFCLSIISSNILILVGQTQTLNKGVCTMTAAFLHFFFL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1021 SSFCWVLTEAWQSYMAVTGHLRNRLIRKRFLCLGWGLPALVVAISVGFTKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVV 1100
Cdd:cd15251     81 SSFCWVLTEAWQSYMAVTGRMRTRLIRKRFLCLGWGLPALVVAVSVGFTRTKGYGTSSYCWLSLEGGLLYAFVGPAAAVV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1101 LVNMVIGILVFNKLVSKDGITDkklkeragqpsphplgralkcaecgvlsaadatsdatsNAMASLWSSCVVLPLLALTW 1180
Cdd:cd15251    161 LVNMVIGILVFNKLVSRDGISD--------------------------------------NAMASLWSSCVVLPLLALTW 202
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034661056 1181 MSAVLAVTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVKCRVVD 1231
Cdd:cd15251    203 MSAVLAMTDRRSVLFQILFAVFDSLQGFVIVMVHCILRREVQDAVKCRMGV 253
7tmB2_BAI1 cd15990
brain-specific angiogenesis inhibitor 1, a group VII adhesion GPCR, member of the class B2 ...
938-1237 4.18e-154

brain-specific angiogenesis inhibitor 1, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320656  Cd Length: 267  Bit Score: 470.63  E-value: 4.18e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  938 MEKATLPSVTLIVGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHF 1017
Cdd:cd15990      1 MEKALLPSVTLIVGCGVSSLTLLLLIIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1018 FFLSSFCWVLTEAWQSYMAVTGHLRNRLIRKRFLCLGWGLPALVVAISVGFTKAKGYSTMNYCWLSLEGGLLYAFVGPAA 1097
Cdd:cd15990     81 FFLSSFCWVLTEAWQSYMAVTGRLRNRIIRKRFLCLGWGLPALVVAISVGFTKAKGYGTVNYCWLSLEGGLLYAFVGPAA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1098 AVVLVNMVIGILVFNKLVSKDGITDKKLKERAGqpsphplgralkcaecgvlsaadatsdatsnamASLWSSCVVLPLLA 1177
Cdd:cd15990    161 AVVLVNMVIGILVFNKLVSKDGITDKKLKERAG---------------------------------ASLWSSCVVLPLLA 207
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1178 LTWMSAVLAVTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVKCRVVDRQEEGN 1237
Cdd:cd15990    208 LTWMSAVLAITDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVKCRVVDRQEEGN 267
7tmB2_BAI2 cd15988
brain-specific angiogenesis inhibitor 2, a group VII adhesion GPCR, member of the class B2 ...
941-1229 7.84e-147

brain-specific angiogenesis inhibitor 2, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320654 [Multi-domain]  Cd Length: 291  Bit Score: 452.10  E-value: 7.84e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  941 ATLPSVTLIVGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFL 1020
Cdd:cd15988      1 TGSPSVPLMIGCAVSCMALLILLAIYAAFWRFIRSERSIILLNFCLSILASNILILVGQSQTLSKGVCTMTAAFLHFFFL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1021 SSFCWVLTEAWQSYMAVTGHLRNRLIRKRFLCLGWGLPALVVAISVGFTKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVV 1100
Cdd:cd15988     81 SSFCWVLTEAWQSYLAVIGRMRTRLVRKRFLCLGWGLPALVVAVSVGFTRTKGYGTASYCWLSLEGGLLYAFVGPAAVIV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1101 LVNMVIGILVFNKLVSKDGITDKKLKERAGQPSPHPLGRALKCAECGVLSAADATSDATSNAMASLWSSCVVLPLLALTW 1180
Cdd:cd15988    161 LVNMLIGIIVFNKLMSRDGISDKSKKQRAGSEAEPCSSLLLKCSKCGVVSSAAMSSATASSAMASLWSSCVVLPLLALTW 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1034661056 1181 MSAVLAVTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVKCRV 1229
Cdd:cd15988    241 MSAVLAMTDRRSILFQVLFAVFNSVQGFVIITVHCFLRREVQDVVKCQM 289
7tmB2_BAI3 cd15989
brain-specific angiogenesis inhibitor 3, a group VII adhesion GPCR, member of the class B2 ...
939-1229 6.83e-139

brain-specific angiogenesis inhibitor 3, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320655 [Multi-domain]  Cd Length: 293  Bit Score: 430.65  E-value: 6.83e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  939 EKATLPSVTLIVGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFF 1018
Cdd:cd15989      1 ESSGTPSVTLIVGCGLSCLALITLAVVYAALWRYIRSERSIILINFCLSIISSNILILVGQTQTHNKGICTMTTAFLHFF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1019 FLSSFCWVLTEAWQSYMAVTGHLRNRLIRKRFLCLGWGLPALVVAISVGFTKAKGYSTMNYCWLSLEGGLLYAFVGPAAA 1098
Cdd:cd15989     81 FLASFCWVLTEAWQSYMAVTGKIRTRLIRKRFLCLGWGLPALVVAISMGFTKAKGYGTPHYCWLSLEGGLLYAFVGPAAA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1099 VVLVNMVIGILVFNKLVSKDGITDKKLKERAGQPSPHPLGRALKCAECGVLSAADATSDATSNAMASLWSSCVVLPLLAL 1178
Cdd:cd15989    161 VVLVNMVIGILVFNKLVSRDGILDKKLKHRAGQMSEPHSGLTLKCAKCGVVSTTALSATTASNAMASLWSSCVVLPLLAL 240
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034661056 1179 TWMSAVLAVTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVKCRV 1229
Cdd:cd15989    241 TWMSAVLAMTDKRSILFQILFAVFDSLQGFVIVMVHCILRREVQDAFRCRL 291
AGRB_N pfam19188
Adhesion GPCR B N-terminal region; This region is found at the N-terminus of various adhesion ...
41-216 1.69e-92

Adhesion GPCR B N-terminal region; This region is found at the N-terminus of various adhesion G-protein coupled receptor B proteins. This region contains 10 cysteine residues that probably form disulphide bonds.


Pssm-ID: 465991  Cd Length: 177  Bit Score: 296.70  E-value: 1.69e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056   41 EPCATLVQGKFFGYFSAAAVFPANASRCSWTLRNPDPRRYTLYMKVAKAPVPCSgPGRVRTYQFDSFLES-TRTYLGVES 119
Cdd:pfam19188    1 DPCSTLVQGVLYGSFSLRDLFPTNASGCSWTLENPDPTKYTLYLKFTKPTQSCL-PFSPRLLQFDHYLENtTRTYLGRES 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  120 FDEVLRLCDPSAPLAFLQASKQFLQMRRQQPPQHDglrPRAGPPGPTDDFSVEYLVVGNRNPSRAACQMLCRWLDACLAG 199
Cdd:pfam19188   80 FDEVVELCDASSPFSFLEFDKNFVQLCLLAEPRGD---PESVVPGPSGDFKVEVLVINNENPSQFTCGVLCRWLEECLSA 156
                          170
                   ....*....|....*..
gi 1034661056  200 SRSSHPCGIMQTPCACL 216
Cdd:pfam19188  157 STSSRPCGIMQTPCICP 173
7tm_2 pfam00002
7 transmembrane receptor (Secretin family); This family is known as Family B, the ...
941-1210 5.52e-70

7 transmembrane receptor (Secretin family); This family is known as Family B, the secretin-receptor family or family 2 of the G-protein-coupled receptors (GCPRs). They have been described in many animal species, but not in plants, fungi or prokaryotes. Three distinct sub-families are recognized. Subfamily B1 contains classical hormone receptors, such as receptors for secretin and glucagon, that are all involved in cAMP-mediated signalling pathways. Subfamily B2 contains receptors with long extracellular N-termini, such as the leukocyte cell-surface antigen CD97; calcium-independent receptors for latrotoxin, and brain-specific angiogenesis inhibitors amongst others. Subfamily B3 includes Methuselah and other Drosophila proteins. Other than the typical seven-transmembrane region, characteriztic structural features include an amino-terminal extracellular domain involved in ligand binding, and an intracellular loop (IC3) required for specific G-protein coupling.


Pssm-ID: 459625 [Multi-domain]  Cd Length: 248  Bit Score: 235.25  E-value: 5.52e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  941 ATLPSVTLIVGCGVSSLTLLMLVIIYVSVwRYIRSERSVILINFCLSIISSNALILIGQTQTRNK--------VVCTLVA 1012
Cdd:pfam00002    1 ALSLKVIYTVGYSLSLVALLLAIAIFLLF-RKLHCTRNYIHLNLFASFILRALLFLVGDAVLFNKqdldhcswVGCKVVA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1013 AFLHFFFLSSFCWVLTEAWQSYMA-VTGHLRNRLIRKRFLCLGWGLPALVVAISVGFTkAKGYSTMNYCWLSLEGGLLYA 1091
Cdd:pfam00002   80 VFLHYFFLANFFWMLVEGLYLYTLlVEVFFSERKYFWWYLLIGWGVPALVVGIWAGVD-PKGYGEDDGCWLSNENGLWWI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1092 FVGPAAAVVLVNMVIGILVFNKLVSKDGITDKKLKERAgqpsphplgralkcaecgvlsaadatsdatsNAMASLWSSCV 1171
Cdd:pfam00002  159 IRGPILLIILVNFIIFINIVRILVQKLRETNMGKSDLK-------------------------------QYRRLAKSTLL 207
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1034661056 1172 VLPLLALTWMSAVLAVTDRR--SALFQILFAVFDSLEGFVI 1210
Cdd:pfam00002  208 LLPLLGITWVFGLFAFNPENtlRVVFLYLFLILNSFQGFFV 248
7tmB2_Adhesion cd15040
adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G ...
945-1225 8.23e-70

adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G protein-coupled receptors; The B2 subfamily of class B GPCRs consists of cell-adhesion receptors with 33 members in humans and vertebrates. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing a variety of structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, linked to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320168 [Multi-domain]  Cd Length: 253  Bit Score: 235.16  E-value: 8.23e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  945 SVTLIVGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFC 1024
Cdd:cd15040      5 SIITYIGCGLSLLGLLLTIITYILFRKLRKRKPTKILLNLCLALLLANLLFLFGINSTDNPVLCTAVAALLHYFLLASFM 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1025 WVLTEAWQSYMAVTG--HLRNRLIRKRFLCLGWGLPALVVAISVGFTKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVVLV 1102
Cdd:cd15040     85 WMLVEALLLYLRLVKvfGTYPRHFILKYALIGWGLPLIIVIITLAVDPDSYGNSSGYCWLSNGNGLYYAFLGPVLLIILV 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1103 NMVIGILVFNKLVSKDGITDKKLKeragqpsphplgralkcaecgvlsaadatsdatSNAMASLWSSCVVLPLLALTWMS 1182
Cdd:cd15040    165 NLVIFVLVLRKLLRLSAKRNKKKR---------------------------------KKTKAQLRAAVSLFFLLGLTWIF 211
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1034661056 1183 AVLAVTDRRSAlFQILFAVFDSLEGFVIVMVHCILRREVQDAV 1225
Cdd:cd15040    212 GILAIFGARVV-FQYLFAIFNSLQGFFIFIFHCLRNKEVRKAW 253
GAIN pfam16489
GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and ...
658-856 2.84e-52

GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and beta-strands that is found in cell-adhesion GPCRs and precedes the GPS motif where the autoproteolysis occurs, family, pfam01825. The full GAIN domain, comprises the GPS and the GAIN, in cell-adhesion GPCRs, and is the functional unit for autoproteolysis. The GPS motif at the end of the GAIN domain is an ancient domain that exists in primitive ancestor organizms, and the full GAIN + GPS is conserved in all cell-adhesion GPCRs and all PKD1-related proteins.


Pssm-ID: 465137  Cd Length: 205  Bit Score: 182.85  E-value: 2.84e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  658 GVSEVIQTLVEISQDGTSYSGDLLSTIDVLRNMTEIFRRAYYSPTPGDVQNFVQILSNLLAEENRDKWEEAQLAGPNAKE 737
Cdd:pfam16489    1 GAKELARELRNATRHGPLYGGDVLTAVELLSQLFDLLATQDATLSNAFLENFVQTVSNLLDPENRESWEDLQQTERGTAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  738 --LFRLVEDFVDVIGFRMKDLRDAYQVTDNLVLSIHKLPAS---GATDISFPMKGWRATGdwakvpEDRVTVSKSVFStg 812
Cdd:pfam16489   81 tkLLRTLEEYALLLAQNMKYLTPFTIVTPNIVLSVDRLDTHnfkGARFPRFPMKGERPKD------EDSVKLPPKAFK-- 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034661056  813 ltEADEASVFVVGTVLYRNLGSFLALQRN-----------TTVLNSKVISVTVKP 856
Cdd:pfam16489  153 --PPDSNGTVVVVFILYRNLGSLLPPSSRydpdrrslrlpRRVVNSPVVSASVHS 205
7tmB2_GPR133-like_Adhesion_V cd15933
orphan GPR133 and related proteins, group V adhesion GPCRs, member of class B2 family of ...
949-1224 8.95e-49

orphan GPR133 and related proteins, group V adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; group V adhesion GPCRs include orphan receptors GPR133, GPR144, and closely related proteins. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the G(s) protein, leading to activation of adenylate cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320599 [Multi-domain]  Cd Length: 252  Bit Score: 174.44  E-value: 8.95e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  949 IVGCGVSSLTLLMLVIIYVSVwRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCWVLT 1028
Cdd:cd15933      9 YIGCGISIACLALTLIIFLVL-RVLSSDRFQIHKNLCVALLLAQILLLAGEWAEGNKVACKVVAILLHFFFMAAFSWMLV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1029 EAWQSYMAVTGHLRNRLIRKRFLCLGWGLPALVVAISVGFtKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVVLVNMVIGI 1108
Cdd:cd15933     88 EGLHLYLMIVKVFNYKSKMRYYYFIGWGLPAIIVAISLAI-LFDDYGSPNVCWLSLDDGLIWAFVGPVIFIITVNTVILI 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1109 LVFNKLVSKDGITDKKLKERAGQpsphplgraLKcaecgvlsaadatsdATSNAMAslwsscVVLPLLALTWMSAVLAVT 1188
Cdd:cd15933    167 LVVKITVSLSTNDAKKSQGTLAQ---------IK---------------STAKASV------VLLPILGLTWLFGVLVVN 216
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1034661056 1189 DRrSALFQILFAVFDSLEGFVIVMVHCILRREVQDA 1224
Cdd:cd15933    217 SQ-TIVFQYIFVILNSLQGLMIFLFHCVLNSEVRSA 251
7tm_classB cd13952
class B family of seven-transmembrane G protein-coupled receptors; The class B of ...
949-1225 4.50e-47

class B family of seven-transmembrane G protein-coupled receptors; The class B of seven-transmembrane GPCRs is classified into three major subfamilies: subfamily B1 (secretin-like receptor family), B2 (adhesion family), and B3 (Methuselah-like family). The class B receptors have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi or prokaryotes. The B1 subfamily comprises receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the subfamily B1 receptors preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The subfamily B2 consists of cell-adhesion receptors with 33 members in humans and vertebrates. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing a variety of structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, linked to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. Furthermore, the subfamily B3 includes Methuselah (Mth) protein, which was originally identified in Drosophila as a GPCR affecting stress resistance and aging, and its closely related proteins.


