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Conserved domains on  [gi|1189690239|ref|NP_001337049|]
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semaphorin-3C isoform 1 [Homo sapiens]

Protein Classification

Sema_3C and Ig_Sema3 domain-containing protein( domain architecture ID 10181345)

protein containing domains Sema_3C, PSI, and Ig_Sema3

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Sema_3C cd11251
The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted ...
63-532 0e+00

The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted semaphorin expressed in and adjacent to cardiac neural crest cells, and causes impaired migration of neural crest cells to the developing cardiac outflow tract, resulting in the interruption of the aortic arch and persistent truncus arteriosus. It has been proposed that Sema3C acts as a guidance molecule, regulating migration of neural crest cells that express semaphorin receptors such as plexin A2. Sema3C may also participate in tumor progression. The cleavage of Sema3C induced by ADAMTS1 promotes the migration of breast cancer cells. Sema3C is a member of the class 3 semaphorin family of secreted proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


:

Pssm-ID: 200512 [Multi-domain]  Cd Length: 470  Bit Score: 1039.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  63 FSLSHHPLDYRILLMDEDQDRIYVGSKDHILSLNINNISQEALSVFWPASTIKVEECKMAGKDPTHGCGNFVRVIQTFNR 142
Cdd:cd11251     1 YSLSERPLDYRILFMDEDQDRIYVGSKDHILSLNINNISQDALSIFWPASASKVEECKMAGKDPTHGCGNFVRVIQPYNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 143 THLYVCGSGAFSPVCTYLNRGRRSEDQVFMIDSKCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTK 222
Cdd:cd11251    81 THLYVCGSGAFSPVCVYVNRGRRSEEQVFHIDSKAESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 223 RNAVRTDQHNSKWLSEPMFVDAHVIPDGTDPNDAKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTFL 302
Cdd:cd11251   161 RNAVRTDQHNSKWLSEPIFVDAHLIPDGTDPNDAKLYFFLKERLTDNSGSTKQIHSMIARVCPNDTGGQRSLVNKWTTFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 303 KARLVCSVTDEDGPETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNHQLI 382
Cdd:cd11251   241 KARLVCSVMDEDGTETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHMSDIQTVFNGPFAHKEGPNHQLI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 383 SYQGRIPYPRPGTCPGGAFTPNMRTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDYKYTKIAVDRVNAADGRY 462
Cdd:cd11251   321 AYQGRIPYPRPGTCPGGAFTPNMQSTKEFPDDVVTFIRNHPLMFNPIYPIGRRPLLVRTGTDYKYTKIAVDRVNAADGRY 400
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 463 HVLFLGTDRGTVQKVVVLPTNNSVSGELILEELEVFKNHAPITTMKISSKKQQLYVSSNEGVSQVSLHRC 532
Cdd:cd11251   401 HVLFLGTDKGTVQKVVVLPTNGSLSGELILEELEVFKNHAPITNMKISSKKQQLYVSSEEGISQVSLHRC 470
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
592-682 1.81e-43

Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed of the immunoglobulin (Ig)-like domain of Sema3 and similar proteins. Semaphorins are classified based on structural features additional to the Sema domain. Sema3 is a Class III semaphorin that is secreted. It is a vertebrate class having a Sema domain, an Ig domain, a short basic domain. They have been shown to be axonal guidance cues and have a part in the regulation of the cardiovascular, immune, and respiratory systems. Sema3A, the prototype member of this class III subfamily, induces growth cone collapse and is an inhibitor of axonal sprouting. In perinatal rat cortex, it acts as a chemoattractant and functions to direct the orientated extension of apical dendrites. It may play a role, prior to the development of apical dendrites, in signaling the radial migration of newborn cortical neurons towards the upper layers. Sema3A selectively inhibits vascular endothelial growth factor receptor (VEGF)-induced angiogenesis and induces microvascular permeability. This group also includes Sema3B, -C, -D, -E, -G.


:

Pssm-ID: 409455  Cd Length: 92  Bit Score: 151.73  E-value: 1.81e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 592 NAAEIVQYGVKNNTTFLECAPKSPQASIKWLLQKDKDRRK-EVKLNERIIATSQGLLIRSVQGSDQGLYHCIATENSFKQ 670
Cdd:cd05871     1 NAEEKVVYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKeEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQ 80
                          90
                  ....*....|..
gi 1189690239 671 TIAKINFKVLDS 682
Cdd:cd05871    81 TLVKIRLHVIEP 92
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
531-568 1.40e-07

domain found in Plexins, Semaphorins and Integrins;


:

Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 48.31  E-value: 1.40e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1189690239  531 RCHIYGTaCADCCLARDPYCAWD--GHSCSRFYPTGKRRS 568
Cdd:smart00423   1 RCSKYTS-CSECLLARDPYCAWCssQGRCTSGERCDSRRQ 39
 
Name Accession Description Interval E-value
Sema_3C cd11251
The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted ...
63-532 0e+00

The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted semaphorin expressed in and adjacent to cardiac neural crest cells, and causes impaired migration of neural crest cells to the developing cardiac outflow tract, resulting in the interruption of the aortic arch and persistent truncus arteriosus. It has been proposed that Sema3C acts as a guidance molecule, regulating migration of neural crest cells that express semaphorin receptors such as plexin A2. Sema3C may also participate in tumor progression. The cleavage of Sema3C induced by ADAMTS1 promotes the migration of breast cancer cells. Sema3C is a member of the class 3 semaphorin family of secreted proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200512 [Multi-domain]  Cd Length: 470  Bit Score: 1039.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  63 FSLSHHPLDYRILLMDEDQDRIYVGSKDHILSLNINNISQEALSVFWPASTIKVEECKMAGKDPTHGCGNFVRVIQTFNR 142
Cdd:cd11251     1 YSLSERPLDYRILFMDEDQDRIYVGSKDHILSLNINNISQDALSIFWPASASKVEECKMAGKDPTHGCGNFVRVIQPYNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 143 THLYVCGSGAFSPVCTYLNRGRRSEDQVFMIDSKCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTK 222
Cdd:cd11251    81 THLYVCGSGAFSPVCVYVNRGRRSEEQVFHIDSKAESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 223 RNAVRTDQHNSKWLSEPMFVDAHVIPDGTDPNDAKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTFL 302
Cdd:cd11251   161 RNAVRTDQHNSKWLSEPIFVDAHLIPDGTDPNDAKLYFFLKERLTDNSGSTKQIHSMIARVCPNDTGGQRSLVNKWTTFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 303 KARLVCSVTDEDGPETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNHQLI 382
Cdd:cd11251   241 KARLVCSVMDEDGTETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHMSDIQTVFNGPFAHKEGPNHQLI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 383 SYQGRIPYPRPGTCPGGAFTPNMRTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDYKYTKIAVDRVNAADGRY 462
Cdd:cd11251   321 AYQGRIPYPRPGTCPGGAFTPNMQSTKEFPDDVVTFIRNHPLMFNPIYPIGRRPLLVRTGTDYKYTKIAVDRVNAADGRY 400
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 463 HVLFLGTDRGTVQKVVVLPTNNSVSGELILEELEVFKNHAPITTMKISSKKQQLYVSSNEGVSQVSLHRC 532
Cdd:cd11251   401 HVLFLGTDKGTVQKVVVLPTNGSLSGELILEELEVFKNHAPITNMKISSKKQQLYVSSEEGISQVSLHRC 470
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
74-511 1.08e-157

Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and transmembrane proteins, some of which function as repellent signals during axon guidance. Sema domains also occur in the hepatocyte growth factor receptor and plexin-A3.


Pssm-ID: 426245 [Multi-domain]  Cd Length: 364  Bit Score: 462.16  E-value: 1.08e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  74 ILLMDEDQDRIYVGSKDHILSLNINNISQeaLSVFWPASTIKVEECKMAGKDPThGCGNFVRVIQTFNRTHLYVCGSGAF 153
Cdd:pfam01403   1 TLLLDEDSGRLYVGARNALYALNLDNLSL--LQEKQTGPEEDREECRPKGKDET-ECANYIRVLQPLNDTHLYVCGTNAF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 154 SPVCTYLNrgrrsedqvfMIDSKCESGKGRCSFNPNVNTVSVM-INEELFSGMYIDFMGTDAAIfRSLTKRNAVRTDQHN 232
Cdd:pfam01403  78 QPLCAYIR----------LEDEHYESGKGKCPFDPSQNSTAVVvVDGELYSGTSIDFLGSDPVI-RSLGSRPSLRTEQYD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 233 SKWLSEPMFVDAHVIPDgtdpndaKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTFLKARLVCSVtd 312
Cdd:pfam01403 147 SKWLNEPNFVSSFEIGD-------SVYFFFRETAVEYDFCGKAVVSRVARVCKNDVGGQRTLQKKWTSFLKARLVCSV-- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 313 eDGPETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFngpfahkegpnhqlisyqgripypr 392
Cdd:pfam01403 218 -PGVEGYFNELQDVFLLGISDWKDTVLYGVFTTQSNSIGGSAVCAFSLSDINEVF------------------------- 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 393 pgtcpggaftpnmrttkefpdDVVTFIRNHPLMYNSIYPIHKRPLIVRigTDYKYTKIAVDRVNAADGRYHVLFLGTDRG 472
Cdd:pfam01403 272 ---------------------KVLNFVKDHPLMDEAVPPPGGRPLLVR--RDVRLTRIAVDRVQADGGTYTVLFLGTDDG 328
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1189690239 473 TVQKVVVLPTNNsvsGELILEELEVFKNHAPITTMKISS 511
Cdd:pfam01403 329 RLHKVVVLGSEN---EAHIIEEIQVFPEPQPVLNLLLSS 364
Sema smart00630
semaphorin domain;
72-504 1.35e-155

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 457.60  E-value: 1.35e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239   72 YRILLMDEDQDRIYVGSKDHILSLNINNISQEALSVFWPASTIKVEECKMAGKDPTHGCGNFVRVIQTFNRTHLYVCGSG 151
Cdd:smart00630   1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAELKTGPVLSSPDCEECVSKGKDPPTDCVNYIRLLLDYNEDRLLVCGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  152 AFSPVCTYLNRGrrsedqvfmidskcesgkgrcsfnpnvntvsvmineELFSGMYIDFMGTDAAIFRSLTKRNAV----- 226
Cdd:smart00630  81 AFQPVCRLRNLG------------------------------------ELYVGTVADFSGSDPAIPRSLSVRRLKgtsgv 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  227 --RTDQHNSKWLSEPMFVDAHVIpdgtdpnDAKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTFLKA 304
Cdd:smart00630 125 slRTVLYDSKWLNEPNFVYAFES-------GDFVYFFFRETAVEDDNCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKA 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  305 RLVCSVTDEDGpeTHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNHQLISY 384
Cdd:smart00630 198 RLECSVPGEDP--FYFNELQAAFLLPPGSESDDVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLPY 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  385 -QGRIPYPRPGTCPGGAFtpnmrTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDYKYTKIAVDRVNaADGRYH 463
Cdd:smart00630 276 sRGKVPYPRPGTCPNKPP-----SSKDLPDETLNFIKSHPLMDEVVQPLTGRPLFVKTDSNYLLTSIAVDRVA-TDGNYT 349
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1189690239  464 VLFLGTDRGTVQKVVVLPTNNSVSgELILEELEVFKNHAPI 504
Cdd:smart00630 350 VLFLGTSDGRILKVVLSESSSSSE-SVVLEEISVFPDGSPI 389
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
592-682 1.81e-43

Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed of the immunoglobulin (Ig)-like domain of Sema3 and similar proteins. Semaphorins are classified based on structural features additional to the Sema domain. Sema3 is a Class III semaphorin that is secreted. It is a vertebrate class having a Sema domain, an Ig domain, a short basic domain. They have been shown to be axonal guidance cues and have a part in the regulation of the cardiovascular, immune, and respiratory systems. Sema3A, the prototype member of this class III subfamily, induces growth cone collapse and is an inhibitor of axonal sprouting. In perinatal rat cortex, it acts as a chemoattractant and functions to direct the orientated extension of apical dendrites. It may play a role, prior to the development of apical dendrites, in signaling the radial migration of newborn cortical neurons towards the upper layers. Sema3A selectively inhibits vascular endothelial growth factor receptor (VEGF)-induced angiogenesis and induces microvascular permeability. This group also includes Sema3B, -C, -D, -E, -G.


