juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein 4 (Notch4) and similar proteins; Neurogenic locus notch homolog protein 4 (Notch4) functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. It affects the implementation of differentiation, proliferation and apoptotic programs. This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of Notch4, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958757745 1436 SPATRLPWPILCSPVVGVLLLALGALLVLQLIRRRRREHGALWLPPGFIRRPQTQqaPHRRRPPLGEDNIGLKALK 1511
Cdd:cd21705     19 LVAAQLPWPLVCSSVAGVLALVLGALLGVQLIRRRQREHGALWLPPGFARHRDPN--PHRRREPVGEDAIGLKPLK 92

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958757745  429 DLDECQMaqqgPSPCEHGGSCINTPGSFNCLCLPGYTGSRCE 470
Cdd:cd00054      1 DIDECAS----GNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1958757745 1207 WKGCPPhSQCWLLFRDGRCHPQCDSEECLFDGYDCE 1242
Cdd:pfam00066    1 WPNCPY-PYCWDKFGNGVCDEECNNAECLWDGGDCS 35

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1958757745  966 DACQSG-PCHNHGTCTPRPGGFHCACPPGFVGLRCE 1000
Cdd:cd00054      3 DECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1958757745  311 DIDECEAQGPprCRNGGTCQNSAGGFHCVCVSGWGGEGC 349
Cdd:cd00054      1 DIDECASGNP--CQNGGTCVNTVGSYRCSCPPGYTGRNC 37

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                           10        20        30
                   ....*....|....*....|....*....|...
gi 1958757745  892 EISNLCQNGGLCIDTGSSYFCRCPPGFEGKLCQ 924
Cdd:cd00054      6 ASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1958757745  588 DECRS-DPCPVGASCLDLPGAFLCLCRPGFTGQLCE 622
Cdd:cd00054      3 DECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958757745  765 VDHCASAS-CLNGGTCMSKPGTFFCHCATGFQGLHCE 800
Cdd:cd00054      2 IDECASGNpCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                           10        20        30
                   ....*....|....*....|....*....|
gi 1958757745  810 NPCRNKATCQDTPRGARCLCSPGYTGSSCQ 839
Cdd:cd00054      9 NPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958757745  352 NLDDCAAAT-CALGSTCIDRVGSFSCLCPPGRTGLLC 387
Cdd:cd00054      1 DIDECASGNpCQNGGTCVNTVGSYRCSCPPGYTGRNC 37

juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein 4 (Notch4) and similar proteins; Neurogenic locus notch homolog protein 4 (Notch4) functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. It affects the implementation of differentiation, proliferation and apoptotic programs. This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of Notch4, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958757745 1436 SPATRLPWPILCSPVVGVLLLALGALLVLQLIRRRRREHGALWLPPGFIRRPQTQqaPHRRRPPLGEDNIGLKALK 1511
Cdd:cd21705     19 LVAAQLPWPLVCSSVAGVLALVLGALLGVQLIRRRQREHGALWLPPGFARHRDPN--PHRRREPVGEDAIGLKPLK 92

ankyrin repeat protein; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757745 1626 GETPLHLAARFSRPTAARRLLEAGANPNQPDRAGRTPLHTAVAADaREVCQLLLASRqtAVDARTDDGTTPLMLAARLAV 1705
Cdd:PHA02874   190 GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN-RSAIELLINNA--SINDQDIDGSTPLHHAINPPC 266

                           90       100
                   ....*....|....*....|....*...
gi 1958757745 1706 E-DLVEELIAARADVGARDKRGQNPWET 1732
Cdd:PHA02874   267 DiDIIDILLYHKADISIKDNKGENPIDT 294

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958757745  429 DLDECQMaqqgPSPCEHGGSCINTPGSFNCLCLPGYTGSRCE 470
Cdd:cd00054      1 DIDECAS----GNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1958757745  548 DMDECSSA-PCANGGHCQDQPGAFHCECLPGFEGPRCE 584
Cdd:cd00054      1 DIDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1958757745 1207 WKGCPPhSQCWLLFRDGRCHPQCDSEECLFDGYDCE 1242
Cdd:pfam00066    1 WPNCPY-PYCWDKFGNGVCDEECNNAECLWDGGDCS 35

Domain found in Notch and Lin-12; The Notch protein is essential for the proper differentiation of the Drosophila ectoderm. This protein contains 3 NL domains.