Pssm-ID: 410627 [Multi-domain]  Cd Length: 260  Bit Score: 170.09  E-value: 4.50e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  949 IVGCGVSSLTLLMLVIIYVSVWRYiRSERSVILINFCLSIISSNALILIGQTQTRNK--VVCTLVAAFLHFFFLSSFCWV 1026
Cdd:cd13952      9 YIGCSLSLVGLLLTIITYLLFPKL-RNLRGKILINLCLSLLLAQLLFLIGQLLTSSDrpVLCKALAILLHYFLLASFFWM 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1027 LTEAWQSYMAVTGHLRNRlIRKRFL---CLGWGLPALVVAISVGFTKAKGYSTM----NYCWLSLEGGLLYAFVGPAAAV 1099
Cdd:cd13952     88 LVEAFDLYRTFVKVFGSS-ERRRFLkysLYGWGLPLLIVIITAIVDFSLYGPSPgyggEYCWLSNGNALLWAFYGPVLLI 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1100 VLVNMVIGILVFNKLVSKDGITDKKLKeragqpsphplgralkcaecgvlsaadatsdaTSNAMASLWSSCVVLPLLALT 1179
Cdd:cd13952    167 LLVNLVFFILTVRILLRKLRETPKQSE--------------------------------RKSDRKQLRAYLKLFPLMGLT 214
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1034661056 1180 WMSAVLAVTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAV 1225
Cdd:cd13952    215 WIFGILAPFVGGSLVFWYLFDILNSLQGFFIFLIFCLKNKEVRRLL 260
7tmB2_latrophilin-like_invertebrate cd15440
invertebrate latrophilin-like receptors, member of the class B2 family of seven-transmembrane ...
950-1222 3.75e-35

invertebrate latrophilin-like receptors, member of the class B2 family of seven-transmembrane G protein-coupled receptors; This subgroup includes latrophilin-like proteins that are found in invertebrates such as insects and worms. Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of vertebrate latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320556 [Multi-domain]  Cd Length: 259  Bit Score: 135.47  E-value: 3.75e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  950 VGCGVSSLTLLMLVIIYVSVwRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCWVLTE 1029
Cdd:cd15440     10 IGCIISIVCLLLAFITFTCF-RNLQCDRNTIHKNLCLCLLIAEIVFLLGIDQTENRTLCGVIAGLLHYFFLAAFSWMLLE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1030 AWQSY-MAVTGHLRNRLIRKRFLCLGWGLPALVVAISVGFtKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVVLVNmvigi 1108
Cdd:cd15440     89 GFQLYvMLVEVFEPEKSRIKWYYLFGYGLPALIVAVSAGV-DPTGYGTEDHCWLSTENGFIWSFVGPVIVVLLAN----- 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1109 LVFnklvskdgitdkklkeragqpsphpLGRALkCAECGVLSAADATSDATSNAMASLW--SSCVVLPLLALTWMSAVLA 1186
Cdd:cd15440    163 LVF-------------------------LGMAI-YVMCRHSSRSASKKDASKLKNIRGWlkGSIVLVVLLGLTWTFGLLF 216
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1034661056 1187 VtDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQ 1222
Cdd:cd15440    217 I-NQESIVMAYIFTILNSLQGLFIFIFHCVLNEKVR 251
7tmB2_CD97 cd15438
CD97 antigen, member of the class B2 family of seven-transmembrane G protein-coupled receptors; ...
946-1223 7.88e-35

CD97 antigen, member of the class B2 family of seven-transmembrane G protein-coupled receptors; group II adhesion GPCRs, including the leukocyte cell-surface antigen CD97 and the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4), are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily B2 of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying numbers of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of CD97, alternative splicing results in three isoforms possessing either three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. For example, CD97, which is involved in angiogenesis and the migration and invasion of tumor cells, has been shown to promote cell aggregation in a GPS proteolysis-dependent manner. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment.


Pssm-ID: 320554 [Multi-domain]  Cd Length: 261  Bit Score: 134.51  E-value: 7.88e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  946 VTLIVGCGVS-SLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFC 1024
Cdd:cd15438      4 LTLITKVGLSvSLFCLFLCILTFLFCRSIRGTRNTIHLHLCLSLFLAHLIFLLGINNTNNQVACAVVAGLLHYFFLAAFC 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1025 WVLTEAWQSYMAVTGHLRNRLIRKRFLCL-GWGLPALVVAISVGfTKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVVLVN 1103
Cdd:cd15438     84 WMSLEGVELYLMVVQVFNTQSLKKRYLLLiGYGVPLVIVAISAA-VNSKGYGTQRHCWLSLERGFLWSFLGPVCLIILVN 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1104 MVIGIlvfnklvskdgITDKKLKERAGQPSPhplgralkcaECGVLSAADATsdaTSNAMASLwssCVvlplLALTWMSA 1183
Cdd:cd15438    163 AIIFV-----------ITVWKLAEKFSSINP----------DMEKLRKIRAL---TITAIAQL---CI----LGCTWIFG 211
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1034661056 1184 VLAVTDrRSALFQILFAVFDSLEGFVIVMVHCILRREVQD 1223
Cdd:cd15438    212 FFQFSD-STLVMSYLFTILNSLQGLFIFLLHCLLSKQVRE 250
7tmB2_CELSR_Adhesion_IV cd15441
cadherin EGF LAG seven-pass G-type receptors, group IV adhesion GPCRs, member of the class B2 ...
943-1221 6.28e-34

cadherin EGF LAG seven-pass G-type receptors, group IV adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. Celsr3 is expressed in both the developing and adult mouse brain. It has been functionally implicated in proper neuron migration and axon guidance in the CNS.


Pssm-ID: 320557 [Multi-domain]  Cd Length: 254  Bit Score: 131.99  E-value: 6.28e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  943 LPSVTLIVGCGVSsLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSS 1022
Cdd:cd15441      3 LLKIVTYIGIGIS-LVLLVIAFLVLSCLRGLQSNSNSIHKNLVACLLLAELLFLLGINQTENLFPCKLIAILLHYFYLSA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1023 FCWVLTEAWQSYMAVT-------GHLRnrlirkRFLCLGWGLPALVVAISVGFtKAKGYSTMNYCWLSLEGGLLYAFVGP 1095
Cdd:cd15441     82 FSWLLVESLHLYRMLTeprdinhGHMR------FYYLLGYGIPAIIVGLSVGL-RPDGYGNPDFCWLSVNETLIWSFAGP 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1096 AAAVVLVNMVIGILVFNKLVSKDGITDKKLKERAGqpsphplgralkcaecgvlsaadatsdatsnamasLWSSCVVLPL 1175
Cdd:cd15441    155 IAFVIVITLIIFILALRASCTLKRHVLEKASVRTD-----------------------------------LRSSFLLLPL 199
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1034661056 1176 LALTWMSAVLAVTDrRSALFQILFAVFDSLEGFVIVMVHCILRREV 1221
Cdd:cd15441    200 LGATWVFGLLAVNE-DSELLHYLFAGLNFLQGLFIFLFYCIFNKKV 244
7tmB2_EMR cd15439
epidermal growth factor-like module-containing mucin-like hormone receptors, member of the ...
944-1226 1.96e-32

epidermal growth factor-like module-containing mucin-like hormone receptors, member of the class B2 family of seven-transmembrane G protein-coupled receptors; group II adhesion GPCRs, including the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4) and the leukocyte cell-surface antigen CD97, are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying number of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of EMR2, alternative splicing results in four isoforms possessing either two (EGF1,2), three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment.


Pssm-ID: 320555 [Multi-domain]  Cd Length: 263  Bit Score: 127.84  E-value: 1.96e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  944 PSVTLIVGCGVS-SLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSS 1022
Cdd:cd15439      2 LALTVITYVGLIiSLLCLFLAILTFLLCRSIRNTSTSLHLQLSLCLFLADLLFLVGIDRTDNKVLCSIIAGFLHYLFLAC 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1023 FCWVLTEAWQSYMAV-----TGHLRNRLIRKRFLCL-GWGLPALVVAISVGfTKAKGYSTMNYCWLSLEGGLLYAFVGPA 1096
Cdd:cd15439     82 FAWMFLEAVHLFLTVrnlkvVNYFSSHRFKKRFMYPvGYGLPAVIVAISAA-VNPQGYGTPKHCWLSMEKGFIWSFLGPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1097 AAVVLVNMVIGILVF----NKLVSKDgitdkklKEragqpsphplgralkcaecgvLSAADATSDATSNAMASLWsscvv 1172
Cdd:cd15439    161 CVIIVINLVLFCLTLwilrEKLSSLN-------AE---------------------VSTLKNTRLLTFKAIAQLF----- 207
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034661056 1173 lpLLALTWMSAVLAVTDRRSALfQILFAVFDSLEGFVIVMVHCILRREVQDAVK 1226
Cdd:cd15439    208 --ILGCTWILGLFQVGPVATVM-AYLFTITNSLQGVFIFLVHCLLNRQVREEYR 258
7tmB2_Latrophilin_Adhesion_I cd15252
Latrophilins and similar receptors, group I adhesion GPCRs, member of class B2 family of ...
950-1222 1.58e-30

Latrophilins and similar receptors, group I adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; Group I adhesion GPCRs consist of latrophilins (also called lectomedins or latrotoxin receptors) and ETL (EGF-TM7-latrophilin-related protein. These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320380 [Multi-domain]  Cd Length: 257  Bit Score: 122.23  E-value: 1.58e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  950 VGCgVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCWVLTE 1029
Cdd:cd15252     10 VGI-IISLVCLAICIFTFWFFRGLQSDRTTIHKNLCISLFLAELVFLIGINTTTNKIFCSVIAGLLHYFFLAAFAWMFIE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1030 AWQSYMAVTGHLRNR-LIRKRFLCLGWGLPALVVAISVGFtKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVVLVNMV-IG 1107
Cdd:cd15252     89 GIQLYLMLVEVFENEgSRHKNFYIFGYGSPAVIVGVSAAL-GYRYYGTTKVCWLSTENYFIWSFIGPATLIILLNLIfLG 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1108 ILVFnklvskdgitdKKLKERAGQPSPHplgralKCAEcgvlsaadatsdatsNAMASLWSSCVVLPLLALTWMSAVLAV 1187
Cdd:cd15252    168 VAIY-----------KMFRHTAGLKPEV------SCLE---------------NIRSWARGAIALLFLLGLTWIFGVLHI 215
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1034661056 1188 tDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQ 1222
Cdd:cd15252    216 -NHASVVMAYLFTVSNSLQGMFIFLFHCVLSRKVR 249
7tmB2_GPR133 cd15256
orphan adhesion receptor GPR133, member of the class B2 family of seven-transmembrane G ...
940-1226 1.43e-28

orphan adhesion receptor GPR133, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR133 is an orphan receptor that belongs to the group V adhesion-GPCRs together with GPR144. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the Gs protein, leading to activation of adenylyl cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320384 [Multi-domain]  Cd Length: 260  Bit Score: 116.56  E-value: 1.43e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  940 KATLPSVTLIvGCGVSSLTLLMLVIIY--VSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHF 1017
Cdd:cd15256      1 QVALSSITYV-GCSLSIFCLAITLVTFavLSSVSTIRNQRYHIHANLSFAVLVAQILLLISFRFEPGTLPCKIMAILLHF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1018 FFLSSFCWVLTEAWQSYMAVTGHLRNRLIRKRFLC-LGWGLPALVVAISVGFTkAKGYSTMNYCWLSLEGGLLYAFVGPA 1096
Cdd:cd15256     80 FFLSAFAWMLVEGLHLYSMVIKVFGSEESKHFYYYgIGWGSPLLICIISLTSA-LDSYGESDNCWLSLENGAIWAFVAPA 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1097 AAVVLVNmvIGILV-FNKLVSKDGITDKKLKeraGQPSPHPLgralkcaecgvlsaadatsdaTSNAMAslwsscVVLPL 1175
Cdd:cd15256    159 LFVIVVN--IGILIaVTRVISRISADNYKVH---GDANAFKL---------------------TAKAVA------VLLPI 206
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034661056 1176 LALTWMSAVLAVtDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVK 1226
Cdd:cd15256    207 LGSSWVFGVLAV-NTHALVFQYMFAIFNSLQGFFIFLFHCLLNSEVRAAFK 256
7tmB2_CELSR1 cd15991
Cadherin EGF LAG seven-pass G-type receptor 1, member of the class B2 family of ...
956-1226 8.88e-28

Cadherin EGF LAG seven-pass G-type receptor 1, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320657 [Multi-domain]  Cd Length: 254  Bit Score: 114.17  E-value: 8.88e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  956 SLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCWVLTEAWQSYM 1035
Cdd:cd15991     15 SLVALLITFILLVLIRTLRSNLHSIHKNLVAALFFSELIFLIGINQTENPFVCTVVAILLHYFYMSTFAWMFVEGLHIYR 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1036 AVT-------GHLRnrlirkRFLCLGWGLPALVVAISVGFtKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVVLVNMVIGI 1108
Cdd:cd15991     95 MLTevrnintGHMR------FYYVVGWGIPAIITGLAVGL-DPQGYGNPDFCWLSVQDTLIWSFAGPIGIVVIINTVIFV 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1109 LvfnklvskdgitdkklkeragqpsphplgrALKcAECGvlsaADATSDATSNAMASLWSSCVVLPLLALTWMSAVLAV- 1187
Cdd:cd15991    168 L------------------------------AAK-ASCG----RRQRYFEKSGVISMLRTAFLLLLLISATWLLGLMAVn 212
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1034661056 1188 TDRRSalFQILFAVFDSLEGFVIVMVHCILRREVQDAVK 1226
Cdd:cd15991    213 SDTLS--FHYLFAIFSCLQGIFIFFFHCIFNKEVRKHLK 249
7tmB2_EMR_Adhesion_II cd15931
EGF-like module receptors, group II adhesion GPCRs, member of class B2 family of ...
944-1226 1.63e-26

EGF-like module receptors, group II adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; group II adhesion GPCRs, including the leukocyte cell-surface antigen CD97 and the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4), are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily B2 of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying numbers of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of CD97, alternative splicing results in three isoforms possessing either three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. On the other hand, EMR2 generates four isoforms possessing either two (EGF1,2), three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. For example, CD97, which is involved in angiogenesis and the migration and invasion of tumor cells, has been shown to promote cell aggregation in a GPS proteolysis-dependent manner. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment.