Pssm-ID: 409455  Cd Length: 92  Bit Score: 151.73  E-value: 1.81e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 592 NAAEIVQYGVKNNTTFLECAPKSPQASIKWLLQKDKDRRK-EVKLNERIIATSQGLLIRSVQGSDQGLYHCIATENSFKQ 670
Cdd:cd05871     1 NAEEKVVYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKeEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQ 80
                          90
                  ....*....|..
gi 1189690239 671 TIAKINFKVLDS 682
Cdd:cd05871    81 TLVKIRLHVIEP 92
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
531-568 1.40e-07

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 48.31  E-value: 1.40e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1189690239  531 RCHIYGTaCADCCLARDPYCAWD--GHSCSRFYPTGKRRS 568
Cdd:smart00423   1 RCSKYTS-CSECLLARDPYCAWCssQGRCTSGERCDSRRQ 39
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
608-671 8.15e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 41.72  E-value: 8.15e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189690239  608 LEC-APKSPQASIKWLlqkdKDRRKEVKLNERIIATSQG----LLIRSVQGSDQGLYHCIATENSFKQT 671
Cdd:smart00410  14 LSCeASGSPPPEVTWY----KQGGKLLAESGRFSVSRSGststLTISNVTPEDSGTYTCAATNSSGSAS 78
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
531-560 4.10e-04

Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas shows 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 38.84  E-value: 4.10e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1189690239 531 RCHIYGTaCADCCLARDPYCAWD--GHSCSRF 560
Cdd:pfam01437   1 RCSQYTS-CSSCLAARDPYCGWCssEGRCVRR 31
I-set pfam07679
Immunoglobulin I-set domain;
605-679 4.73e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 39.55  E-value: 4.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 605 TTFLECAPK-SPQASIKWLlqkdKDRrKEVKLNERIIATSQG----LLIRSVQGSDQGLYHCIATeNSFKQTIAKINFKV 679
Cdd:pfam07679  17 SARFTCTVTgTPDPEVSWF----KDG-QPLRSSDRFKVTYEGgtytLTISNVQPDDSGKYTCVAT-NSAGEAEASAELTV 90
 
Name Accession Description Interval E-value
Sema_3C cd11251
The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted ...
63-532 0e+00

The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted semaphorin expressed in and adjacent to cardiac neural crest cells, and causes impaired migration of neural crest cells to the developing cardiac outflow tract, resulting in the interruption of the aortic arch and persistent truncus arteriosus. It has been proposed that Sema3C acts as a guidance molecule, regulating migration of neural crest cells that express semaphorin receptors such as plexin A2. Sema3C may also participate in tumor progression. The cleavage of Sema3C induced by ADAMTS1 promotes the migration of breast cancer cells. Sema3C is a member of the class 3 semaphorin family of secreted proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200512 [Multi-domain]  Cd Length: 470  Bit Score: 1039.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  63 FSLSHHPLDYRILLMDEDQDRIYVGSKDHILSLNINNISQEALSVFWPASTIKVEECKMAGKDPTHGCGNFVRVIQTFNR 142
Cdd:cd11251     1 YSLSERPLDYRILFMDEDQDRIYVGSKDHILSLNINNISQDALSIFWPASASKVEECKMAGKDPTHGCGNFVRVIQPYNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 143 THLYVCGSGAFSPVCTYLNRGRRSEDQVFMIDSKCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTK 222
Cdd:cd11251    81 THLYVCGSGAFSPVCVYVNRGRRSEEQVFHIDSKAESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 223 RNAVRTDQHNSKWLSEPMFVDAHVIPDGTDPNDAKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTFL 302
Cdd:cd11251   161 RNAVRTDQHNSKWLSEPIFVDAHLIPDGTDPNDAKLYFFLKERLTDNSGSTKQIHSMIARVCPNDTGGQRSLVNKWTTFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 303 KARLVCSVTDEDGPETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNHQLI 382
Cdd:cd11251   241 KARLVCSVMDEDGTETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHMSDIQTVFNGPFAHKEGPNHQLI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 383 SYQGRIPYPRPGTCPGGAFTPNMRTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDYKYTKIAVDRVNAADGRY 462
Cdd:cd11251   321 AYQGRIPYPRPGTCPGGAFTPNMQSTKEFPDDVVTFIRNHPLMFNPIYPIGRRPLLVRTGTDYKYTKIAVDRVNAADGRY 400
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 463 HVLFLGTDRGTVQKVVVLPTNNSVSGELILEELEVFKNHAPITTMKISSKKQQLYVSSNEGVSQVSLHRC 532
Cdd:cd11251   401 HVLFLGTDKGTVQKVVVLPTNGSLSGELILEELEVFKNHAPITNMKISSKKQQLYVSSEEGISQVSLHRC 470
Sema_3 cd11239
The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins ...
63-532 0e+00

The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins (Sema3s) are secreted regulator molecules involved in the development of the nervous system, vasculogenesis, angiogenesis,and tumorigenesis. There are 7 distinct subfamilies named Sema3A to 3G. Sema3s function as repellent signals during axon guidance by repelling neurons away from the source of Sema3s. However, Sema3s that are secreted by tumor cells play an inhibitory role in tumor growth and angiogenesis (specifically Sema3B and Sema3F). Sema3s functions by forming complexes with neuropilins and A-type plexins, where neuropilins serve as the ligand binding moiety and the plexins function as signal transduction component. Sema3s primarily inhibit the cell motility and migration of tumor and endothelial cells by inducing collapse of the actin cytoskeleton via neuropilins and plexins. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200500 [Multi-domain]  Cd Length: 471  Bit Score: 887.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  63 FSLSHHPLDYRILLMDEDQDRIYVGSKDHILSLNINNISQEALSVFWPASTIKVEECKMAGKDPTHGCGNFVRVIQTFNR 142
Cdd:cd11239     1 FLGSMNSLDYRSLLLDEDRDRLYVGGKDHILSLSLDNINQDPKKIYWPASPERIEECKMAGKDPNTECANFVRVLQPYNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 143 THLYVCGSGAFSPVCTYLNRGRRSEDQVF-MIDSKCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLT 221
Cdd:cd11239    81 THLYACGTGAFHPICAFINVGRRLEDPIFkLDDSSLESGRGKCPFDPNQPFASVLIDGELYSGTAIDFMGRDAAIFRSLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 222 KRNAVRTDQHNSKWLSEPMFVDAHVIPDGTDPNDAKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTF 301
Cdd:cd11239   161 HRHYIRTEQYDSRWLNEPKFVGAYLIPDSDNPDDDKVYFFFREKAVEAEGSGKAIYSRVGRICKNDVGGQRSLVNKWSTF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 302 LKARLVCSVTDEDGPETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNHQL 381
Cdd:cd11239   241 LKARLVCSVPGPDGIDTYFDELEDVFLLPTRDPKNPLIYGVFTTSSNVFKGSAVCVYSMADIRAAFNGPFAHKEGPNYQW 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 382 ISYQGRIPYPRPGTCPGGAFTPNMRTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDYKYTKIAVDRVNAADGR 461
Cdd:cd11239   321 VEYQGKVPYPRPGTCPSKTYGPLYKSTKDFPDDVISFARSHPLMYNPVYPLHGRPLLIRTNVPYRLTQIAVDRVEAEDGQ 400
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189690239 462 YHVLFLGTDRGTVQKVVVLPTNNSVSGELILEELEVFKNHAPITTMKISSKKQQLYVSSNEGVSQVSLHRC 532
Cdd:cd11239   401 YDVLFIGTDSGTVLKVVSLPKENWEMEEVILEELQVFKHPSPITSMEISSKRQQLYVGSAEGVVQLPLHRC 471
Sema_3F cd11254
The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is ...
63-532 0e+00