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1958757745  1203 VPDPWKGCPpHSQCWLLFRDGRCHPQCDSEECLFDGYDC 1241
Cdd:smart00004    1 PQDPWSRCE-DAQCWDKFGDGVCDEECNNAECLWDGGDC 38

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958757745  511 INECAS-NPCLNQAACHDQLNGFLCLCLPGFTGARCE 546
Cdd:cd00054      2 IDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1958757745  311 DIDECEAQGPprCRNGGTCQNSAGGFHCVCVSGWGGEGC 349
Cdd:cd00054      1 DIDECASGNP--CQNGGTCVNTVGSYRCSCPPGYTGRNC 37

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757745 1627 ETPLHLAARFSRPTAARRLLE-AGANPNQPDRAGRTPLHTAVAADAREVCQLLL-ASRQTAVDARTDD---GTTPLMLAA 1701
Cdd:cd22192     18 ESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeAAPELVNEPMTSDlyqGETALHIAV 97

                           90
                   ....*....|....*...
gi 1958757745 1702 RLAVEDLVEELIAARADV 1719
Cdd:cd22192     98 VNQNLNLVRELIARGADV 115

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                           10        20        30
                   ....*....|....*....|....*....|...
gi 1958757745  892 EISNLCQNGGLCIDTGSSYFCRCPPGFEGKLCQ 924
Cdd:cd00054      6 ASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1958757745  472 DHNECLSQ-PCHPGSTCLDLLATFQCLCPPGLEGRLCE 508
Cdd:cd00054      1 DIDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1958757745   510 EINECAS-NPCLNQAACHDQLNGFLCLCLPGFT-GARCE 546
Cdd:smart00179    1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1958757745   966 DACQS-GPCHNHGTCTPRPGGFHCACPPGFV-GLRCE 1000
Cdd:smart00179    3 DECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1958757745   927 VNPCTSK-PCLHGATCVPQPNGYVCQCAPGYE-GQNC 961
Cdd:smart00179    2 IDECASGnPCQNGGTCVNTVGSYRCECPPGYTdGRNC 38

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958757745  765 VDHCASAS-CLNGGTCMSKPGTFFCHCATGFQGLHCE 800
Cdd:cd00054      2 IDECASGNpCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958757745 1002 DVDECLDR-PCHPSGTasCHSLANAFYCQCLPGHTGQRCE 1040
Cdd:cd00054      1 DIDECASGnPCQNGGT--CVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....
gi 1958757745   892 EISNLCQNGGLCIDTGSSYFCRCPPGFE-GKLCQ 924
Cdd:smart00179    6 ASGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                           10        20
                   ....*....|....*....|....*...
gi 1958757745  696 PCAHGGTCHPQPSGYNCSCLAGYTGLTC 723
Cdd:cd00054     10 PCQNGGTCVNTVGSYRCSCPPGYTGRNC 37

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1958757745  429 DLDECQmaqQGPSPCEHGGSCINTPGSFNCLCLPG 463
Cdd:pfam07645    1 DVDECA---TGTHNCPANTVCVNTIGSFECRCPDG 32

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958757745  352 NLDDCAAAT-CALGSTCIDRVGSFSCLCPPGRTGLLC 387
Cdd:cd00054      1 DIDECASGNpCQNGGTCVNTVGSYRCSCPPGYTGRNC 37

Ankyrin repeat [Signal transduction mechanisms];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757745 1571 DSDTCGPDGVTPLMSAVFCGgvQSTTVQRLglgnpepweplLDRGACPQAHTvGTGETPLHLAARFSRPTAARRLLEAGA 1650
Cdd:COG0666    112 DVNARDKDGETPLHLAAYNG--NLEIVKLL-----------LEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEAGA 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757745 1651 NPNQPDRAGRTPLHTAVAADAREVCQLLLAsrQTA-VDARTDDGTTPLMLAARLAVEDLVEELIAARADVGARDKRGQNP 1729
Cdd:COG0666    178 DVNARDNDGETPLHLAAENGHLEIVKLLLE--AGAdVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255

Ankyrin repeat [Signal transduction mechanisms];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757745 1611 LLDRGACPQAHTVGTGETPLHLAARFSRPTAARRLLEAGANPNQPDRAGRTPLHTAVAADAREVCQLLLAsRQTAVDART 1690
Cdd:COG0666     72 LLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-AGADVNAQD 150

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958757745 1691 DDGTTPLMLAARLAVEDLVEELIAARADVGARDKRGQNP 1729
Cdd:COG0666    151 NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189

Ankyrin repeats (3 copies);