Pssm-ID: 320597 [Multi-domain]  Cd Length: 262  Bit Score: 110.68  E-value: 1.63e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  944 PSVTLIVGCGVS-SLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSS 1022
Cdd:cd15931      2 PFLEWINRVGVIvSLFCLGLAIFTFLLCRWIPKINTTAHLHLCLCLSMSHTLFLAGIEYVENELACTVMAGLLHYLFLAS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1023 FCWVLTEAWQSYMAV-----TGHLRNRLIRKRFLCL-GWGLPALVVAISvGFTKAKGYSTMNYCWLSLEGGLLYAFVGPA 1096
Cdd:cd15931     82 FVWMLLEALQLHLLVrrltkVQVIQRDGLPRPLLCLiGYGVPFLIVGVS-ALVYSDGYGEAKMCWLSQERGFNWSFLGPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1097 AAVVLVNMVIGILVFNKLVSKdgitdkklkeragqpsphplgralkcaecgvLSAADATSDATSNAMASLWSSCVVLPLL 1176
Cdd:cd15931    161 IAIIGINWILFCATLWCLRQT-------------------------------LSNMNSDISQLKDTRLLTFKAVAQLFIL 209
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1177 ALTWMSAvLAVTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVK 1226
Cdd:cd15931    210 GCTWVLG-LFQTNPVALVFQYLFTILNSLQGAFLFLVHCLLNKEVREEYI 258
7tmB2_GPR116-like_Adhesion_VI cd15932
orphan GPR116 and related proteins, group IV adhesion GPCRs, member of the class B2 family of ...
944-1226 6.20e-25

orphan GPR116 and related proteins, group IV adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; group VI adhesion GPCRs consist of orphan receptors GPR110, GPR111, GPR113, GPR115, GPR116, and closely related proteins. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. GPR110 possesses a SEA box in the N-terminal has been identified as an oncogene over-expressed in lung and prostate cancer. GPR113 contains a hormone binding domain and one EGF (epidermal grown factor) domain. GPR112 has extremely long N-terminus (about 2,400 amino acids) containing a number of Ser/Thr-rich glycosylation sites and a pentraxin (PTX) domain. GPR116 has two C2-set immunoglobulin-like repeats, which is found in the members of the immunoglobulin superfamily of cell surface proteins, and a SEA (sea urchin sperm protein, enterokinase, and a grin)-box, which is present in the extracellular domain of the transmembrane mucin (MUC) family and known to enhance O-glycosylation. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320598 [Multi-domain]  Cd Length: 268  Bit Score: 106.24  E-value: 6.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  944 PSVTLI--VGCGVSSLTLLMLVIIYVSVWRYI-RSE----RSVILINFCLSIISSNALILIG---QTQTRNKVVCTLVAA 1013
Cdd:cd15932      2 PALDYItyVGLGISILSLVLCLIIEALVWKSVtKNKtsymRHVCLVNIALSLLIADIWFIIGaaiSTPPNPSPACTAATF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1014 FLHFFFLSSFCWVLTEA---WQSYMAVTGHLRNRLIRKRFLCLGWGLPALVVAISVGFTK-AKGYSTMNYCWLSL-EGGL 1088
Cdd:cd15932     82 FIHFFYLALFFWMLTLGlllFYRLVLVFHDMSKSTMMAIAFSLGYGCPLIIAIITVAATApQGGYTRKGVCWLNWdKTKA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1089 LYAFVGPAAAVVLVNMVIGILVFNKLVSKdgitdkklkeragqpsphplgralkcaecgvlSAADATSDATSNAMASLWS 1168
Cdd:cd15932    162 LLAFVIPALAIVVVNFIILIVVIFKLLRP--------------------------------SVGERPSKDEKNALVQIGK 209
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034661056 1169 SCVVL-PLLALTWMSAVLAVTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVK 1226
Cdd:cd15932    210 SVAILtPLLGLTWGFGLGTMIDPKSLAFHIIFAILNSFQGFFILVFGTLLDSKVREALL 268
7tmB2_ETL cd15437
Epidermal Growth Factor, latrophilin and seven transmembrane domain-containing protein 1; ...
954-1223 1.36e-23

Epidermal Growth Factor, latrophilin and seven transmembrane domain-containing protein 1; member of the class B2 family of seven-transmembrane G protein-coupled receptors; ETL (EGF-TM7-latrophilin-related protein) belongs to Group I adhesion GPCRs, which also include latrophilins (also called lectomedins or latrotoxin receptors). All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. ETL, for instance, contains EGF-like repeats, which also present in other EGF-TM7 adhesion GPCRs, such as Cadherin EGF LAG seven-pass G-type receptors (CELSR1-3), EGF-like module receptors (EMR1-3), CD97, and Flamingo. ETL is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320553 [Multi-domain]  Cd Length: 258  Bit Score: 101.88  E-value: 1.36e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  954 VSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCWVLTEAWQS 1033
Cdd:cd15437     13 IISLICLSMCIFTFWFFSEIQSTRTTIHKNLCCSLFLAELIFLIGINMNANKLFCSIIAGLLHYFFLAAFAWMCIEGIHL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1034 YMAVTGHLRNR-LIRKRFLCLGWGLPALVVAIS--VGFtkaKGYSTMNYCWLSLEGGLLYAFVGPAAAVVLVN-MVIGIL 1109
Cdd:cd15437     93 YLIVVGVIYNKgFLHKNFYIFGYGSPAVVVGISaaLGY---KYYGTTKVCWLSTENNFIWSFIGPACLIILVNlLAFGVI 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1110 VFnklvskdgitdKKLKERAGqpsphpLGRALKCAEcGVLSAAdatsdatSNAMASLWsscvvlpLLALTWMSAVLAVTd 1189
Cdd:cd15437    170 IY-----------KVFRHTAM------LKPEVSCYE-NIRSCA-------RGALALLF-------LLGATWIFGVLHVV- 216
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1034661056 1190 RRSALFQILFAVFDSLEGFVIVMVHCILRREVQD 1223
Cdd:cd15437    217 YGSVVTAYLFTISNAFQGMFIFIFLCVLSRKIQE 250
7tmB2_GPR144 cd15255
orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G ...
941-1226 1.52e-23

orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR144 is an orphan receptor that belongs to the group V adhesion-GPCRs together with GPR133. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the Gs protein, leading to activation of adenylyl cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320383 [Multi-domain]  Cd Length: 263  Bit Score: 101.85  E-value: 1.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  941 ATLPSVTLIvGCGVSSLTLLMLVIIYVSVwRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFL 1020
Cdd:cd15255      2 ATLRTLSFI-GCGVSLCALIVTFILFLAV-GVPKSERTTVHKNLIFALAAAEFLLMFSEWAKGNQVACWAVTALLHLFFL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1021 SSFCWVLTEA---WQSYMAVTGHLRNRLirKRFLCLGWGLPALVVAISVGFTKAKgYSTMNYCWLSLEGGLLYAFVGPAA 1097
Cdd:cd15255     80 AAFSWMLVEGlllWSKVVAVNMSEDRRM--KFYYVTGWGLPVVIVAVTLATSFNK-YVADQHCWLNVQTDIIWAFVGPVL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1098 AVVLVNMVIGILVFNKLVSkdgitdkKLKERAGQPSPHPlgralkCAECGVLSAADATSDATsnamaslwssCVVLPLLA 1177
Cdd:cd15255    157 FVLTVNTFVLFRVVMVTVS-------SARRRAKMLTPSS------DLEKQIGIQIWATAKPV----------LVLLPVLG 213
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1034661056 1178 LTWMSAVLAvtdRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVK 1226
Cdd:cd15255    214 LTWLCGVLV---HLSDVWAYVFITLNSFQGLYIFLVYAIYNSEVRNAIQ 259
7tmB2_Latrophilin cd15436
Latrophilins, member of the class B2 family of seven-transmembrane G protein-coupled receptors; ...
946-1227 6.80e-23

Latrophilins, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320552 [Multi-domain]  Cd Length: 258  Bit Score: 99.87  E-value: 6.80e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  946 VTLIVGCGVS-SLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFC 1024
Cdd:cd15436      4 LFVITWVGIViSLVCLLICIFTFCFFRGLQTDRNTIHKNLCINLFIAELLFLIGINRTQYTIACPIFAGLLHFFFLAAFC 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1025 WVLTEAWQSYMAVTGHLRNRLIRKRFLCL-GWGLPALVVAISVGFtKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVVLVN 1103
Cdd:cd15436     84 WLCLEGVQLYLLLVEVFESEYSRRKYFYLcGYSFPALVVAVSAAI-DYRSYGTEKACWLRVDNYFIWSFIGPVTFVITLN 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1104 MVIGILVFNKLVSKDGItdkkLKeragqpsphPLGRALkcaecgvlsaadatsdatSNAMASLWSSCVVLPLLALTWMSA 1183
Cdd:cd15436    163 LVFLVITLHKMVSHSDL----LK---------PDSSRL------------------DNIKSWALGAIALLFLLGLTWSFG 211
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1034661056 1184 VLAVtDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQ-DAVKC 1227
Cdd:cd15436    212 LMFI-NEESVVMAYLFTIFNAFQGVFIFIFHCALQKKVRkEYSKC 255
7tmB2_Latrophilin-3 cd16005
Latrophilin-3, member of the class B2 family of seven-transmembrane G protein-coupled ...
956-1222 8.71e-23

Latrophilin-3, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320671 [Multi-domain]  Cd Length: 258  Bit Score: 99.63  E-value: 8.71e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  956 SLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCWVLTEAWQSYM 1035
Cdd:cd16005     15 SLVCLLICIFTFCFFRGLQSDRNTIHKNLCISLFVAELLFLIGINRTDQPIACAVFAALLHFFFLAAFTWMFLEGVQLYI 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1036 AVTGHLRNRLIRKR-FLCLGWGLPALVVAISVGfTKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVVLVNMVIGILVFNKL 1114
Cdd:cd16005     95 MLVEVFESEHSRRKyFYLVGYGMPALIVAVSAA-VDYRSYGTDKVCWLRLDTYFIWSFIGPATLIIMLNVIFLGIALYKM 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1115 VSKDGItdkkLKERAGqpsphplgralkcaecgvlsaadatsdATSNAMASLWSSCVVLPLLALTWMSAVLAVTDrRSAL 1194
Cdd:cd16005    174 FHHTAI----LKPESG---------------------------CLDNIKSWVIGAIALLCLLGLTWAFGLMYINE-STVI 221
                          250       260
                   ....*....|....*....|....*...
gi 1034661056 1195 FQILFAVFDSLEGFVIVMVHCILRREVQ 1222
Cdd:cd16005    222 MAYLFTIFNSLQGMFIFIFHCVLQKKVR 249
7tmB2_Latrophilin-1 cd16007
Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled ...
943-1227 1.27e-22

Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320673 [Multi-domain]  Cd Length: 258  Bit Score: 99.23  E-value: 1.27e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  943 LPSVTLIVGCgVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSS 1022
Cdd:cd16007      3 LLSVITWVGI-VISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLIGIDKTQYQIACPIFAGLLHFFFLAA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1023 FCWVLTEAWQSYMAVTGHLRNRLIRKRFLCL-GWGLPALVVAISVGFtKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVVL 1101
Cdd:cd16007     82 FSWLCLEGVQLYLMLVEVFESEYSRKKYYYLcGYCFPALVVGISAAI-DYRSYGTEKACWLRVDNYFIWSFIGPVSFVIV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1102 VNMVIGILVFNKLVSKDgitdkklkeragqpsphplgralkcaecgvlSAADATSDATSNAMASLWSSCVVLPLLALTWM 1181
Cdd:cd16007    161 VNLVFLMVTLHKMIRSS-------------------------------SVLKPDSSRLDNIKSWALGAITLLFLLGLTWA 209
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1034661056 1182 SAVLAVtDRRSALFQILFAVFDSLEGFVIVMVHCILRREV-QDAVKC 1227
Cdd:cd16007    210 FGLLFI-NKESVVMAYLFTTFNAFQGMFIFIFHCALQKKVhKEYSKC 255
7tmB2_GPR113 cd15253
orphan adhesion receptor GPR113, member of the class B2 family of seven-transmembrane G ...
943-1229 4.48e-22

orphan adhesion receptor GPR113, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR113 is an orphan receptor that belongs to group VI adhesion-GPCRs along with GPR110, GPR111, GPR115, and GPR116. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. GPR113 contains a hormone binding domain and one EGF (epidermal grown factor) domain, and is primarily expressed in a subset of taste receptor cells. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320381 [Multi-domain]  Cd Length: 271  Bit Score: 97.91  E-value: 4.48e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  943 LPSVTLI--VGCGVSSLTLLMLVIIYVSVWR-YIRSE----RSVILINFCLSIISSNALILIGQ--TQTRNKVVCTLVAA 1013
Cdd:cd15253      1 SFWLDFLsqVGLGASILALLLCLGIYRLVWRsVVRNKisyfRHMTLVNIAFSLLLADTCFLGATflSAGHESPLCLAAAF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1014 FLHFFFLSSFCWVLTEA---WQSYMAVTGHLRNRLIRKRFLCLGWGLPALVVAISVG-FTKAKGYSTMNYCWLSLEGGLL 1089
Cdd:cd15253     81 LCHFFYLATFFWMLVQAlmlFHQLLFVFHQLAKRSVLPLMVTLGYLCPLLIAAATVAyYYPKRQYLHEGACWLNGESGAI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1090 YAFVGPAAAVVLVNMVIGILVFNKLVskdgitdkklkeragQPSPhplgralkcaecgvlsaADATSDATSNAMASLWSS 1169
Cdd:cd15253    161 YAFSIPVLAIVLVNLLVLFVVLMKLM---------------RPSV-----------------SEGPPPEERKALLSIFKA 208
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034661056 1170 CVVL-PLLALTWMSAVLAVTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVKCRV 1229
Cdd:cd15253    209 LLVLtPVFGLTWGLGVATLTGESSQVSHYGFAILNAFQGVFILLFGCLMDKKVREALLKRL 269
7tmB2_CELSR2 cd15992
Cadherin EGF LAG seven-pass G-type receptor 2, member of the class B2 family of ...
943-1226 4.60e-22

Cadherin EGF LAG seven-pass G-type receptor 2, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320658  Cd Length: 255  Bit Score: 97.58  E-value: 4.60e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  943 LPSVTLIVGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSS 1022
Cdd:cd15992      2 LPLKTLTWSSVGVTLGFLLLTFLFLLCLRALRSNKTSIRKNGATALFLSELVFILGINQADNPFACTVIAILLHFFYLCT 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1023 FCWVLTEAWQSYMAVTgHLR--NRLIRKRFLCLGWGLPALVVAISVGFtKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVV 1100
Cdd:cd15992     82 FSWLFLEGLHIYRMLS-EVRdiNYGPMRFYYLIGWGVPAFITGLAVGL-DPEGYGNPDFCWLSIYDTLIWSFAGPVAFAV 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1101 LVNMVIGILVFNKLVSkdgITDKKLKERAGQpsphplgralkcaecgvlsaadatsdatsnaMASLWSSCVVLPLLALTW 1180
Cdd:cd15992    160 SMNVFLYILSSRASCS---AQQQSFEKKKGP-------------------------------VSGLRTAFTVLLLVSVTC 205
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1034661056 1181 MSAVLAVtDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVK 1226
Cdd:cd15992    206 LLALLSV-NSDVILFHYLFAGFNCLQGPFIFLSHVVLLKEVRKALK 250
7tmB2_Latrophilin-2 cd16006
Latrophilin-2, member of the class B2 family of seven-transmembrane G protein-coupled ...
946-1222 5.01e-22

Latrophilin-2, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320672 [Multi-domain]  Cd Length: 258  Bit Score: 97.29  E-value: 5.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  946 VTLIVGCGVS-SLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFC 1024
Cdd:cd16006      4 LTVITWVGIViSLVCLAICIFTFCFFRGLQSDRNTIHKNLCINLFIAEFIFLIGIDKTEYKIACPIFAGLLHFFFLAAFA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1025 WVLTEAWQSYMAVTGHLRNRLIRKRFLCL-GWGLPALVVAISVGfTKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVVLVN 1103
Cdd:cd16006     84 WMCLEGVQLYLMLVEVFESEYSRKKYYYVaGYLFPATVVGVSAA-IDYKSYGTEKACWLRVDNYFIWSFIGPVTFIILLN 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1104 MVIGILVFNKLVsKDGITDKKLKERAGQPSPHPLGralkcaecgvlsaadatsdatsnamaslwsSCVVLPLLALTWMSA 1183
Cdd:cd16006    163 LIFLVITLCKMV-KHSNTLKPDSSRLENIKSWVLG------------------------------AFALLCLLGLTWSFG 211
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1034661056 1184 VLAVTDrRSALFQILFAVFDSLEGFVIVMVHCILRREVQ 1222
Cdd:cd16006    212 LLFINE-ETIVMAYLFTIFNAFQGMFIFIFHCALQKKVR 249
7tmB2_CELSR3 cd15993
Cadherin EGF LAG seven-pass G-type receptor 3, member of the class B2 family of ...
956-1226 2.83e-21

Cadherin EGF LAG seven-pass G-type receptor 3, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. Celsr3 is expressed in both the developing and adult mouse brain. It has been functionally implicated in proper neuronal migration and axon guidance in the CNS. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320659 [Multi-domain]  Cd Length: 254  Bit Score: 95.29  E-value: 2.83e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  956 SLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCWVLTEAWQSY- 1034
Cdd:cd15993     15 SLAALVLTFSVLTCLRGLKSNTRGIHSNIAAALFLSELLFLLGINRTENQFLCTVVAILLHYFFLSTFAWLFVQGLHIYr 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1035 MAVTGHLRNRLIRKRFLCLGWGLPALVVAISVGFtKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVVLVNMVIGILVFNKL 1114
Cdd:cd15993     95 MQTEARNVNFGAMRFYYAIGWGVPAIITGLAVGL-DPEGYGNPDFCWISIHDKLVWSFAGPIVVVIVMNGVMFLLVARMS 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1115 VSKDGITDKKLkeragqpsphplgralkcaecgvlsaadatsdatsNAMASLWSSCVVLPLLALTWMSAVLAVTDRRSAl 1194
Cdd:cd15993    174 CSPGQKETKKT-----------------------------------SVLMTLRSSFLLLLLISATWLFGLLAVNNSVLA- 217
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1034661056 1195 FQILFAVFDSLEGFVIVMVHCILRREVQDAVK 1226
Cdd:cd15993    218 FHYLHAILCCLQGLAVLLLFCVLNEEVQEAWK 249
7tmB2_GPR116_Ig-Hepta cd15254
The immunoglobulin-repeat-containing receptor Ig-hepta/GPR116, member of the class B2 family ...
950-1224 1.08e-17