The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is coexpressed with semaphorin3B. Both Sema3B and Sema3F proteins are candidate tumor suppressors that are down-regulated in highly metastatic tumors. Two receptor families, the neuropilins and plexins, have been implicated in mediating the actions of semaphorins 3B and 3F. Sema3F is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200515 [Multi-domain]  Cd Length: 470  Bit Score: 775.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  63 FSLSHHPLDYRILLMDEDQDRIYVGSKDHILSLNINNISQEALSVFWPASTIKVEECKMAGKDPTHGCGNFVRVIQTFNR 142
Cdd:cd11254     1 FSFLLNTSDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWPASPQRIEECILSGKGSNGECGNFIRLIQPWNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 143 THLYVCGSGAFSPVCTYLNRGRRSEDQVF-MIDSKCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLT 221
Cdd:cd11254    81 THLYVCGTGAYNPVCAYINRGRRAEDYMFrLEPDKLESGKGKCPYDPKQDSVSALINGELYAGVYIDFMGTDAAIFRTMG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 222 KRNAVRTDQHNSKWLSEPMFVDAHVIPDGTDPNDAKVYFFFKEKLTDNNRSTKqIHSMIARICPNDTGGLRSLVNKWTTF 301
Cdd:cd11254   161 KQPAMRTDQYNSRWLNDPAFVHAHLIPDSSEKNDDKLYFFFREKSLEAPQSPA-VLSRIGRVCLNDDGGHCCLVNKWSTF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 302 LKARLVCSVTDEDGPETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNHQL 381
Cdd:cd11254   240 LKARLVCSVPGADGIETHFDELRDVFIQPTQDTKNPVIYAVFSTSGSVFKGSAVCVYSMADIRMVFNGPFAHKEGPNYQW 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 382 ISYQGRIPYPRPGTCPGGAFTPNMRTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDYKYTKIAVDRVNAADGR 461
Cdd:cd11254   320 MPYTGKIPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYNAVYPVHRRPLVVRTNVNYRFTTIAVDQVDAADGR 399
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189690239 462 YHVLFLGTDRGTVQKVVVLPTNNSVSGELILEELEVFKNHAPITTMKISSKKQQLYVSSNEGVSQVSLHRC 532
Cdd:cd11254   400 YEVLFLGTDRGTVQKVIVLPKDDLETEELTLEEVEVFKVPAPIKTMKISSKRQQLYVSSAVGVTHLSLHRC 470
Sema_3B cd11250
The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is ...
72-532 0e+00

The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is coexpressed with semaphorin 3F and both proteins are candidate tumor suppressors. Both Sema3B and Sema3F show high levels of expression in normal tissues and low-grade tumors but are down-regulated in highly metastatic tumors in the lung, melanoma cells, bladder carcinoma cells and prostate carcinoma. They are upregulated by estrogen and inhibit cell motility and invasiveness through decreased FAK phosphorylation and inhibition of MMP-2 and MMP-9 expression. Two receptor families, the neuropilins (NP) and plexins, have been implicated in mediating the actions of semaphorins 3B and 3F. Sema3B is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200511 [Multi-domain]  Cd Length: 471  Bit Score: 621.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  72 YRILLMDEDQDRIYVGSKDHILSLNINNISQEALSVFWPASTIKVEECKMAGKDPTHGCGNFVRVIQTFNRTHLYVCGSG 151
Cdd:cd11250    10 YDALLLDEERGRLFVGAKNYLASLSLDNISKQEKKIYWPAPVEWREECNWAGKDINTDCMNYVKILHHYNRTHLYACGTG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 152 AFSPVCTYLNRGRRSEDQVFMID-SKCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTKRNAVRTDQ 230
Cdd:cd11250    90 AFHPTCAFVEVGQRMEDHVFRLDpSRVEDGKGKSPYDPRHTAASVLVGDELYSGVATDLMGRDFTIFRSLGQRPSLRTEQ 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 231 HNSKWLSEPMFVDAHVIPDGTDPNDAKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTFLKARLVCSV 310
Cdd:cd11250   170 HDSRWLNEPKFVKVFWIPESENPDDDKIYFFFRETAVEAAGLGKQSYSRIGQICRNDMGGQRSLVNKWTTFLKARLVCSV 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 311 TDEDGPETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNHQLISYQGRIPY 390
Cdd:cd11250   250 PGNEGGDTHFDELRDVFLLQTRDKRNPLIYAVFSTSSSVFQGSAVCVYTMNDVRRAFLGPFAHKEGPNYQWVSYQGKVPY 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 391 PRPGTCPGGAFTpNMRTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDYKYTKIAVDRVNAADGRYHVLFLGTD 470
Cdd:cd11250   330 PRPGMCPSKTFG-SFESTKDFPDDVIQFARNHPLMFNPVLPLGGRPLFLRTGIPYTFTQIAVDRVAAADGHYDVMFIGTD 408
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189690239 471 RGTVQKVVVLPTNNSVSGE-LILEELEVFKNHAPITTMKISSKKQQLYVSSNEGVSQVSLHRC 532
Cdd:cd11250   409 VGSVLKVISVPKGSWPSNEeLLLEELHVFKDSSPITSMQISSKRQQLYVGSRSGVSQLPLHRC 471
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
46-532 0e+00