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757745 1630 LHLAARFSRPTAARRLLEAGANPNQPDRAGRTPLHTAVAADAREVCQLLLASRQTAVDartDDGTTPLMLAARLAVEDLV 1709
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK---DNGRTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 1958757745 1710 EELIAARADVGARD 1723
Cdd:pfam12796   78 KLLLEKGADINVKD 91

juxtamembrane and transmembrane (JMTM) domain found in Notch protein family; Neurogenic locus notch homolog (Notch) proteins are a family of type-1 transmembrane proteins that form a core component of the Notch signaling pathway. They operate in a variety of different tissues and play a role in a variety of developmental processes by controlling cell fate decisions. The model corresponds to the juxtamembrane and transmembrane (JMTM) domain of Notch proteins, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958757745 1466 LIRRRRREHGALWLPPGFIRRPQTQqaPHRRRPPLGEDNIGLKAL 1510
Cdd:cd21701     43 LVARKRRRHGTLWFPEGFPRTRASR--RSRRRDPVGQDSVGLKNL 85

juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein 2 (Notch2) and similar proteins; Neurogenic locus notch homolog protein 2 (Notch2) functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Notch2 is involved in bone remodeling and homeostasis. In collaboration with RELA/p65, it enhances NFATc1 promoter activity and positively regulates RANKL-induced osteoclast differentiation. Notch2 positively regulates self-renewal of liver cancer cells. This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of Notch2, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958757745 1466 LIRRRRREHGALWLPPGFIRRPQTQQapHRRRPPLGEDNIGLKAL 1510
Cdd:cd21703     40 LVAKRKRKHGPLWFPEGFILNKENSN--RKRREPVGQDAVGMKNL 82

ankyrin repeat protein; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757745 1626 GETPLHLAARFSRPTAARRLLEAGANPNQPDRAGRTPLHTAVAADaREVCQLLLASRqtAVDARTDDGTTPLMLAARLAV 1705
Cdd:PHA02874   190 GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN-RSAIELLINNA--SINDQDIDGSTPLHHAINPPC 266

                           90       100
                   ....*....|....*....|....*...
gi 1958757745 1706 E-DLVEELIAARADVGARDKRGQNPWET 1732
Cdd:PHA02874   267 DiDIIDILLYHKADISIKDNKGENPIDT 294

ankyrin-like protein; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757745 1612 LDRGACPQAHTVGTGETPLHLAARFS--RPTAARRLLEAGANPNQPDRAGRTPLHTAVAADAREVCQLLLAsrQTA-VDA 1688
Cdd:PHA03095   208 LIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIA--LGAdINA 285

                           90
                   ....*....|....
gi 1958757745 1689 RTDDGTTPLMLAAR 1702
Cdd:PHA03095   286 VSSDGNTPLSLMVR 299

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958757745 1245 PTCTPAYdqyCRDHFHNGHCEKGCNNAQCGWDGGDCR 1281
Cdd:pfam00066    2 PNCPYPY---CWDKFGNGVCDEECNNAECLWDGGDCS 35

ankyrin repeat protein; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757745 1611 LLDRGACPQAHTVGTGETPLHLAARFSRPTAARRLLEAGANPNQPDRAGRTPLHTAVAADAREVCQLLLASrQTAVDART 1690
Cdd:PHA02878   153 LLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN-GASTDARD 231

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958757745 1691 DDGTTPLMLA-ARLAVEDLVEELIAARADVGAR 1722
Cdd:PHA02878   232 KCGNTPLHISvGYCKDYDILKLLLEHGVDVNAK 264

ankyrin-like protein; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757745 1643 RRLLEAGANPNQPDRAGRTPLHTAVA---ADAREVCQLLLASrQTAVDARTDDGTTPLMLAARLA-VEDLVEELIAARAD 1718
Cdd:PHA03095    31 RRLLAAGADVNFRGEYGKTPLHLYLHyssEKVKDIVRLLLEA-GADVNAPERCGFTPLHLYLYNAtTLDVIKLLIKAGAD 109

                           90
                   ....*....|.
gi 1958757745 1719 VGARDKRGQNP 1729
Cdd:PHA03095   110 VNAKDKVGRTP 120

juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein 3 (Notch3) and similar proteins; Neurogenic locus notch homolog protein 3 (Notch3) functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. The model corresponds to the juxtamembrane and transmembrane (JMTM) domain of Notch3, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958757745 1466 LIRRRRREHGALWLPPGFIRRPQTqqAPHRRRPPLGEDNIGLK 1508
Cdd:cd21704     46 LVARRKREHSTLWFPEGFFLKKES--SNKNRREPVGQDALGMK 86