The immunoglobulin-repeat-containing receptor Ig-hepta/GPR116, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR116 (also known as Ig-hepta) is an orphan receptor that belongs to group VI adhesion-GPCRs along with GPR110, GPR111, GPR113, and GPR115. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. GPR116 has four I-set immunoglobulin-like repeats, which is found in the members of the immunoglobulin superfamily of cell surface proteins, and a SEA (sea urchin sperm protein, enterokinase, and a grin)-box, which is present in the extracellular domain of the transmembrane mucin (MUC) family and known to enhance O-glycosylation. GPR116 is highly expressed in fetal and adult lung, and it has been shown to regulate lung surfactant levels as well as to stimulate breast cancer metastasis through a G(q)-p63-RhoGEF-Rho GTPase signaling pathway. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320382 [Multi-domain]  Cd Length: 275  Bit Score: 85.24  E-value: 1.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  950 VGCGVSSLTLLMLVIIYVSVWRYIRSERS-----VILINFCLSIISSNA-LILIGQTQTRNKVVC-TLVAAFLHFFFLSS 1022
Cdd:cd15254     10 IGLSISILSLAICIVIESLVWKSVTKNRTsymrhVCILNIAVSLLIADIwFIVVAAIQDQNYAVNgNVCVAATFFIHFFY 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1023 FC---WVLTEAWQSY--MAVTGHLRNRLIRKRF-LCLGWGLPALVVAISVGFTKAK-GYSTMNYCWLSLEGG-LLYAFVG 1094
Cdd:cd15254     90 LCvffWMLALGLMLFyrLVFILHDTSKTIQKAVaFCLGYGCPLIISVITIAVTLPRdSYTRKKVCWLNWEDSkALLAFVI 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1095 PAAAVVLVNMVIGILVFNKlVSKDGITDKKLKERAGQpsphpLGRALKcaecgvlsaadatsdatsnamaslwSSCVVLP 1174
Cdd:cd15254    170 PALIIVAVNSIITVVVIVK-ILRPSIGEKPSKQERSS-----LFQIIK-------------------------SIGVLTP 218
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1175 LLALTWMSAVLAVTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDA 1224
Cdd:cd15254    219 LLGLTWGFGLATVIKGSSIVFHILFTLLNAFQGLFILVFGTLWDKKVQEA 268
7tmB2_GPR112 cd15997
Probable G protein-coupled receptor 112, member of the class B2 family of seven-transmembrane ...
947-1229 1.97e-17

Probable G protein-coupled receptor 112, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR112 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR64, GPR97, GPR114, and GPR126. GPR112 is specifically expressed in normal enterochromatin cells and gastrointestinal neuroendocrine carcinoma cells, but its biological function is unknown. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320663  Cd Length: 269  Bit Score: 84.33  E-value: 1.97e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  947 TLI--VGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQ--TQTRNKVVCTLVAAFLHFFFLSS 1022
Cdd:cd15997      5 TLItyLGCGISSIFLGITLVTYLAFEKLRRDYPSKILINLCTALLMLNLVFLLNSwlSSFNNYGLCITVAAFLHYFLLAS 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1023 FCWVLTEAWQSYMAVTgHLRNRLIRK---RFLCLGWGLPALVVAISVGFTK--------AKGY-STMNYCWLSLEGGLLY 1090
Cdd:cd15997     85 FTWMGLEAVHMYFALV-KVFNIYIPNyilKFCIAGWGIPAVVVALVLAINKdfygnelsSDSLhPSTPFCWIQDDVVFYI 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1091 AFVGPAAAVVLVNMVIGILVFNKLVSkdgITDKKLKERAGQPSPHPLGRAlkcaecgvlsaadatsdatsnamASLwssc 1170
Cdd:cd15997    164 SVVAYFCLIFLCNISMFITVLIQIRS---MKAKKPSRNWKQGFLHDLKSV-----------------------ASL---- 213
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034661056 1171 vvLPLLALTWMSAVLAVTDRRsALFQILFAVFDSLEGFVIVMVHCILRREVQDavKCRV 1229
Cdd:cd15997    214 --TFLLGLTWGFAFFAWGPVR-IFFLYLFSICNTLQGFFIFVFHCLMKENVRK--QWRI 267
7tmB2_GPR126-like_Adhesion_VIII cd15258
orphan GPR126 and related proteins, group VIII adhesion GPCRs, member of the class B2 family ...
947-1222 4.35e-17

orphan GPR126 and related proteins, group VIII adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Group VIII adhesion GPCRs include orphan GPCRs such as GPR56, GPR64, GPR97, GPR112, GPR114, and GPR126. GPR56 is involved in the regulation of oligodendrocyte development and myelination in the central nervous system via coupling to G(12/13) proteins, which leads to the activation of RhoA GTPase. GPR126, on the other hand, is required for Schwann cells, but not oligodendrocyte myelination in the peripheral nervous system. Gpr64 is mainly expressed in the epididymis of male reproductive tract, and targeted deletion of GPR64 causes sperm stasis and efferent duct blockage due to abnormal fluid reabsorption, resulting in male infertility. GPR64 is also over-expressed in Ewing's sarcoma (ES), as well as upregulated in other carcinomas from kidney, prostate or lung, and promotes invasiveness and metastasis in ES via the upregulation of placental growth factor (PGF) and matrix metalloproteinase (MMP) 1. GPR97 is identified as a lymphatic adhesion receptor that is specifically expressed in lymphatic endothelium, but not in blood vascular endothelium, and is shown to regulate migration of lymphatic endothelial cells via the small GTPases RhoA and cdc42. GPR112 is specifically expressed in normal enterochromatin cells and gastrointestinal neuroendocrine carcinoma cells, but its biological function is unknown. GPR114 is mainly found in granulocytes (polymorphonuclear leukocytes), and GPR114-transfected cells induced an increase in cAMP levels via coupling to G(s) protein. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320386 [Multi-domain]  Cd Length: 267  Bit Score: 83.23  E-value: 4.35e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  947 TLI--VGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILI--GQTQTRNKVVCTLVAAFLHFFFLSS 1022
Cdd:cd15258      5 TFIsyVGCGISAIFLAITILTYIAFRKLRRDYPSKIHMNLCAALLLLNLAFLLssWIASFGSDGLCIAVAVALHYFLLAC 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1023 FCWVLTEAWQSYMAVtGHLRNRLIRKRFL---CLGWGLPALVVAIS----------VGFTKAKGYSTMNYCWLSLEGGLL 1089
Cdd:cd15258     85 LTWMGLEAFHLYLLL-VKVFNTYIRRYILklcLVGWGLPALLVTLVlsvrsdnygpITIPNGEGFQNDSFCWIRDPVVFY 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1090 YAFVGPAAAVVLVNMVIGILVFNKLVSKDGITDKKLKERAGQpsphplgralkcaecGVLSAADATSdatsnamaslwss 1169
Cdd:cd15258    164 ITVVGYFGLTFLFNMVMLATVLVQICRLREKAQATPRKRALH---------------DLLTLLGLTF------------- 215
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034661056 1170 cvvlpLLALTWMSAVLAVtdrrsALFQI----LFAVFDSLEGFVIVMVHCILRREVQ 1222
Cdd:cd15258    216 -----LLGLTWGLAFFAW-----GPFNLpflyLFAIFNSLQGFFIFIWYCSMKENVR 262
7tmB2_GPR124-like_Adhesion_III cd15259
orphan GPR124 and related proteins, group III adhesion GPCRs, member of class B2 family of ...
950-1221 1.09e-16

orphan GPR124 and related proteins, group III adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; group III adhesion GPCRs include orphan GPR123, GPR124, GPR125, and their closely related proteins. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. GPR123 is predominantly expressed in the CNS including thalamus, brain stem and regions containing large pyramidal cells. GPR124, also known as tumor endothelial marker 5 (TEM5), is highly expressed in tumor vessels and in the vasculature of the developing embryo. GPR124 is essentially required for proper angiogenic sprouting into neural tissue, CNS-specific vascularization, and formation of the blood-brain barrier. GPR124 also interacts with the PDZ domain of DLG1 (discs large homolog 1) through its PDZ-binding motif. Recently, studies of double-knockout mice showed that GPR124 functions as a co-activator of Wnt7a/Wnt7b-dependent beta-catenin signaling in brain endothelium. Furthermore, WNT7-stimulated beta-catenin signaling is regulated by GPR124's intracellular PDZ binding motif and leucine-rich repeats (LRR) in its N-terminal extracellular domain. GPR125 directly interacts with dishevelled (Dvl) via its intracellular C-terminus, and together, GPR125 and Dvl recruit a subset of planar cell polarity (PCP) components into membrane subdomains, a prerequisite for activation of Wnt/PCP signaling. Thus, GPR125 influences the noncanonical WNT/PCP pathway, which does not involve beta-catenin, through interacting with and modulating the distribution of Dvl.


Pssm-ID: 320387 [Multi-domain]  Cd Length: 260  Bit Score: 81.65  E-value: 1.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  950 VGCGVSSLTLLMLVIIYVSVWRYIRSERSV--ILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCWV- 1026
Cdd:cd15259     10 AGAALCLLCLLATIITYIVFHRLIRISRKGrhMLVNLCLHLLLTCVVFVGGINRTANQLVCQAVGILLHYSTLCTLLWVg 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1027 ---------LTEAWQSYMAVTGHLRNRLIRKRFLCLGWGLPALVVAISVGfTKAKGYSTMNYCWLSLEGGLLyAFVGPAA 1097
Cdd:cd15259     90 vtarnmykqVTKTAKPPQDEDQPPRPPKPMLRFYLIGWGIPLIICGITAA-VNLDNYSTYDYCWLAWDPSLG-AFYGPAA 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1098 AVVLVNMVIGIlvfnklvskdgitdkklkeragqpsphplgralkCAECGVlsaadatSDATSNAMASLWSSCVVLPLLA 1177
Cdd:cd15259    168 LIVLVNCIYFL----------------------------------RIYCQL-------KGAPVSFQSQLRGAVITLFLYV 206
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1034661056 1178 LTWMSAVLAVTDRR--SALFQILFAVFDSLEGFVIVMVHCILRREV 1221
Cdd:cd15259    207 AMWACGALAVSQRYflDLVFSCLYGATCSSLGLFVLIHHCLSREDV 252
7tmB2_GPR111_115 cd15994
orphan adhesion receptors GPR111 and GPR115, member of the class B2 family of ...
950-1226 2.76e-16

orphan adhesion receptors GPR111 and GPR115, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR111 and GPR115 are highly homologous orphan receptors that belong to group VI adhesion-GPCRs along with GPR110, GPR113, and GPR116. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS. Both GPR111 and GPR5 are present only in land-living animals and are predominantly expressed in the developing skin.


Pssm-ID: 320660 [Multi-domain]  Cd Length: 267  Bit Score: 80.65  E-value: 2.76e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  950 VGCGVSSLTLLMLVIIYVSVW-RYIRSE----RSVILINFCLSIISSNALILIG---QTQTRNKVVCTLVAAFLHFFFLS 1021
Cdd:cd15994     10 IGLGLSIFSLALCLTIEAVVWsHVTKTEitymRHVCIVNIATSLLIADVWFILAsivHNTALNYPLCVAATFFLHFFYLS 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1022 SFCWVLTEAwqsYMAVTGHLR--NRLIRKRFLC----LGWGLPALVVAISVGFTK-AKGYSTMNYCWLSL-EGGLLYAFV 1093
Cdd:cd15994     90 LFFWMLTKA---LLILYGILLvfFKITKSVFIAtafsIGYGCPLVIAVLTVAITEpKKGYLRPEACWLNWdETKALLAFI 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1094 GPAAAVVLVNMVIGILVFNKlvskdgitdkklkeragqpsphpLGRAlkcaecgvlSAADATSDATSNAMASLWSSCVVL 1173
Cdd:cd15994    167 IPALSIVVVNLIVVGVVVVK-----------------------TQRS---------SIGESCKQDVSNIIRISKNVAILT 214
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034661056 1174 PLLALTWMSAVLAVTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVK 1226
Cdd:cd15994    215 PLLGLTWGFGLATIIDSRSLPFHIIFALLNAFQGFFILLFGTILDRKIRIALY 267
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
412-462 5.52e-16

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 73.39  E-value: 5.52e-16
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034661056   412 WDEWSPWSLCSSTCGRGFRDRTRTC--RPPQFGGNPCEGPEKQTKFCNIALCP 462
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTGEDVETRACNEQPCP 53
7tmB2_GPR64 cd15444
orphan adhesion receptor GPR64 and related proteins, member of subfamily B2 of the class B ...
950-1222 2.46e-14

orphan adhesion receptor GPR64 and related proteins, member of subfamily B2 of the class B secretin-like receptors of seven-transmembrane G protein-coupled receptors; GPR64 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR97, GPR112, GPR114, and GPR126. GPR64 is mainly expressed in the epididymis of male reproductive tract, and targeted deletion of GPR64 causes sperm stasis and efferent duct blockage due to abnormal fluid reabsorption, resulting in male infertility. GPR64 is also over-expressed in Ewing's sarcoma (ES), as well as upregulated in other carcinomas from kidney, prostate or lung, and promotes invasiveness and metastasis in ES via the upregulation of placental growth factor (PGF) and matrix metalloproteinase (MMP) 1. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320560 [Multi-domain]  Cd Length: 271  Bit Score: 75.25  E-value: 2.46e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  950 VGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVV---CTLVAAFLHFFFLSSFCWV 1026
Cdd:cd15444     10 IGCGLSAIFLSVTLVTYIAFEKIRRDYPSKILIQLCVALLLLNLVFLLDSWIALYKDIvglCISVAVFLHYFLLVSFTWM 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1027 LTEAWQSYMAVTgHLRNRLIRK---RFLCLGWGLPALVVAISVGFTK------AKGY----STMNYCWLSLEGGLLYAFV 1093
Cdd:cd15444     90 GLEAFHMYLALV-KVFNTYIRKyilKFCIVGWGVPAVVVAIVLAVSKdnyglgSYGKspngSTDDFCWINNNIVFYITVV 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1094 GPAAAVVLVNMVIGILVFNKLVSkdgITDKKlkeragqpsphPLGRALKcaecgvlsaadatsdatsNAMASLWSSCVVL 1173
Cdd:cd15444    169 GYFCVIFLLNISMFIVVLVQLCR---IKKQK-----------QLGAQRK------------------TSLQDLRSVAGIT 216
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1034661056 1174 PLLALTWMSAVLAvTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQ 1222
Cdd:cd15444    217 FLLGITWGFAFFA-WGPVNLAFMYLFAIFNTLQGFFIFIFYCVAKENVR 264
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
522-572 2.50e-14