The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been reported to inhibit the growth of certain experimental tumors and to regulate endothelial cell migration and apoptosis in vitro, as well as arteriogenesis in the muscle, skin vessel permeability, and tumor angiogenesis in vivo. The function of Sema3A is mediated through receptors neuropilin-1 (NP1) and plexins, although little is known about the requirement of specific plexins in its receptor complex. It is known however that Plexin-A4 is the receptor for Sema3A in the Toll-like receptor- and sepsis-induced cytokine storm during immune response. Sema3A is a member of the Class 3 semaphorin family of secreted proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200510 [Multi-domain]  Cd Length: 493  Bit Score: 608.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  46 RVYLTFDELRETKTSEYFSLSHHPLDYRILLMDEDQDRIYVGSKDHILSLNINNISQEALsVFWPASTIKVEECKMAGKD 125
Cdd:cd11249     6 RLKLSYKEMLESNNLITFNGLANSSSYHTFLLDEERGRLYVGAKDHIFSFNLVNIKDFQK-IVWPVSPSRRDECKWAGKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 126 PTHGCGNFVRVIQTFNRTHLYVCGSGAFSPVCTYLNRGRRSEDQVF-MIDSKCESGKGRCSFNPNVNTVSVMINEELFSG 204
Cdd:cd11249    85 ILKECANFIKVLKAYNQTHLYACGTGAFHPVCTYIEVGHHPEDNIFrLEDSHFENGRGKSPYDPKLLTASLLIDGELYSG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 205 MYIDFMGTDAAIFRSLTKRNAVRTDQHNSKWLSEPMFVDAHVIPDGTDPNDAKVYFFFKEKLTDNNRSTKQIHSMIARIC 284
Cdd:cd11249   165 TAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLNDPRFISAHLIPESDNPEDDKIYFFFRENAIDGEHTGKATHARIGQLC 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 285 PNDTGGLRSLVNKWTTFLKARLVCSVTDEDGPETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQ 364
Cdd:cd11249   245 KNDFGGHRSLVNKWTTFLKARLICSVPGPNGIDTHFDELQDVFLMNSKDPKNPIVYAVFTTSSNIFKGSAVCMYSMTDIR 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 365 TVFNGPFAHKEGPNHQLISYQGRIPYPRPGTCPGGAFTpNMRTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTD 444
Cdd:cd11249   325 RVFLGPYAHRDGPNYQWVPFQGRVPYPRPGTCPSKTFG-GFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIIIKTDVD 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 445 YKYTKIAVDRVNAADGRYHVLFLGTDRGTVQKVVVLPTNNSVS-GELILEELEVFKNHAPITTMKISSKKQQLYVSSNEG 523
Cdd:cd11249   404 YQFTQIVVDRVEAEDGQYDVMFIGTDMGTVLKVVSIPKETWHDlEEVLLEEMTVFREPTAISAMELSTKQQQLYIGSAIG 483

                  ....*....
gi 1189690239 524 VSQVSLHRC 532
Cdd:cd11249   484 VSQLPLHRC 492
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
63-532 0e+00

The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted semaphorin expressed during the development of the nervous system. In zebrafish, Sema3D is expressed in the ventral tectum. It guides retinal axons along the dorsoventral axis of the tectum and guides the laterality of retinal ganglion cell (RGC) projections. Both Sema3D knockdown or its ubiquitous overexpression induced aberrant ipsilateral projections. Proper balance of Sema3D is needed at the midline for the progression of RGC axons from the chiasm midline into the contralateral optic tract. Sema3D is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200513 [Multi-domain]  Cd Length: 474  Bit Score: 606.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  63 FSLSHHPLDYRILLMDEDQDRIYVGSKDHILSLNINNISQEALSVFWPASTIKVEECKMAGKDPTHGCGNFVRVIQTFNR 142
Cdd:cd11252     1 FLGSSEGLDFQTLLLDEERGRLLLGAKDHIYLLDLVDLNKNPKKIYWPAAKERVELCKLAGKDANTECANFIRVLHPYNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 143 THLYVCGSGAFSPVCTYLNRGRRSEDQVFMIDSK-CESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSL- 220
Cdd:cd11252    81 THVYVCGTGAFHPTCGYIELGTHKEDRIFLLDTQnLESGRLKCPFDPQQPFASVMTDEYLYAGTASDFLGKDTTFTRSLg 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 221 --TKRNAVRTDQHNSKWLSEPMFVDAHVIPDGTDPNDAKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKW 298
Cdd:cd11252   161 ptPDHHYIRTDISEHYWLNGAKFIGTFPIPDTYNPDDDKIYFFFREASQDGSTSDKSVLSRVGRVCKNDVGGQRSLINKW 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 299 TTFLKARLVCSVTDEDGPETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPN 378
Cdd:cd11252   241 TTFLKARLVCSIPGPDGADTHFDELQDIFLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESPD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 379 HQLISYQGRIPYPRPGTCPGGAFTPNMRTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDYKYTKIAVDRVNAA 458
Cdd:cd11252   321 HRWVQYEGRIPYPRPGTCPSKTYDPLIKSTKDFPDEVISFIKRHPLMYKSVYPLTGGPVFTRINVDYRLTQIVVDHVAAE 400
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189690239 459 DGRYHVLFLGTDRGTVQKVVVLPTNNSVSGELILEELEVFKNHAPITTMKISSKKQQLYVSSNEGVSQVSLHRC 532
Cdd:cd11252   401 DGQYDVMFLGTDIGTVLKVVSITKEKWTMEEVVLEELQIFKHPSPILNMELSLKQQQLYIGSRDGLVQLSLHRC 474
Sema_3E cd11253
The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted ...
70-532 0e+00