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 68.77  E-value: 2.50e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034661056   522 WQAWASWGSCSVTCGAGSQRRERVCSGP--FFGGAACQGPQDEYRQCGTQRCP 572
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPppQNGGGPCTGEDVETRACNEQPCP 53
7tmB2_GPR128 cd15257
orphan adhesion receptor GPR128, member of the class B2 family of seven-transmembrane G ...
950-1217 3.84e-14

orphan adhesion receptor GPR128, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR128 is an orphan receptor of the adhesion family (subclass B2) that belongs to the class B GPCRs. Expression of GPR128 was detected in the mouse intestinal mucosa and is thought to be involved in energy balance, as its knockout mice showed a decrease in body weight gain and an increase in intestinal contraction frequency compared to wild-type controls. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320385 [Multi-domain]  Cd Length: 303  Bit Score: 75.29  E-value: 3.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  950 VGCGVSsLTLLMLVIIYVSVWRYIRSER-SVILINFCLSIISSNALILIGQTQTRNKV---------------------- 1006
Cdd:cd15257     10 IGCVLS-IAGLVITIIFHLHTRKLRKSSvTWVLLNLCSSLLLFNIIFTSGVENTNNDYeistvpdretntvllseeyvep 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1007 ---VCTLVAAFLHFFFLSSFCWVLTEAWQSYMAVTGHLRN--RLIRKRFLCLGWGLPALVVAISVGFTKA---------K 1072
Cdd:cd15257     89 dtdVCTAVAALLHYFLLVTFMWNAVYSAQLYLLLIRMMKPlpEMFILQASAIGWGIPAVVVAITLGATYRfptslpvftR 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1073 GYSTMNYCWL-------SLEGGLLYAFVGPAAAVVLVNMVIGILVFNKLVSKDgITDKKLKERAgqpsphplgralkcae 1145
Cdd:cd15257    169 TYRQEEFCWLaaldknfDIKKPLLWGFLLPVGLILITNVILFIMTSQKVLKKN-NKKLTTKKRS---------------- 231
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034661056 1146 cgvlsaadatsdatsnAMASLWSSCVVLPLLALTWMSA--VLAVTDRRSALFQILFAVFDSLEGFVIvmvhCIL 1217
Cdd:cd15257    232 ----------------YMKKIYITVSVAVVFGITWILGylMLVNNDLSKLVFSYIFCITNTTQGVQI----FIL 285
7tmB1_CRF-R1 cd15445
corticotropin-releasing factor receptor 1, member of the class B family of seven-transmembrane ...
950-1228 8.99e-14

corticotropin-releasing factor receptor 1, member of the class B family of seven-transmembrane G protein-coupled receptors; The vertebrate corticotropin-releasing factor (CRF) receptors are predominantly expressed in central nervous system with high levels in cortex tissue, brain stem, and pituitary. They have two isoforms as a result of alternative splicing of the same receptor gene: CRF-R1 and CRF-R2, which differ in tissue distribution and ligand binding affinities. Recently, a third CRF receptor (CRF-R3) has been identified in catfish pituitary. The catfish CRF-R1 is highly homologous to CRF-R3. CRF is a 41-amino acid neuropeptide that plays a central role in coordinating neuroendocrine, behavioral, and autonomic responses to stress by acting as the primary neuroregulator of the hypothalamic-pituitary-adrenal axis, which controls the levels of cortisol and other stress related hormones. In addition, the CRF family of neuropeptides also includes structurally related peptides such as mammalian urocortin, fish urotensin I, and frog sauvagine. The actions of CRF and CRF-related peptides are mediated through specific binding to CRF-R1 and CRF-R2. CRF and urocortin 1 bind and activate mammalian CRF-R1 with similar high affinities. By contrast, urocortin 2 and urocortin 3 do not bind to CRF-R1 or stimulate CRF-R1-mediated cAMP formation. Urocortin 1 also shows high affinity for mammalian CRF-R2, whereas CRF has significantly lower affinity for this receptor. These evidence suggest that urocortin 1 is an endogenous ligand for CRF-R1 and CRF-R2. The CRF receptors are members of the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, and parathyroid hormone (PTH). These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on its cellular location and function, CRF receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320561 [Multi-domain]  Cd Length: 265  Bit Score: 73.43  E-value: 8.99e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  950 VGCGVSSLTLLMLVIIYVSVwRYIRSERSVILINFCLSIISSNA------LILIGQTQTRNKVVCTLVAAFLHFFFLSSF 1023
Cdd:cd15445     10 LGHCISLVALLVAFVLFLRL-RSIRCLRNIIHWNLITAFILRNAtwfvvqLTMSPEVHQSNVVWCRLVTAAYNYFHVTNF 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1024 CWVLTEAWQSYMA-VTGHLRNRLIRKRFLCLGWGLP-ALVVAISVGftkaKGYSTMNYCWLSLEGGLL--YAFVGPAAAV 1099
Cdd:cd15445     89 FWMFGEGCYLHTAiVLTYSTDKLRKWMFICIGWCIPfPIIVAWAIG----KLYYDNEKCWFGKRAGVYtdYIYQGPMILV 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1100 VLVNMvigILVFNKLvskdGITDKKLKEragqpsphplgralkcaecgvlsaadATSDATSNAMASLWSSCVVLPLLALT 1179
Cdd:cd15445    165 LLINF---IFLFNIV----RILMTKLRA--------------------------STTSETIQYRKAVKATLVLLPLLGIT 211
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034661056 1180 WMSA-VLAVTDRRSALFQILFAVF-DSLEGFVIVMVHCILRREVQDAVKCR 1228
Cdd:cd15445    212 YMLFfVNPGEDEISRIVFIYFNSFlESFQGFFVSVFYCFLNSEVRSAVRKR 262
7tmB2_GPR126 cd15996
orphan adhesion receptor GPR126, member of the class B2 family of seven-transmembrane G ...
950-1222 3.64e-13

orphan adhesion receptor GPR126, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR126 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR64, GPR97, GPR112, and GPR114. GPR126 is required in Schwann cells for proper differentiation and myelination via G-Protein Activation. GPR126 is believed to couple to G(s)-protein, which leads to activation of adenylate cyclase for cAMP production. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320662  Cd Length: 271  Bit Score: 71.84  E-value: 3.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  950 VGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILI-GQTQTRN-KVVCTLVAAFLHFFFLSSFCWVL 1027
Cdd:cd15996     10 IGCGISAIFSAATLLTYIAFEKLRRDYPSKILMNLSTALLFLNLVFLLdGWIASFEiDELCITVAVLLHFFLLATFTWMG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1028 TEAWQSYMAVTgHLRNRLIRK---RFLCLGWGLPALVVAISVGFTK---AKGYSTMNY--------CWLSLEGGLLYAFV 1093
Cdd:cd15996     90 LEAIHMYIALV-KVFNTYIRRyilKFCIIGWGLPALIVSIVLASTNdnyGYGYYGKDKdgqggdefCWIKNPVVFYVTCA 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1094 GPAAAVVLVNMVIGILVFNKLVSKDGI-TDKKLKEragqpsphplgralkcaecgvlsaadatsdatsNAMASLWSSCVV 1172
Cdd:cd15996    169 AYFGIMFLMNVAMFIVVMVQICGRNGKrSNRTLRE---------------------------------EILRNLRSVVSL 215
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1173 LPLLALTWMSAVLAVTDRRSAlFQILFAVFDSLEGFVIVMVHCILRREVQ 1222
Cdd:cd15996    216 TFLLGMTWGFAFFAWGPVNLA-FMYLFTIFNSLQGLFIFVFHCALKENVQ 264
7tmB1_CRF-R cd15264
corticotropin-releasing factor receptors, member of the class B family of seven-transmembrane ...
946-1229 4.21e-13

corticotropin-releasing factor receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; The vertebrate corticotropin-releasing factor (CRF) receptors are predominantly expressed in central nervous system with high levels in cortex tissue, brain stem, and pituitary. They have two isoforms as a result of alternative splicing of the same receptor gene: CRF-R1 and CRF-R2, which differ in tissue distribution and ligand binding affinities. Recently, a third CRF receptor (CRF-R3) has been identified in catfish pituitary. The catfish CRF-R1 is highly homologous to CRF-R3. CRF is a 41-amino acid neuropeptide that plays a central role in coordinating neuroendocrine, behavioral, and autonomic responses to stress by acting as the primary neuroregulator of the hypothalamic-pituitary-adrenal axis, which controls the levels of cortisol and other stress related hormones. In addition, the CRF family of neuropeptides also includes structurally related peptides such as mammalian urocortin, fish urotensin I, and frog sauvagine. The actions of CRF and CRF-related peptides are mediated through specific binding to CRF-R1 and CRF-R2. CRF and urocortin 1 bind and activate mammalian CRF-R1 with similar high affinities. By contrast, urocortin 2 and urocortin 3 do not bind to CRF-R1 or stimulate CRF-R1-mediated cAMP formation. Urocortin 1 also shows high affinity for mammalian CRF-R2, whereas CRF has significantly lower affinity for this receptor. These evidence suggest that urocortin 1 is an endogenous ligand for CRF-R1 and CRF-R2. The CRF receptors are members of the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, and parathyroid hormone (PTH). These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on its cellular location and function, CRF receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320392 [Multi-domain]  Cd Length: 265  Bit Score: 71.29  E-value: 4.21e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  946 VTLI---VGCGVSSLTLLMLVIIYVsVWRYIRSERSVILINFCLSIISSNALILIGQ------TQTRNKVVCTLVAAFLH 1016
Cdd:cd15264      3 VALIiyyLGFSISLVALAVALIIFL-YFRSLRCLRNNIHCNLIVTFILRNVTWFIMQntlteiHHQSNQWVCRLIVTVYN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1017 FFFLSSFCWVLTEAWQSY-MAVTGHLRNRLIRKRFLCLGWGLPA-LVVAISVGftkaKGYSTMNYCWLSLEGGLLYAFV- 1093
Cdd:cd15264     82 YFQVTNFFWMFVEGLYLHtMIVWAYSADKIRFWYYIVIGWCIPCpFVLAWAIV----KLLYENEHCWLPKSENSYYDYIy 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1094 -GPAAAVVLVNMVIgilVFNKLVskdgITDKKLKEragqpsphplgralkcaecgvlsaadATSDATSNAMASLWSSCVV 1172
Cdd:cd15264    158 qGPILLVLLINFIF---LFNIVW----VLITKLRA--------------------------SNTLETIQYRKAVKATLVL 204
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034661056 1173 LPLLALTWMSAVLAVTDrrSALFQILFAVFD----SLEGFVIVMVHCILRREVQDAVKCRV 1229
Cdd:cd15264    205 LPLLGITYMLFFINPGD--DKTSRLVFIYFNtflqSFQGLFVAVFYCFLNGEVRSAIRKKF 263
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
877-935 3.50e-12

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


Pssm-ID: 197639  Cd Length: 49  Bit Score: 62.40  E-value: 3.50e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034661056   877 TNQTCILWDETDvpsssappqlGPWSWRGCRTVPLDALRTRCLCDRLSTFAILAQLSAD 935
Cdd:smart00303    1 FNPICVFWDESS----------GEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
359-407 7.08e-12

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 61.83  E-value: 7.08e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1034661056   359 EWSPWSVCSSTCGEGWQTRTRFCVSSSYS---TQCSGPLREQRLCNNSAvCP 407
Cdd:smart00209    3 EWSEWSPCSVTCGGGVQTRTRSCCSPPPQnggGPCTGEDVETRACNEQP-CP 53
7tmB1_hormone_R cd15041
The subfamily B1 of hormone receptors (secretin-like), member of the class B family ...
943-1226 9.67e-12

The subfamily B1 of hormone receptors (secretin-like), member of the class B family seven-transmembrane G protein-coupled receptors; The B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of this subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. Moreover, the B1 subfamily receptors play key roles in hormone homeostasis and are promising drug targets in various human diseases including diabetes, osteoporosis, obesity, neurodegenerative conditions (Alzheimer###s and Parkinson's), cardiovascular disease, migraine, and psychiatric disorders (anxiety, depression). Furthermore, the subfamilies B2 and B3 consist of receptors that are capable of interacting with epidermal growth factors (EGF) and the Drosophila melanogaster Methuselah gene product (Mth), respectively. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes.


Pssm-ID: 341321 [Multi-domain]  Cd Length: 273  Bit Score: 67.25  E-value: 9.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  943 LPSVTLI-VGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNA-LILIGQTQTRNKVvcTLVAAFLHFFFL 1020
Cdd:cd15041      1 LLVVYYIyLVGYSLSLVALLPAIVIFLYFRSLRCTRIRLHINLFLSFILRAVfWIIWDLLVVYDRL--TSSGVETVLMQN 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1021 SSFCWVLTEAWQ-------SYMAVTG-HLRNRLIR---------KRFLCLGWGLPALVVAIsVGFTKAKGYSTMnyCWLS 1083
Cdd:cd15041     79 PVGCKLLSVLKRyfksanyFWMLCEGlYLHRLIVVaffsepsslKLYYAIGWGLPLVIVVI-WAIVRALLSNES--CWIS 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1084 L-EGGLLYAFVGPAAAVVLVNMVIGILVFNKLVSKdgitdkkLKEragQPSPHPLG--RALKcaecgvlsaadatsdats 1160
Cdd:cd15041    156 YnNGHYEWILYGPNLLALLVNLFFLINILRILLTK-------LRS---HPNAEPSNyrKAVK------------------ 207
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034661056 1161 namASLwsscVVLPLLALTWMSAVL--AVTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVK 1226
Cdd:cd15041    208 ---ATL----ILIPLFGIQYLLTIYrpPDGSEGELVYEYFNAILNSSQGFFVAVIYCFLNGEVQSELK 268
TSP_1 pfam00090
Thrombospondin type 1 domain;
414-461 2.80e-11

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 59.74  E-value: 2.80e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1034661056  414 EWSPWSLCSSTCGRGFRDRTRTCRPPQFGGNPCEGPEKQTKFCNIALC 461
Cdd:pfam00090    2 PWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
414-461 3.85e-11

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 59.60  E-value: 3.85e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1034661056  414 EWSPWSLCSSTCGRGFRDRTRT-CRPPQFGGNPCeGPEKQTKFCNIALC 461
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTRTvIVEPQNGGRPC-PELLERRPCNLPPC 52
HormR smart00008
Domain present in hormone receptors;
574-640 9.31e-11

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 59.07  E-value: 9.31e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034661056   574 PHEICDEDNFGAVIWKETPAGEVAAVRCPRNATGL-----ILRRCELDEegiaYWEP--PTYIRCVSIDYRNIQ 640
Cdd:smart00008    1 TDLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGFsyktgASRNCTENG----GWSPpfPNYSNCTSNDYEELK 70
7tmB3_Methuselah-like cd15039
Methuselah-like subfamily B3, member of the class B family of seven-transmembrane G ...
949-1114 9.44e-11

Methuselah-like subfamily B3, member of the class B family of seven-transmembrane G protein-coupled receptors; The subfamily B3 of class B GPCRs consists of Methuselah (Mth) and its closely related proteins found in bilateria. Mth was originally identified in Drosophila as a GPCR affecting stress resistance and aging. In addition to the seven transmembrane helices, Mth contains an N-terminal extracellular domain involved in ligand binding, and a third intracellular loop (IC3) required for the specificity of G-protein coupling. Drosophila Mth mutants showed an increase in average lifespan by 35% and greater resistance to a variety of stress factors, including starvation, high temperature, and paraquat-induced oxidative toxicity. Moreover, mutations in two endogenous peptide ligands of Methuselah, Stunted A and B, showed an increased in lifespan and resistance to oxidative stress induced by dietary paraquat. These results strongly suggest that the Stunted-Methuselah system plays important roles in stress response and aging.