The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted molecule implicated in axonal path finding and inhibition of developmental and postischemic angiogenesis. It is also highly expressed in metastatic cancer cells. Sema3E signaling, through its high affinity functional receptor Plexin D1, drives cancer cell invasiveness and metastatic spreading. Sema3E is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200514  Cd Length: 471  Bit Score: 548.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  70 LDYRILLMDEDQDRIYVGSKDHILSLNINNISQEALSVFWPASTIKVEECKMAGKDPTHgCGNFVRVIQTFNRTHLYVCG 149
Cdd:cd11253     8 LDLHTMLLDEYQERLFVGGRDLLYSLSLERISANYKEIHWPSTQLQVEDCIMKGRDKPE-CANYIRVLHHYNRTHLLACG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 150 SGAFSPVCTYLNRGRRSEDQVFMIDS-KCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTKRNAVRT 228
Cdd:cd11253    87 TGAFDPVCAFIRVGRGSEDHLFQLESdKFERGRGRCPFDPNSSFISTLIGGELFVGLYSDYWGRDAAIFRTMNHLAHIRT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 229 DQHNSKWLSEPMFVDAHVIPDGTDPNDAKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTFLKARLVC 308
Cdd:cd11253   167 EHDDERLLKEPKFVGSYMIPDNEDPDDNKVYFFFTEKALEAEGGNHAIYTRVGRVCANDQGGQRMLVNKWSTFLKTRLIC 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 309 SVTDEDGPETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNHQLISYQGRI 388
Cdd:cd11253   247 SVPGPNGIDTHFDELEDVFLLRTRDNKNPEIFGLFSTTSNIFKGYAICVYHMASIRAAFNGPFAHKEGPEYHWSVYEGKV 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 389 PYPRPGTCP----GGAFTpnmrTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDYKYTKIAVDRVNAADGRYHV 464
Cdd:cd11253   327 PYPRPGSCAskvnGGHYG----TTKDYPDEALRFARSHPLMYQAVKPVHKRPILVKTDGKYNLKQIAVDRVEAEDGQYDV 402
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189690239 465 LFLGTDRGTVQKVVVLPTNNSVS-GELILEELEVFKNHAPITTMKISSKKQQLYVSSNEGVSQVSLHRC 532
Cdd:cd11253   403 LFIGTDNGIVLKVITIYNQETETmEEVILEELQVFKVPVPIISMEISSKRQQLYIGSESGVAQIRFHQC 471
Sema_3G cd11255
The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is ...
67-532 0e+00

The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is identified as a primarily endothelial cell- expressed class 3 semaphorin that controls endothelial and smooth muscle cell functions in autocrine and paracrine manners, respectively. It is mainly expressed in the lung and kidney, and a little in the brain. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200516 [Multi-domain]  Cd Length: 474  Bit Score: 547.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  67 HHPLDYRILLMDEDQDRIYVGSKDHILSLNINNISQEALSVFWPASTIKVEECKMAGKDPTHGCGNFVRVIQTFNRTHLY 146
Cdd:cd11255     5 HGDLHLSAVYLDEYRDRLFLGGKDVLYSLRLDQTHPDAKEIHWPPLPGQREECIRKGKDPETECANFVRVLQPFNRTHLL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 147 VCGSGAFSPVCTYLNRGRRSEdQVFMID-SKCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTKRNA 225
Cdd:cd11255    85 ACGTGAFQPVCALINVGHRGE-HVFSLDpTTVESGRGRCPHEPKRPFASTFTGGELYTGLTADFLGRDSVIFRGFGTRSP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 226 VRTDQhNSKWLSEPMFVDAHVIPDGTDPNDAKVYFFFKEKLTDNNRSTKQ-IHSMIARICPNDTGGLRSLVNKWTTFLKA 304
Cdd:cd11255   164 LRTET-DQRLLHEPRFVAAHLIPDNADRDNDKVYFFFTERATETAEDDDGaIHSRVGRLCANDAGGQRVLVNKWSTFIKA 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 305 RLVCSVTDEDGPETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNHQLISY 384
Cdd:cd11255   243 RLVCSVPGPHGIQTHFDQLEDVFLLRTKDGKSPEIYALFSTISNVFQGFAVCVYSMADIWEVFNGPFAHKDGPDHQWGPY 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 385 QGRIPYPRPGTC-------PGGAFtpnmRTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDYKYTKIAVDRVNA 457
Cdd:cd11255   323 EGKVPYPRPGVCpskitaqPGRAF----RSTKDYPDEVLQFARAHPLMWRPVYPSHRRPVLVKTGLPYRLTQIVVDRVEA 398
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189690239 458 ADGRYHVLFLGTDRGTVQKVVVLPTNNSVSG-ELILEELEVFKNHAPITTMKISSKKQQLYVSSNEGVSQVSLHRC 532
Cdd:cd11255   399 EDGYYDVMFIGTDSGSVLKVIVLQKGNSAAGeEVTLEELQVFKVPTPITEMEISVKRQMLYVGSRTGVAQVPLHRC 474
Sema_semaphorin cd11235
The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator ...
70-530 2.11e-168

The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. They can be divided into 7 classes. Vertebrates have members in classes 3-7, whereas classes 1 and 2 are known only in invertebrates. Class 2 and 3 semaphorins are secreted proteins; classes 1 and 4 through 6 are transmembrane proteins; and class 7 is membrane associated via glycosylphosphatidylinositol (GPI) linkage. The semaphorins exert their function through their receptors, the neuropilin and plexin families. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200496 [Multi-domain]  Cd Length: 437  Bit Score: 492.31  E-value: 2.11e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  70 LDYRILLMDEDQDRIYVGSKDHILSLNINNISQEaLSVFWPASTIKVEECKMAGKDPTHgCGNFVRVIQTFNRTHLYVCG 149
Cdd:cd11235     1 LKYHTKLLHEDRSTLYVGARDRVYLVDLDSLYTE-QKVAWPSSPDDVDTCYLKGKSKDD-CRNFIKVLEKNSDDSLLVCG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 150 SGAFSPVCTYLNrgrrseDQVFMIDSKCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTKRNAVRTD 229
Cdd:cd11235    79 TNAFNPSCRNYN------VETFELVGKEESGRGKCPYDPDHNSTALFADGELYSGTSADFLGTDPVIYRTLGHNPPLRTE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 230 QHNSKWLSEPMFVDAHVIPDgtdpndaKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTFLKARLVCS 309
Cdd:cd11235   153 YHDSKWLNEPQFVGAFDIGD-------YVYFFFREIAVEYINCGKAVYSRVARVCKNDQGGSRSLEKKWTTFLKARLNCS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 310 VTDEDGpeTHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNHQLISYQG-RI 388
Cdd:cd11235   226 VPGEFP--FYFNELQDVFDLPSPSNKEKIFYAVFTTPYNSIPGSAVCAYSLSDIEAVFNGPFKEQHSSNSAWLPVPDeRV 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 389 PYPRPGTCPGgaftpnmrTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDYKYTKIAVDRVNAADGR-YHVLFL 467
Cdd:cd11235   304 PEPRPGTCVD--------DSSPLPDDTLNFIKSHPLMDEAVTPILNRPLFIKTDVNYRFTKIAVDRVQAKLGQtYDVLFV 375
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189690239 468 GTDRGTVQKVVVLPTNNSvSGELILEELEVFKNHAPITTMKISSKKQQLYVSSNEGVSQVSLH 530
Cdd:cd11235   376 GTDRGIILKVVSLPEQGL-QASNILEEMPVGPPPEPIQTMQLSRKRRSLYVGSETGVLQVPLA 437
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
74-511 1.08e-157

Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and transmembrane proteins, some of which function as repellent signals during axon guidance. Sema domains also occur in the hepatocyte growth factor receptor and plexin-A3.


Pssm-ID: 426245 [Multi-domain]  Cd Length: 364  Bit Score: 462.16  E-value: 1.08e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  74 ILLMDEDQDRIYVGSKDHILSLNINNISQeaLSVFWPASTIKVEECKMAGKDPThGCGNFVRVIQTFNRTHLYVCGSGAF 153
Cdd:pfam01403   1 TLLLDEDSGRLYVGARNALYALNLDNLSL--LQEKQTGPEEDREECRPKGKDET-ECANYIRVLQPLNDTHLYVCGTNAF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 154 SPVCTYLNrgrrsedqvfMIDSKCESGKGRCSFNPNVNTVSVM-INEELFSGMYIDFMGTDAAIfRSLTKRNAVRTDQHN 232
Cdd:pfam01403  78 QPLCAYIR----------LEDEHYESGKGKCPFDPSQNSTAVVvVDGELYSGTSIDFLGSDPVI-RSLGSRPSLRTEQYD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 233 SKWLSEPMFVDAHVIPDgtdpndaKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTFLKARLVCSVtd 312
Cdd:pfam01403 147 SKWLNEPNFVSSFEIGD-------SVYFFFRETAVEYDFCGKAVVSRVARVCKNDVGGQRTLQKKWTSFLKARLVCSV-- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 313 eDGPETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFngpfahkegpnhqlisyqgripypr 392
Cdd:pfam01403 218 -PGVEGYFNELQDVFLLGISDWKDTVLYGVFTTQSNSIGGSAVCAFSLSDINEVF------------------------- 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 393 pgtcpggaftpnmrttkefpdDVVTFIRNHPLMYNSIYPIHKRPLIVRigTDYKYTKIAVDRVNAADGRYHVLFLGTDRG 472
Cdd:pfam01403 272 ---------------------KVLNFVKDHPLMDEAVPPPGGRPLLVR--RDVRLTRIAVDRVQADGGTYTVLFLGTDDG 328
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1189690239 473 TVQKVVVLPTNNsvsGELILEELEVFKNHAPITTMKISS 511
Cdd:pfam01403 329 RLHKVVVLGSEN---EAHIIEEIQVFPEPQPVLNLLLSS 364
Sema smart00630
semaphorin domain;
72-504 1.35e-155

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 457.60  E-value: 1.35e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239   72 YRILLMDEDQDRIYVGSKDHILSLNINNISQEALSVFWPASTIKVEECKMAGKDPTHGCGNFVRVIQTFNRTHLYVCGSG 151
Cdd:smart00630   1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAELKTGPVLSSPDCEECVSKGKDPPTDCVNYIRLLLDYNEDRLLVCGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  152 AFSPVCTYLNRGrrsedqvfmidskcesgkgrcsfnpnvntvsvmineELFSGMYIDFMGTDAAIFRSLTKRNAV----- 226
Cdd:smart00630  81 AFQPVCRLRNLG------------------------------------ELYVGTVADFSGSDPAIPRSLSVRRLKgtsgv 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  227 --RTDQHNSKWLSEPMFVDAHVIpdgtdpnDAKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTFLKA 304
Cdd:smart00630 125 slRTVLYDSKWLNEPNFVYAFES-------GDFVYFFFRETAVEDDNCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKA 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  305 RLVCSVTDEDGpeTHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNHQLISY 384
Cdd:smart00630 198 RLECSVPGEDP--FYFNELQAAFLLPPGSESDDVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLPY 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  385 -QGRIPYPRPGTCPGGAFtpnmrTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDYKYTKIAVDRVNaADGRYH 463
Cdd:smart00630 276 sRGKVPYPRPGTCPNKPP-----SSKDLPDETLNFIKSHPLMDEVVQPLTGRPLFVKTDSNYLLTSIAVDRVA-TDGNYT 349
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1189690239  464 VLFLGTDRGTVQKVVVLPTNNSVSgELILEELEVFKNHAPI 504
Cdd:smart00630 350 VLFLGTSDGRILKVVLSESSSSSE-SVVLEEISVFPDGSPI 389
Sema_4 cd11240
The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 ...
71-529 2.63e-139

The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 semaphorins (Sema4s) are transmembrane regulator molecules involved in the development of the nervous system, immune response, cytoskeletal organization, angiogenesis, and cell-cell interactions. There are 7 distinct subfamilies in class 4 semaphorins, named 4A to 4G. Several class 4 subfamilies play important roles in the immune system and are called "immune semaphorins". Sema4A plays critical roles in T cell-DC interactions in the immune response. Sema4D/CD100, expressed by lymphocytes, promotes the aggregation and survival of B lymphocytes and inhibits cytokine-induced migration of immune cells in vitro. It is required for normal activation of B and T lymphocytes. Sema4B negatively regulates basophil functions through T cell-basophil contacts and significantly inhibits IL-4 and IL-6 production from basophils in response to various stimuli, including IL-3 and papain. Sema4s not only influence the activation state of cells but also modulate their migration and survival. The effects of Sema4s on nonlymphoid cells are mediated by plexin D1 and plexin Bs. The Sema4G and Sema4C genes are expressed in the developing cerebellar cortex and are involved in neural tube closure and development of cerebellar granules cells through receptor plexin B2. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200501 [Multi-domain]  Cd Length: 456  Bit Score: 418.35  E-value: 2.63e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  71 DYRILLMDEDQDRIYVGSKDHILSLNINNISQE-ALSVFWPASTIKVEECKMAGKDPTHGCGNFVRVIQTFNRTHLYVCG 149
Cdd:cd11240     8 NYSTLLLSEDEGTLYVGAREALFALNVSDISTElKDKIKWEASEDKKKECANKGKDNQTDCFNFIRILQFYNSTHLYVCG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 150 SGAFSPVCTYLNRGRRSedqvfMIDSKCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTKRNAVRTD 229
Cdd:cd11240    88 TFAFSPRCTYINLSDFS-----LSSIKFEDGKGRCPFDPAQRYTAIMVDGELYSATVNNFLGSEPVISRNHSEGNVLKTE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 230 qHNSKWLSEPMFVDAHVIPDGTDP---NDAKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTFLKARL 306
Cdd:cd11240   163 -NTLRWLNEPAFVGSAHIRESIDSpdgDDDKIYFFFTETAVEYDFYEKVTVSRVARVCKGDLGGQRTLQKKWTTFLKAQL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 307 VCSVTDEdgpETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNHQLISYQG 386
Cdd:cd11240   242 VCSQPDS---GLPFNVLRDVFVLSPDSWDATIFYGVFTSQWNVSGLSAVCAYSLEDIKKVFSGKYKEFNRETSKWSRYTG 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 387 RIPYPRPGTC-PGGAFTPNMRTTKEFPDDVVTFIRNHPLMYNSIYPIHkRPLIVRIGTdyKYTKIAVDRVNAADGR-YHV 464
Cdd:cd11240   319 PVPDPRPGACiTNSARSQGITSSLNLPDNVLTFVKDHPLMDEQVHPIN-RPLLVKSGV--NYTRIAVHRVQALDGQtYTV 395
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189690239 465 LFLGTDRGTVQKVVVLptNNSVSgelILEELEVFKNHAPITTMKISSKKQQLYVSSNEGVSQVSL 529
Cdd:cd11240   396 LFLGTEDGFLHKAVSL--DGGMH---IIEEIQLFDQPQPVKNLLLSSSKGVLYVGSSSGVVQVPL 455
Sema_4G cd11262
The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and ...
70-529 6.03e-125