Pssm-ID: 410632 [Multi-domain]  Cd Length: 270  Bit Score: 64.55  E-value: 9.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  949 IVGCGVSSLTLLMLVIIYVsvwrYIRSERSV---ILINFCLSIISSNALILIGQTQT-RNKVVCTLVAAFLHFFFLSSFC 1024
Cdd:cd15039      9 LIGLIISLVFLLLTLAVYA----LLPELRNLhgkCLMCLVLSLFVAYLLLLIGQLLSsGDSTLCVALGILLHFFFLAAFF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1025 WVLTEAWQSYMAVTGHL---RNRLIRKRFL---CLGWGLPALVVAISVGFTKAK-------GYSTmNYCWLSLEGGLLYA 1091
Cdd:cd15039     85 WLNVMSFDIWRTFRGKRsssSRSKERKRFLrysLYAWGVPLLLVAVTIIVDFSPntdslrpGYGE-GSCWISNPWALLLY 163
                          170       180
                   ....*....|....*....|...
gi 1034661056 1092 FVGPAAAVVLVNMVIGILVFNKL 1114
Cdd:cd15039    164 FYGPVALLLLFNIILFILTAIRI 186
TSP_1 pfam00090
Thrombospondin type 1 domain;
525-571 4.12e-10

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 56.66  E-value: 4.12e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1034661056  525 WASWGSCSVTCGAGSQRRERVCSGPFFGGAACQGPQDEYRQCGTQRC 571
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49
7tmB2_GPR125 cd15999
G protein-coupled receptor 125, member of the class B2 family of seven-transmembrane G ...
957-1224 7.96e-10

G protein-coupled receptor 125, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR125 is an orphan receptor that has been classified as that belongs to the group III of adhesion GPCRs, which also includes orphan receptors GPR123 and GPR124. GPR125 directly interacts with dishevelled (Dvl) via its intracellular C-terminus, and together, GPR125 and Dvl recruit a subset of planar cell polarity (PCP) components into membrane subdomains, a prerequisite for activation of Wnt/PCP signaling. Thus, GPR125 influences the noncanonical WNT/PCP pathway, which does not involve beta-catenin, through interacting with and modulating the distribution of Dvl. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320665  Cd Length: 312  Bit Score: 62.19  E-value: 7.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  957 LTLLMLVIIYVSVWRYIRSERSV--ILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCWVLTEAWQSY 1034
Cdd:cd15999     17 LCLLTIIVSYIYHHSLVRISRKSwhMLVNLCFHIFLTCAVFVGGINQTRNASVCQAVGIILHYSTLATVLWVGVTARNIY 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1035 MAVTGHL-------------RNRLirkRFLCLGWGLPALVVAISVGfTKAKGY-STMN--YCWLSLEGGlLYAFVGPAAA 1098
Cdd:cd15999     97 KQVTRKAkrcqdpdepppppRPML---RFYLIGGGIPIIVCGITAA-ANIKNYgSRPNapYCWMAWEPS-LGAFYGPAGF 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1099 VVLVNMVIGILVFNKLvskdgitdKKLKERAGQ-PSPHPLGRALKCAECGVLSAADATSDATSNAMAS------------ 1165
Cdd:cd15999    172 IIFVNCMYFLSIFIQL--------KRHPERKYElKEPTEEQQRLAASEHGELNHQDSGSSSASCSLVStsalenehsfqa 243
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034661056 1166 -LWSSCVVLPLLALTWMSAVLAVTDR--RSALFQILFAVFD-SLEGFVIVMvHCILRREVQDA 1224
Cdd:cd15999    244 qLLGASLALFLYVALWIFGALAVSLYypMDLVFSCLFGATClSLGAFLVVH-HCVNREDVRRA 305
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
880-929 1.17e-09

GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for auto-proteolysis, so is thus named, GPS. The GPS motif is a conserved sequence of ~40 amino acids containing canonical cysteine and tryptophan residues, and is the most highly conserved part of the domain. In most, if not all, cell-adhesion GPCRs these undergo autoproteolysis in the GPS between a conserved aliphatic residue (usually a leucine) and a threonine, serine, or cysteine residue. In higher eukaryotes this motif is found embedded in the C-terminal beta-stranded part of a GAIN domain - GPCR-Autoproteolysis INducing (GAIN). The GAIN-GPS domain adopts a fold in which the GPS motif, at the C-terminus, forms five beta-strands that are tightly integrated into the overall GAIN domain. The GPS motif, evolutionarily conserved from tetrahymena to mammals, is the only extracellular domain shared by all human cell-adhesion GPCRs and PKD proteins, and is the locus of multiple human disease mutations. The GAIN-GPS domain is both necessary and sufficient functionally for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyze peptide bond hydrolysis. In the cell-adhesion GPCRs and PKD proteins, the GPS motif is always located at the end of their long N-terminal extracellular regions, immediately before the first transmembrane helix of the respective protein.


Pssm-ID: 460350  Cd Length: 44  Bit Score: 55.01  E-value: 1.17e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034661056  880 TCILWDETDvpsssapPQLGPWSWRGCRTVPLDALRTRCLCDRLSTFAIL 929
Cdd:pfam01825    2 QCVFWDFTN-------STTGRWSTEGCTTVSLNDTHTVCSCNHLTSFAVL 44
7tmB1_CRF-R2 cd15446
corticotropin-releasing factor receptor 2, member of the class B family of seven-transmembrane ...
950-1228 1.35e-09

corticotropin-releasing factor receptor 2, member of the class B family of seven-transmembrane G protein-coupled receptors; The vertebrate corticotropin-releasing factor (CRF) receptors are predominantly expressed in central nervous system with high levels in cortex tissue, brain stem, and pituitary. They have two isoforms as a result of alternative splicing of the same receptor gene: CRF-R1 and CRF-R2, which differ in tissue distribution and ligand binding affinities. Recently, a third CRF receptor (CRF-R3) has been identified in catfish pituitary. The catfish CRF-R1 is highly homologous to CRF-R3. CRF is a 41-amino acid neuropeptide that plays a central role in coordinating neuroendocrine, behavioral, and autonomic responses to stress by acting as the primary neuroregulator of the hypothalamic-pituitary-adrenal axis, which controls the levels of cortisol and other stress related hormones. In addition, the CRF family of neuropeptides also includes structurally related peptides such as mammalian urocortin, fish urotensin I, and frog sauvagine. The actions of CRF and CRF-related peptides are mediated through specific binding to CRF-R1 and CRF-R2. CRF and urocortin 1 bind and activate mammalian CRF-R1 with similar high affinities. By contrast, urocortin 2 and urocortin 3 do not bind to CRF-R1 or stimulate CRF-R1-mediated cAMP formation. Urocortin 1 also shows high affinity for mammalian CRF-R2, whereas CRF has significantly lower affinity for this receptor. These evidence suggest that urocortin 1 is an endogenous ligand for CRF-R1 and CRF-R2. The CRF receptors are members of the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, and parathyroid hormone (PTH). These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on its cellular location and function, CRF receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320562 [Multi-domain]  Cd Length: 264  Bit Score: 60.74  E-value: 1.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  950 VGCGVSSLTLLMLVIIYVSVwRYIRSERSVILINFCLSIISSNALILIGQ-----TQTRNKVVCTLVAAFLHFFFLSSFC 1024
Cdd:cd15446     10 LGHCISVGALVVAFLLFLCL-RSIRCLRNIIHWNLITTFILRNVMWFLLQmidhnIHESNEVWCRCITTIYNYFVVTNFF 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1025 WVLTEAWQSYMA-VTGHLRNRLIRKRFLCLGWGLPA-LVVAISVGftkaKGYSTMNYCWLSLEGGLL--YAFVGPAAAVV 1100
Cdd:cd15446     89 WMFVEGCYLHTAiVMTYSTDKLRKWVFLFIGWCIPCpIIVAWAIG----KLYYENEQCWFGKEPGKYidYIYQGPVILVL 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1101 LVNMVIGILVFNKLVSKdgitdkklkeragqpsphplgralkcaecgvLSAadATSDATSNAMASLWSSCVVLPLLALTW 1180
Cdd:cd15446    165 LINFVFLFNIVRILMTK-------------------------------LRA--STTSETIQYRKAVKATLVLLPLLGITY 211
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034661056 1181 MsaVLAVTDRRSALFQILFAVFD----SLEGFVIVMVHCILRREVQDAVKCR 1228
Cdd:cd15446    212 M--LFFVNPGEDDISQIVFIYFNsflqSFQGFFVSVFYCFLNGEVRSAARKR 261
7tmB1_NPR_B4_insect-like cd15260
insect neuropeptide receptor subgroup B4 and related proteins, member of the class B family of ...
949-1228 4.56e-09

insect neuropeptide receptor subgroup B4 and related proteins, member of the class B family of seven-transmembrane G protein-coupled receptors; This subgroup includes a neuropeptide receptor found in Nilaparvata lugens (brown planthopper) and its closely related proteins from mollusks and annelid worms. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes.


Pssm-ID: 320388 [Multi-domain]  Cd Length: 267  Bit Score: 59.21  E-value: 4.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  949 IVGCGVSSLTLLMLVIIYVSvWRYIRSERSVILINFCLSIISSNALILI--------GQTQTRNKVVCTLVAAFLHFFFL 1020
Cdd:cd15260      9 IGGYSVSLIALIISLAIFFS-FRSLRCTRITIHMNLFISFALNNLLWIVwyklvvdnPEVLLENPIWCQALHVLLQYFMV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1021 SSFCWVLTEAW--QSYMAVTGHLRNRLIRKrFLCLGWGLPALVVAISVGFTKAKGYSTmNYCWLSlEGGLLYAFVGPAAA 1098
Cdd:cd15260     88 CNYFWMFCEGLylHTVLVVAFISEKSLMRW-FIAIGWGVPLVITAIYAGVRASLPDDT-ERCWME-ESSYQWILIVPVVL 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1099 VVLVNMVIGILVFNKLVskdgitdKKLKeragQPSPHPlgralkcAECGVLSAADATsdatsnamaslwssCVVLPLLAL 1178
Cdd:cd15260    165 SLLINLIFLINIVRVLL-------TKLR----ATSPNP-------APAGLRKAVRAT--------------LILIPLLGL 212
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034661056 1179 TWMsaVLAVTDRRSA----LFQILFAVFDSLEGFVIVMVHCILRREVQDAVKCR 1228
Cdd:cd15260    213 QFL--LIPFRPEPGApletIYQYVSALLTSLQGLCVAVLFCFCNGEVIAAIKRK 264
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
264-314 2.73e-08

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 51.43  E-value: 2.73e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1034661056   264 WKLWSLWGECTRDCGGGLQTRTRTC-LPAPGVEGGGCEGVLEEGRQCNREAC 314
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
359-401 6.63e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 50.49  E-value: 6.63e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1034661056  359 EWSPWSVCSSTCGEGWQTRTRFCVS-SSYSTQCSGPLREQRLCN 401
Cdd:pfam00090    2 PWSPWSPCSVTCGKGIQVRQRTCKSpFPGGEPCTGDDIETQACK 45
7tmB2_GPR114 cd15443
orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G ...
949-1222 7.87e-07

orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR114 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include GPR56, GPR64, GPR97, GPR112, and GPR126. GPR114 is mainly found in granulocytes (polymorphonuclear leukocytes), and GPR114-transfected cells induced an increase in cAMP levels via coupling to G(s) protein. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320559 [Multi-domain]  Cd Length: 268  Bit Score: 52.45  E-value: 7.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  949 IVGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKV--VCTLVAAFLHFFFLSSFCWV 1026
Cdd:cd15443      9 IVGCSISAAASLLTILLHFFSRKQPKDSTTRIHMNLLGSLFLLNGSFLLSPPLATSQStwLCRAAAALLHYSLLCCLTWM 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1027 LTEAWQSYMaVTGHLRNRLIRKRF--LC-LGWGLPALVVAISVGFTKA----------KGYSTMNYCWLSLEGGLLYAFV 1093
Cdd:cd15443     89 AIEGFHLYL-LLVKVYNIYIRRYVlkLCvLGWGLPALIVLLVLIFKREaygphtiptgTGYQNASMCWITSSKVHYVLVL 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1094 GPAAAVVLVNMVIGILVFNKLvskdgitdKKLKERAGQPSphplGRALKcaecgvlsaadatsdatsNAMASLWSSCvvl 1173
Cdd:cd15443    168 GYAGLTSLFNLVVLAWVVRML--------RRLRSRKQELG----ERARR------------------DWVTVLGLTC--- 214
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1174 pLLALTWMSAVLAVTDrrSALFQI-LFAVFDSLEGFVIVMVHCILRREVQ 1222
Cdd:cd15443    215 -LLGTTWALAFFSFGV--FLIPQLfLFTIINSLYGFFICLWYCTQRRRSD 261
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
575-634 9.64e-07

Hormone receptor domain; This extracellular domain contains four conserved cysteines that probably for disulphide bridges. The domain is found in a variety of hormone receptors. It may be a ligand binding domain.


Pssm-ID: 397086  Cd Length: 64  Bit Score: 47.36  E-value: 9.64e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034661056  575 HEICDEDNFGAVIWKETPAGEVAAVRCPR-----NATGLILRRCelDEEGiaYWE---PPTYIRCVSI 634
Cdd:pfam02793    1 GLGCPRTWDGILCWPRTPAGETVEVPCPDyfsgfDPRGNASRNC--TEDG--TWSehpPSNYSNCTSN 64
7tmB1_DH_R cd15263
insect diuretic hormone receptors, member of the class B family of seven-transmembrane G ...
943-1226 1.10e-06

insect diuretic hormone receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; This group includes G protein-coupled receptors that specifically bind to insect diuretic hormones found in Manduca sexta (moth) and Acheta domesticus (the house cricket), among others. Insect diuretic hormone and their GPCRs play critical roles in the regulation of water and ion balance. Thus they are attractive targets for developing new insecticides. Activation of the diuretic hormone receptors stimulate adenylate cyclase, thereby increasing cAMP levels in Malpighian tube. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of Gs family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx.


Pssm-ID: 320391 [Multi-domain]  Cd Length: 272  Bit Score: 51.99  E-value: 1.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  943 LPSVTLIVGCGVSSLTLLMLVIIYVSvWRYIRSERSVILINFCLSIISSNA-----LILIGQTQTRNKVVCTLVAaFLHF 1017
Cdd:cd15263      3 VTTTIYFIGYSLSLVALSLALWIFLY-FKDLRCLRNTIHTNLMFTYILADLtwiltLTLQVSIGEDQKSCIILVV-LLHY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1018 FFLSSFCWVLTEAWQSYMAVTGHLRNRLIRKR-FLCLGWGLPALVVAIsvgFTKAKGYSTMNYCWLSLEGGLL------- 1089
Cdd:cd15263     81 FHLTNFFWMFVEGLYLYMLVVETFSGENIKLRvYAFIGWGIPAVVIVI---WAIVKALAPTAPNTALDPNGLLkhcpwma 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1090 -----YAFVGPAAAVVLVNMVIGILVFNKLvskdgITdkKLKeragqpsphplgralkcaecgvlSAADATSDATSNAMA 1164
Cdd:cd15263    158 ehivdWIFQGPAILVLAVNLVFLVRIMWVL-----IT--KLR-----------------------SANTVETQQYRKAAK 207
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034661056 1165 SLwssCVVLPLLALTWMSAVLAVTDRRSA-LFQILFAVFDSLEGFVIVMVHCILRREVQDAVK 1226
Cdd:cd15263    208 AL---LVLIPLLGITYILVIAGPTEGIAAnIFEYVRAVLLSTQGFTVALFYCFLNTEVRNTLR 267
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
524-571 1.12e-06

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 46.89  E-value: 1.12e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1034661056  524 AWASWGSCSVTCGAGSQRRER-VCSGPFFGGAACqGPQDEYRQCGTQRC 571
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTRtVIVEPQNGGRPC-PELLERRPCNLPPC 52
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
359-379 1.46e-06

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 46.50  E-value: 1.46e-06
                           10        20
                   ....*....|....*....|.
gi 1034661056  359 EWSPWSVCSSTCGEGWQTRTR 379
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTR 25
7tmB2_GPR123 cd16000
G protein-coupled receptor 123, member of the class B2 family of seven-transmembrane G ...
954-1221 1.90e-06

G protein-coupled receptor 123, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR123 is an orphan receptor that has been classified as that belongs to the group III of adhesion GPCRs, and also includes orphan receptors GPR124 and GPR125. GPR123 is predominantly expressed in the CNS including thalamus, brain stem and regions containing large pyramidal cells, yet its biological function remains to be determined. Adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320666 [Multi-domain]  Cd Length: 275  Bit Score: 51.49  E-value: 1.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  954 VSSLTLLMLVIIYVSVWRYIRSERSV--------ILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCW 1025
Cdd:cd16000      8 VYACTAVMLLCLFASIITYIVHHSTIrisrkgwhMLLNFCFHTALTFAVFAGGINRTKYPIICQAVGIVLHYSTLSTMLW 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1026 VLTEAWQSYMAVTG------------HLRNRLIrkRFLCLGWGLPALVVAISVGfTKAKGYSTMN----YCWLSLEGGlL 1089
Cdd:cd16000     88 IGVTARNIYKQVTKkphlcqdtdqppYPKQPLL--RFYLVSGGVPFIICGITAA-TNINNYGTEDedtpYCWMAWEPS-L 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1090 YAFVGPAAAVVLVNMVIGILVFNKLvskdgitdkklkeragqpSPHPlGRALKCAEcgvlsaadatsdaTSNAMASLWSS 1169
Cdd:cd16000    164 GAFYGPVAFIVLVTCIYFLCTYVQL------------------RRHP-ERKYELKN-------------EHSFKAQLRAA 211
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034661056 1170 CVVLPLLALTWMSAVLAVTDRR--SALFQILFAVFDSLEGFVIVMVHCILRREV 1221
Cdd:cd16000    212 AFTLFLFTATWAFGALAVSQGHflDMIFSCLYGAFCVTLGLFILIHHCAKRDDV 265
7tmB1_GHRHR2 cd15271
growth-hormone-releasing hormone receptor type 2, member of the class B family of ...
943-1229 2.25e-06

growth-hormone-releasing hormone receptor type 2, member of the class B family of seven-transmembrane G protein-coupled receptors; Growth hormone-releasing hormone receptor type 2 (GHRHR2) is found in non-mammalian vertebrates such as chicken and frog. It is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, pituitary adenylate cyclase activating polypeptide (PACAP), vasoactive intestinal peptide, and mammalian growth hormone-releasing hormone. These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. Mammalian GHRHR is a specific receptor for the growth hormone-releasing hormone (GHRH) that controls the synthesis and release of growth hormone (GH) from the anterior pituitary somatotrophs. Mutations in the gene encoding GHRHR have been connected to isolated growth hormone deficiency (IGHD), a short-stature condition caused by deficient production of GH or lack of GH action. Mammalian GHRH is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. GHRHR is found in mammals as well as zebrafish and chicken, whereas the GHRHR type 2, an ortholog of the GHRHR, has only been identified in ray-finned fish, chicken and Xenopus. Xenopus laevis GHRHR2 has been shown to interact with both endogenous GHRH and PACAP-related peptide (PRP).


Pssm-ID: 320399 [Multi-domain]  Cd Length: 267  Bit Score: 51.27  E-value: 2.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  943 LPSVTLIVGCGVS-SLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILI-------GQTQ---TRNKVVCTLV 1011
Cdd:cd15271      1 FSTVKLLYTVGYGtSLTSLITAVLIFCTFRKLHCTRNYIHINLFVSFILRALAVFIkdavlfaDESVdhcTMSTVACKAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1012 AAFLHFFFLSSFCWVLTEA--WQSYMAVTGHLRnrliRKRFLC---LGWGLPALVVAIsvgFTKAKGYSTMNYCWLSLEG 1086
Cdd:cd15271     81 VTFFQFCVLANFFWLLVEGmyLQTLLLLTFTSD----RKYFWWyilIGWGAPSVTVTV---WVLTRLQYDNRGCWDDLES 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1087 GLLYAFVGPAAAVVLVNMVIGILVFNKLVSKdgitdkklkeragqpsphplgraLKCAECGVlsaadatsDATSNAMASL 1166
Cdd:cd15271    154 RIWWIIKTPILLSVFVNFLIFINVIRILVQK-----------------------LKSPDVGG--------NDTSHYMRLA 202
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034661056 1167 WSSCVVLPLLALTWMsaVLAVTDRRSALFQILF--AVFDSLEGFVIVMVHCILRREVQDAVKCRV 1229
Cdd:cd15271    203 KSTLLLIPLFGVHYV--VFAFFPEHVGVEARLYfeLVLGSFQGFIVALLYCFLNGEVQAEIKKRL 265
7tmB1_calcitonin_R cd15274
calcitonin receptor, member of the class B family of seven-transmembrane G protein-coupled ...
949-1226 2.28e-06

calcitonin receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; This group includes G protein-coupled receptors for calcitonin (CT) and calcitonin gene-related peptides (CGRPs). Calcitonin, a 32-amino acid peptide hormone, is involved in calcium metabolism in many mammalian species and acts to reduce blood calcium levels and directly inhibits bone resorption by acting on osteoclast. Thus, CT acts as an antagonist to parathyroid hormone and is commonly used in the treatment of bone disorders. The CT receptor is predominantly found in osteoclasts, kidney, and brain, and is primarily coupled to stimulatory G(s) protein, which leads to activation of adenylate cyclase, thereby increasing cAMP production. CGRP, a member of the calcitonin family of peptides, is a potent vasodilator and may contribute to migraine. It is expressed in the peripheral and central nervous system and exists in two forms in humans (alpha-CGRP and beta-CGRP). CGRP meditates its physiological effects through calcitonin receptor-like receptor (CRLR) and receptor activity-modifying protein 1 (RAMP1), a single transmembrane domain protein. Thus, the CRLR/RAMP1 complex serves as a functional CGRP receptor. On the other hand, the CRLR/RAMP2 and CRLR/RAMP3 complexes function as adrenomedullin-specific receptors. The CT and CGRP receptors belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide.


Pssm-ID: 341343 [Multi-domain]  Cd Length: 274  Bit Score: 51.32  E-value: 2.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  949 IVGCGVSSLTLLMLVIIYVSvWRYIRSERSVILINFCLSIISsNALILI---------GQTQTRNKVVCTLVAAFLHFFF 1019
Cdd:cd15274      9 IVGHSLSIATLLISLGIFFF-FRSLSCQRVTLHKNLFLSYIL-NSIIIIihlvavvpnGELVARNPVSCKILHFIHQYMM 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1020 LSSFCWVLTEAWQSY----MAVTGHLRNRLIrkrFLCLGWGLPALVVAISVgFTKAKGYStmNYCWLSLEGGLLYAFVGP 1095
Cdd:cd15274     87 GCNYFWMLCEGIYLHtlivVAVFAEKQRLMW---YYLLGWGFPLIPTTIHA-ITRAVYYN--DNCWLSSETHLLYIIHGP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1096 AAAVVLVNMVIGILVFNKLVSkdgitdkKLKEragqpsphplgralkcaecgvlsaadaTSDATSNA-MASLWSSCVVLP 1174
Cdd:cd15274    161 IMAALVVNFFFLLNIVRVLVT-------KLRE---------------------------THEAESHMyLKAVKATLILVP 206
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034661056 1175 LLA-----LTWMSAVLAVTDRRSALFQILFavfdSLEGFVIVMVHCILRREVQDAVK 1226
Cdd:cd15274    207 LLGiqfvlFPWRPSGKILGKIYDYVMHSLI----HFQGFFVATIFCFCNGEVQATLK 259
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
362-402 2.10e-05

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 43.60  E-value: 2.10e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1034661056  362 PWSVCSSTCGEGWQTRTRFCVSSSY-----STQCSGPLR--EQRLCNN 402
Cdd:pfam19030    5 PWGECSVTCGGGVQTRLVQCVQKGGgsivpDSECSAQKKppETQSCNL 52
7tmB1_PTH3R cd15983
parathyroid hormone 3 receptor, member of the class B family of seven-transmembrane G ...
1053-1226 2.53e-05

parathyroid hormone 3 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; The parathyroid hormone 3 receptor (PTH3R), one of the three subtypes of PTH receptor family, is found in chicken and fish, but it is absent in mammals. On the other hand, the PTH1R is found in all vertebrate species, whereas PTH2R is found in mammals and fish, but not in chicken or frog. PTH1R is activated by two polypeptide ligands: PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH2R is potently activated by tuberoinfundibular peptide-39 (TIP-39), but not by PTHrP. PTH also strongly activates human PTH2R, but only weakly activates rat and zebrafish PTH2Rs, suggesting that TIP-39 is a natural ligand for PTH2R. Conversely, PTH3R binds and responds to both PTH and PTHrP, but not the TIP-39. The PTH family receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways.


Pssm-ID: 320649 [Multi-domain]  Cd Length: 285  Bit Score: 47.99  E-value: 2.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1053 LGWGLPALVVAIsvgFTKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVVLVNMVIGILVFNKLVSKDGITDkklkerAGQP 1132
Cdd:cd15983    136 IGWGLPAVFVSV---WASVRVSLADTQCWDLSAGNLKWIYQVPILAAILVNFFLFLNIVRVLASKLWETN------TGKL 206
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1133 SPHPLGRALkcaecgvlsaadatsdatsnamasLWSSCVVLPLLALTWMS-AVLAVTDRRSALFQILF---AVFDSLEGF 1208
Cdd:cd15983    207 DPRQQYRKL------------------------LKSTLVLMPLFGVHYVLfMAMPYTDVTGLLWQIQMhyeMLFNSSQGF 262
                          170
                   ....*....|....*...
gi 1034661056 1209 VIVMVHCILRREVQDAVK 1226
Cdd:cd15983    263 FVAFIYCFCNGEVQAEIK 280
7tmB1_secretin cd15275
secretin receptor, member of the class B family of seven-transmembrane G protein-coupled ...
950-1228 7.43e-05

secretin receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Secretin receptor is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include vasoactive intestinal peptide (VIP), growth-hormone-releasing hormone (GHRH), and pituitary adenylate cyclase activating polypeptide (PACAP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors, and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. Secretin, a polypeptide secreted by entero-endocrine S cells in the small intestine, is involved in maintaining body fluid balance. This polypeptide regulates the secretion of bile and bicarbonate into the duodenum from the pancreatic and biliary ducts, as well as regulates the duodenal pH by the control of gastric acid secretion. Studies with secretin receptor-null mice indicate that secretin plays a role in regulating renal water reabsorption. Secretin mediates its biological actions by elevating intracellular cAMP via G protein-coupled secretin receptor, which is expressed in the brain, pancreas, stomach, kidney, and liver.


Pssm-ID: 320403 [Multi-domain]  Cd Length: 271  Bit Score: 46.27  E-value: 7.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  950 VGCGVSSLTLLMLVIIyVSVWRYIRSERSVILINFCLSIISSNALILI-----GQTQTRN-----KVVCTLVAAFLHFFF 1019
Cdd:cd15275     10 VGYSVSLVSLAIALAI-LCSFRRLHCTRNYIHMQLFLSFILRAISIFIkdavlFSSEDDNhcdiyTVGCKVAMVFSNYCI 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1020 LSSFCWVLTEAWQSYMAVTGHLRNRliRKR---FLCLGWGLPALVVaisVGFTKAKGYSTMNYCW-LSLEGGLLYAFVGP 1095
Cdd:cd15275     89 MANYSWLLVEGLYLHSLLSISFFSE--RKHlwwYIALGWGSPLIFI---ISWAIARYLHENEGCWdTRRNAWIWWIIRGP 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1096 AAAVVLVNMVIGILVFNKLVSKdgitdkklkeragqpsphplgralkcaecgvLSAADATSDATSNAMASLWSSCVVLPL 1175
Cdd:cd15275    164 VILSIFVNFILFLNILRILMRK-------------------------------LRAPDMRGNEFSQYKRLAKSTLLLIPL 212
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034661056 1176 LALTWMSAVLAVTDRRSALFQI-LFA--VFDSLEGFVIVMVHCILRREVQDAVKCR 1228
Cdd:cd15275    213 FGLHYILFAFFPEDVSSGTMEIwLFFelALGSFQGFVVAVLYCFLNGEVQLEIQRK 268
7tmB2_GPR97 cd15442
orphan adhesion receptor GPR97, member of the class B2 family of seven-transmembrane G ...
950-1217 2.14e-04

orphan adhesion receptor GPR97, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR97 is an orphan receptor that has been classified into the group VIII of adhesion GPCRs. Other members of the Group VII include GPR56, GPR64, GPR112, GPR114, and GPR126. GPR97 is identified as a lymphatic adhesion receptor that is specifically expressed in lymphatic endothelium, but not in blood vascular endothelium, and is shown to regulate migration of lymphatic endothelial cells via the small GTPases RhoA and cdc42. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320558 [Multi-domain]  Cd Length: 277  Bit Score: 45.17  E-value: 2.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  950 VGCGVSSLTLLMLVIIYVSV---WRYIRSERSV-ILINFCLSIISSNA--LILIGQTQTRNKVVCTLVAAFLHFFFLSSF 1023
Cdd:cd15442     10 AGCGVSMVFLIFTIILYFFLrftYQKFKSEDAPkIHVNLSSSLLLLNLafLLNSGVSSRAHPGLCKALGGVTHYFLLCCF 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1024 CWVLTEAWQSYMAVTgHLRNRLIRKRF--LCL-GWGLPALVVAISvGFTKAKGY---------STMNYCWLSlEGGLLYA 1091
Cdd:cd15442     90 TWMAIEAFHLYLLAI-KVFNTYIHHYFakLCLvGWGFPALVVTIT-GSINSYGAytimdmanrTTLHLCWIN-SKHLTVH 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1092 FV---GPAAAVVLVNMVIGILVFNKLVSKDGITdkklkeragqpsphplgralkcaecgvlsAADATSDATSNAMASLWS 1168
Cdd:cd15442    167 YItvcGYFGLTFLFNTVVLGLVAWKIFHLQSAT-----------------------------AGKEKCQAWKGGLTVLGL 217
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1034661056 1169 SCvvlpLLALTWMSAVLAVTDrRSALFQILFAVFDSLEGFVIVMVHCIL 1217
Cdd:cd15442    218 SC----LLGVTWGLAFFTYGS-MSVPTVYIFALLNSLQGLFIFIWFVIL 261
7tmB1_Secretin_R-like cd15930
secretin receptor-like group of hormone receptors, member of the class B family of ...
945-1226 2.25e-04

secretin receptor-like group of hormone receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; This group represents G protein-coupled receptors for structurally similar peptide hormones that include secretin, growth-hormone-releasing hormone (GHRH), pituitary adenylate cyclase activating polypeptide (PACAP), and vasoactive intestinal peptide (VIP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. Secretin, a polypeptide secreted by entero-endocrine S cells in the small intestine, is involved in maintaining body fluid balance. This polypeptide regulates the secretion of bile and bicarbonate into the duodenum from the pancreatic and biliary ducts, as well as regulates the duodenal pH by the control of gastric acid secretion. Studies with secretin receptor-null mice indicate that secretin plays a role in regulating renal water reabsorption. Secretin mediates its biological actions by elevating intracellular cAMP via G protein-coupled secretin receptors, which are expressed in the brain, pancreas, stomach, kidney, and liver. GHRHR is a specific receptor for the growth hormone-releasing hormone (GHRH) that controls the synthesis and release of growth hormone (GH) from the anterior pituitary somatotrophs. Mutations in the gene encoding GHRHR have been connected to isolated growth hormone deficiency (IGHD), a short-stature condition caused by deficient production of GH or lack of GH action. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. All B1 subfamily GPCRs are able to increase intracellular cAMP levels by coupling to adenylate cyclase via a stimulatory Gs protein. However, depending on its cellular location, some members of subfamily B1 are also capable of coupling to additional G proteins such as G(i/o) and/or G(q) proteins, thereby leading to activation of phospholipase C and intracellular calcium influx.


Pssm-ID: 320596 [Multi-domain]  Cd Length: 268  Bit Score: 45.12  E-value: 2.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  945 SVTLIVGCGVS-SLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQT----------QTRNKVVCTLVAA 1013
Cdd:cd15930      3 TVKIIYTVGYSlSLTSLTTAMIILCLFRKLHCTRNYIHMNLFVSFILRAIAVFIKDAvlfssedvdhCFVSTVGCKASMV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1014 FLHFFFLSSFCWVLTEAWQSYMAVTGHLRNRliRKRF---LCLGWGLPALVVAIsvgFTKAKGYSTMNYCW-LSLEGGLL 1089
Cdd:cd15930     83 FFQYCVMANFFWLLVEGLYLHTLLVISFFSE--RRYFwwyVLIGWGAPTVFVTV---WIVARLYFEDTGCWdINDESPYW 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1090 YAFVGPAAAVVLVNMVIGILVFNKLVSKdgitdkklkeragqpsphplgralkcaecgvLSAADATSDATSNAMASLWSS 1169
Cdd:cd15930    158 WIIKGPILISILVNFVLFINIIRILLQK-------------------------------LRSPDIGGNESSQYKRLARST 206
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034661056 1170 CVVLPLLALTWMsaVLAVT-DRRSALFQILFA-VFDSLEGFVIVMVHCILRREVQDAVK 1226
Cdd:cd15930    207 LLLIPLFGIHYI--VFAFFpENISLGIRLYFElCLGSFQGFVVAVLYCFLNGEVQAEIK 263
7tmB1_PTH-R_related cd15272
invertebrate parathyroid hormone-related receptors, member of the class B family of ...
943-1226 2.36e-04

invertebrate parathyroid hormone-related receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; This group includes parathyroid hormone (PTH)-related receptors found in invertebrates such as mollusks and annelid worms. The PTH family receptors are members of the B1 subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. The parathyroid hormone type 1 receptor (PTH1R) is found in all vertebrate species and is activated by two polypeptide ligands: parathyroid hormone (PTH), an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH1R couples predominantly to G(s)- protein that in turn activates adenylyl cyclase thereby producing cAMP, but it can also couple to several G protein subtypes, including G(q/11), G(i/o), and G(12/13), resulting in activation of multiple signaling pathways.


Pssm-ID: 320400 [Multi-domain]  Cd Length: 285  Bit Score: 45.07  E-value: 2.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  943 LPSVTLI--VGCGVSSLTLLMLVIIyVSVWRYIRSERSVILINFCLSIISSNALILIGQ-------------TQTRNKVV 1007
Cdd:cd15272      1 LPSIRLMynIGYGLSLVSLLIAVII-MLYFKKLHCPRNTIHINLFVSFILRAVLSFIKEnllvqgvgfpgdvYYDSNGVI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1008 ----------CTLVAAFLHFFFLSSFCWVLTEAWQSYMAV---TGHLRNRLirKRFLCLGWGLPALVVAISVgFTKAKGY 1074
Cdd:cd15272     80 efkdegshweCKLFFTMFNYILGANYMWIFVEGLYLHMLIfvaVFSENSRV--KWYILLGWLSPLLFVLPWV-FVRATLE 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1075 STMnyCW-LSLEGGLLYAFVGPAAAVVLVNMVIGI----LVFNKLVSKDGITDKKLKERagqpsphplgralKCAEcgvl 1149
Cdd:cd15272    157 DTL--CWnTNTNKGYFWIIRGPIVISIAINFLFFInivrVLFTKLKASNTQESRPFRYR-------------KLAK---- 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1150 saadatsdatsnamaslwSSCVVLPLLALTWMSAVlAVTDRRSA-------LFQILFavFDSLEGFVIVMVHCILRREVQ 1222
Cdd:cd15272    218 ------------------STLVLIPLFGVHYMVFV-VLPDSMSSdeaelvwLYFEMF--FNSFQGFIVALLFCFLNGEVQ 276

                   ....
gi 1034661056 1223 DAVK 1226
Cdd:cd15272    277 SEIK 280
TSP1_CCN pfam19035
CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in ...
361-402 2.80e-04

CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in matricellular CCN proteins that have an alternative disulphide binding pattern compared to the canonical TSP1 domains.


Pssm-ID: 465952  Cd Length: 44  Bit Score: 40.01  E-value: 2.80e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1034661056  361 SPWSVCSSTCGEGWQTRTrfcvsSSYSTQCSgPLREQRLCNN 402
Cdd:pfam19035    6 TEWSPCSKTCGMGVSTRV-----SNDNAECK-LVTETRLCQL 41
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
417-461 4.09e-04

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 39.74  E-value: 4.09e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034661056  417 PWSLCSSTCGRGFRDRTRTCRPP----QFGGNPCEGPEK--QTKFCNIALC 461
Cdd:pfam19030    5 PWGECSVTCGGGVQTRLVQCVQKgggsIVPDSECSAQKKppETQSCNLKPC 55
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
267-287 5.21e-04

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 39.57  E-value: 5.21e-04
                           10        20
                   ....*....|....*....|.
gi 1034661056  267 WSLWGECTRDCGGGLQTRTRT 287
Cdd:pfam19028    6 WSEWSECSVTCGGGVQTRTRT 26
7tmB1_GLP2R cd15266
glucagon-like peptide-2 receptor, member of the class B family of seven-transmembrane G ...
956-1117 8.26e-04

glucagon-like peptide-2 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Glucagon-like peptide-2 receptor (GLP2R) is a member of the glucagon receptor family of G protein-coupled receptors, which also includes glucagon receptor (GCGR) and GLP1R. GLP2R is activated by glucagon-like peptide 2, which is derived from the large proglucagon precursor. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. GLP2R belongs to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320394 [Multi-domain]  Cd Length: 280  Bit Score: 43.20  E-value: 8.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  956 SLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNK--------------------VVCTLVAAFL 1015
Cdd:cd15266     15 SLISLSLALLILLLLRKLHCTRNYIHMNLFASFILRALAVLIKDIVLYSTyskrpddetgwisylseessTSCRVAQVFM 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1016 HFFFLSSFCWVLTEAWQSY-MAVTGHLRNRLIRKRFLCLGWGLPALVVaisVGFTKAKGYSTMNYCWLSLEG-GLLYAFV 1093
Cdd:cd15266     95 HYFVGANYFWLLVEGLYLHtLLVTAVLSERRLLKKYMLIGWGTPVLFV---VPWGVAKILLENTGCWGRNENmGIWWIIR 171
                          170       180
                   ....*....|....*....|....
gi 1034661056 1094 GPAAAVVLVNMVIGILVFNKLVSK 1117
Cdd:cd15266    172 GPILLCITVNFYIFLKILKLLLSK 195
7tmB1_PTH1R cd15984
parathyroid hormone 1 receptor, member of the class B family of seven-transmembrane G ...
1050-1226 9.30e-04

parathyroid hormone 1 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; The parathyroid hormone (PTH) receptor family has three subtypes: PTH1R, PTH2R and PTH3R. PTH1R is expressed in bone and kidney and is activated by two polypeptide ligands: PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH1R couples predominantly to G(s)-protein that in turn activates adenylate cyclase thereby producing cAMP, but it can also couple to several G protein subtypes, including G(q/11), G(i/o), and G(12/13), resulting in activation of multiple intracellular signaling pathways. PTH1R is found in all vertebrate species, whereas PTH2R is found in mammals and fish, but not in chicken or frog. PTH3R is found in chicken and fish, but it is absent in mammals. The PTH receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways.


Pssm-ID: 320650 [Multi-domain]  Cd Length: 290  Bit Score: 43.01  E-value: 9.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1050 FLCLGWGLPALVVAIsvgFTKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVVLVNMVIGILVFNKLVSKdgitdkkLKERa 1129
Cdd:cd15984    138 FTLFGWGLPAVFVTI---WASVRATLADTGCWDLSAGNLKWIIQVPILAAIVVNFILFINIVRVLATK-------LRET- 206
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1130 gqpsphplgRALKCaecgvlsaadatsDATSNAMASLWSSCVVLPLLALTWMS-AVLAVTDRRSALFQILF---AVFDSL 1205
Cdd:cd15984    207 ---------NAGRC-------------DTRQQYRKLLKSTLVLMPLFGVHYIVfMAMPYTEVSGILWQVQMhyeMLFNSF 264
                          170       180
                   ....*....|....*....|.
gi 1034661056 1206 EGFVIVMVHCILRREVQDAVK 1226
Cdd:cd15984    265 QGFFVAIIYCFCNGEVQAEIK 285
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
522-578 1.03e-03

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 38.59  E-value: 1.03e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034661056  522 WQAwASWGSCSVTCGAGSQRRERVCSGPffGGAACQGPQdeyrQCGTQRCPEPHEIC 578
Cdd:pfam19030    1 WVA-GPWGECSVTCGGGVQTRLVQCVQK--GGGSIVPDS----ECSAQKKPPETQSC 50
7tmB1_PDFR cd15261
The pigment dispersing factor receptor, member of the class B seven-transmembrane G ...
949-1227 1.34e-03

The pigment dispersing factor receptor, member of the class B seven-transmembrane G protein-coupled receptors; The pigment dispersing factor receptor (PDFR) is a G protein-coupled receptor that binds the circadian clock neuropeptide PDF, a functional ortholog of the mammalian vasoactive intestinal peptide (VIP), on the pacemaker neurons. The PDFR is implicated in regulating flight circuit development and in modulating acute flight In Drosophila melanogaster. The PDFR activation stimulates adenylate cyclase, thereby increasing cAMP levels in many different pacemakers, and the receptor signaling has been shown to regulate behavioral circadian rhythms and geotaxis in Drosophila. The PDFR belongs to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. . These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. They play key roles in hormone homeostasis in mammals and are promising drug targets in various human diseases including diabetes, osteoporosis, obesity, neurodegenerative conditions (Alzheimer###s and Parkinson's), cardiovascular disease, migraine, and psychiatric disorders (anxiety, depression).


Pssm-ID: 320389 [Multi-domain]  Cd Length: 282  Bit Score: 42.74  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  949 IVGCGVSSLTLLMLVIIYvSVWRYIRSERSVILINFCLSIISSNALIL---IGQTQTRNKVVCTLVA--AFLHFFFLSSF 1023
Cdd:cd15261      9 IVGLCLSLVSLIISLFIF-SYFRTLRNHRTRIHKNLFLAILLQVIIRLvlyIDQAITRSRGSHTNAAttEGRTINSTPIL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1024 C---WVLTEAWQS----YMAVTG-HLRNRLI---------RKRFLCLGWGLPALVVAISVGFTKAKgySTMNYCWLSleg 1086
Cdd:cd15261     88 CegfYVLLEYAKTvmfmWMFIEGlYLHNIIVvsvfsgkpnYLFYYILGWGIPIVHTSAWAIVTLIK--MKVNRCWFG--- 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1087 gllYAFV-------GPAAAVVLVNMVIGILVFNKLVSKdgitdkkLKErAGQPSPHPLGRALKcaecgvlsaadatsdat 1159
Cdd:cd15261    163 ---YYLTpyywileGPRLAVILINLFFLLNIIRVLVSK-------LRE-SHSREIEQVRKAVK----------------- 214
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034661056 1160 sNAMaslwsscVVLPLLALTWMSAVLAVTDRRSAlfqILFAVFD-------SLEGFVIVMVHCILRREVQDAVKC 1227
Cdd:cd15261    215 -AAI-------VLLPLLGITNILQMIPPPLTSVI---VGFAVWSysthfltSFQGFFVALIYCFLNGEVKNVLKK 278
TSP_1 pfam00090
Thrombospondin type 1 domain;
266-314 1.50e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 38.17  E-value: 1.50e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1034661056  266 LWSLWGECTRDCGGGLQTRTRTClPAPGVEGGGCEGVLEEGRQCNREAC 314
Cdd:pfam00090    2 PWSPWSPCSVTCGKGIQVRQRTC-KSPFPGGEPCTGDDIETQACKMDKC 49
7tmB2_GPR124 cd15998
G protein-coupled receptor 124, member of the class B2 family of seven-transmembrane G ...
954-1224 2.04e-03

G protein-coupled receptor 124, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR124 is an orphan receptor that has been classified as that belongs to the group III of adhesion GPCRs, which also includes orphan GPR123 and GPR125. GPR124, also known as tumor endothelial marker 5 (TEM5), is highly expressed in tumor vessels and in the vasculature of the developing embryo. GPR124 is essentially required for proper angiogenic sprouting into neural tissue, CNS-specific vascularization, and formation of the blood-brain barrier. GPR124 interacts with the PDZ domain of DLG1 (discs large homolog 1) through its PDZ-binding motif. Recently, studies of double-knockout mice showed that GPR124 functions as a co-activator of Wnt7a/Wnt7b-dependent beta-catenin signaling in brain endothelium. Moreover, WNT7-stimulated beta-catenin signaling is regulated by GPR124's intracellular PDZ binding motif and leucine-rich repeats (LRR) in its N-terminal extracellular domain. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320664 [Multi-domain]  Cd Length: 268  Bit Score: 41.87  E-value: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056  954 VSSLTLLMLVIIYVSVWRYIRSERSV--------ILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCW 1025
Cdd:cd15998      8 VYPCTALLLLCLFSTIITYILNHSSIhvsrkgwhMLLNLCFHIAMTSAVFAGGITLTNYQMVCQAVGITLHYSSLSTLLW 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1026 VLTEA--------WQSYMAVTGHLRNRLIRK--RFLCLGWGLPALVVAISVGFTKAKGYSTMNYCWLSLEGGlLYAFVGP 1095
Cdd:cd15998     88 MGVKArvlhkeltWRAPPPQEGDPALPTPRPmlRFYLIAGGIPLIICGITAAVNIHNYRDHSPYCWLVWRPS-LGAFYIP 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1096 AAAVVLVNMVIGIlvfnklvskdgitdkklkeragqpsphplgralkCAecGV-LSAADATSDATSNAMASLWSSCVVLP 1174
Cdd:cd15998    167 VALILLVTWIYFL----------------------------------CA--GLhLRGPSADGDSVYSPGVQLGALVTTHF 210
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034661056 1175 LLALTWMSAVLAVTDR--RSALFQILFAVFDSLEGFVIVMVHCILRREVQDA 1224
Cdd:cd15998    211 LYLAMWACGALAVSQRwlPRVVCSCLYGVAASALGLFVFTHHCARRRDVRAS 262
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
270-288 5.35e-03

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 36.66  E-value: 5.35e-03
                           10
                   ....*....|....*....
gi 1034661056  270 WGECTRDCGGGLQTRTRTC 288
Cdd:pfam19030    6 WGECSVTCGGGVQTRLVQC 24
7tmB1_PTHR cd15265
parathyroid hormone receptors, member of the class B family of seven-transmembrane G ...
1049-1226 6.97e-03

parathyroid hormone receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; The parathyroid hormone (PTH) receptor family has three subtypes: PTH1R, PTH2R and PTH3R. PTH1R is expressed in bone and kidney and is activated by two polypeptide ligands: PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH1R couples predominantly to a G(s)-protein that in turn activates adenylate cyclase thereby producing cAMP, but it can also couple to several G protein subtypes, including G(q/11), G(i/o), and G(12/13), resulting in activation of multiple intracellular signaling pathways. PTH2R is potently activated by tuberoinfundibular peptide-39 (TIP-39), but not by PTHrP. PTH also strongly activates human PTH2R, but only weakly activates rat and zebrafish PTH2Rs, suggesting that TIP-39 is a natural ligand for PTH2R. On the other hand, PTH3R binds and responds to both PTH and PTHrP, but not the TIP-39. Moreover, the PTH3R is more closely related to the PTH1R than PTH2R. PTH1R is found in all vertebrate species, whereas PTH2R is found in mammals and fish, but not in chicken or frog. The PTH3R is found in chicken and fish, but it is absent in mammals. The PTH receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways.


Pssm-ID: 320393 [Multi-domain]  Cd Length: 289  Bit Score: 40.44  E-value: 6.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1049 RFLCLGWGLPALVVAI--SVGFTKAKgystmNYCWLSLEGGLLYAFVGPAAAVVLVNMVIGILVFNKLVSKdgitdkkLK 1126
Cdd:cd15265    137 GFTLIGWGFPAVFVIPwaSVRATLAD-----TRCWDLSAGNYKWIYQVPILAAIVVNFILFLNIVRVLATK-------LR 204
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034661056 1127 ER-AGQPSPHPLGRALkcaecgvlsaadatsdatsnamasLWSSCVVLPLLALTWMSAVLAVTDRRSALFQI-----LFa 1200
Cdd:cd15265    205 ETnAGRCDTRQQYRKL------------------------AKSTLVLIPLFGVHYIVFMGMPYTEVGLLWQIrmhyeLF- 259
                          170       180
                   ....*....|....*....|....*.
gi 1034661056 1201 vFDSLEGFVIVMVHCILRREVQDAVK 1226
Cdd:cd15265    260 -FNSFQGFFVAIIYCFCNGEVQAEIK 284
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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