The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and Sema4C genes are expressed in the developing cerebellar cortex. Sema4G and Sema4C proteins specifically bind to Plexin B2 expressed in the cerebellar granule cells. Sema4G and Sema4C are involved in neural tube closure and cerebellar granule cell development through Plexin B2.Sema4G belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200523 [Multi-domain]  Cd Length: 457  Bit Score: 381.42  E-value: 6.03e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  70 LDYRILLMDEDQDRIYVGSKDHILSLNINNISQE-ALSVFWPASTIKVEECKMAGKDPTHGCGNFVRVIQTFNRTHLYVC 148
Cdd:cd11262     8 QNYSTLLLEDESGRLYVGARGAIFSLNASDISDSsALTIDWEASPEQKHQCLKKGKNNQTECFNHVRFLQRFNSTHLYTC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 149 GSGAFSPVCTYLnRGRRsedqvFMIDSKCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTdAAIFRSLTKRNaVRT 228
Cdd:cd11262    88 GTHAFRPLCAYI-DAER-----FTLSSQFEEGKEKCPYDPAKGYTGLIVDGQLYTASQYEFRSF-PDIRRNSPQPT-LRT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 229 DQHNSKWLSEPMFVDAHVIPDGTDP---NDAKVYFFFKEKLTDNNRSTKQIH-SMIARICPNDTGGLRSLVNKWTTFLKA 304
Cdd:cd11262   160 EEAPTRWLNDADFVGSVLVRESMNSsvgDDDKIYFFFTERSQEETAYFSQSRvARVARVCKGDRGGKKTLQRKWTSFLKA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 305 RLVCSVTDEdgpETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNHQLISY 384
Cdd:cd11262   240 RLVCYIPEY---EFLFNVLRSVFVLWGSTPQDTVFYGIFGLEWKNVKASAICRYSLSDIQTAFEGPYMEYQDSSSKWSRY 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 385 QGRIPYPRPGTCPGGAFTPN-MRTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDykYTKIAVDRVNAADGR-Y 462
Cdd:cd11262   317 TGKVPEPRPGSCITDEHRSQgINSSQDLPDNVLDFVRRHPLMAEQVLPVEGRPLLFKRNVI--YTKIAVQTVRGLDGRvY 394
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189690239 463 HVLFLGTDRGTVQKVVVLptnnsVSGELILEELEVFKNHAPITTMKISSKKQQLYVSSNEGVSQVSL 529
Cdd:cd11262   395 DVLFLGTDEGWLHKAVVI-----GSAVHIIEELQVFREPQPVENLVISKKQNSLYVGARSGVVQVPL 456
Sema_4D cd11259
The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); ...
71-526 6.49e-117

The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); Sema4D/CD100 is expressed in immune cells and plays critical roles in immune response; it is thus termed an "immune semaphorin". It is expressed by lymphocytes and promotes the aggregation and survival of B lymphocytes and inhibits cytokine-induced migration of immune cells in vitro. Sema4D/CD100 knock-out mice demonstrate that Sema4D is required for normal activation of B and T lymphocytes. Sema4D increases B-cell and DC function using either Plexin B1 or CD72 as receptors. The function of Sema4D in immune response implicates its role in infectious and noninfectious diseases. Sema4D belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200520 [Multi-domain]  Cd Length: 471  Bit Score: 361.10  E-value: 6.49e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  71 DYRILLMDEDQDRIYVGSKDHILSLNINNISQEALSVFWPASTIKVEECKMAGKDPTHGCGNFVRVIQTFNRTHLYVCGS 150
Cdd:cd11259    19 NYSTLLLSEDKDVLYVGAREAVFALNALNISEKQHELYWKVSEDKRTKCAVKGKSKQTECRNYIRVLQPLNDTFLYVCGT 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 151 GAFSPVCTYLNRgrrsedQVFMIDSKCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTkRNAVRTdQ 230
Cdd:cd11259    99 NAFQPTCDYLNL------TSFRLLGKNEDGKGRCPFDPAQSYTSVMVDGELYSGTSYNFLGSEPIISRNSS-QSPLRT-E 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 231 HNSKWLSEPMFVDAHVI---PDGTDPNDAKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTFLKARLV 307
Cdd:cd11259   171 YAIPWLNEPSFVFADVIradPDSPDGEDDKIYFFFTEVSVEYEFVGKLLIPRIARVCKGDQGGLRTLQKKWTSFLKARLI 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 308 CSVTDEDgpeTHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFN-GPFAHK---EGPNHQLIS 383
Cdd:cd11259   251 CSIPDKN---LVFNVVNDVFILKSPTLKEPVIYGVFTPQLNNVGLSAVCAYNLSTVEEVFSkGKYMQSatvEQSHTKWVR 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 384 YQGRIPYPRPGTCPGG-AFTPNMRTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRigTDYKYTKIAVDRVNAADGR- 461
Cdd:cd11259   328 YNGEVPKPRPGACINNeARAANYTSSLNLPDKTLQFVKDHPLMDDSVTPIGNRPRLIK--KDVNYTQIVVDRVQALDGTi 405
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189690239 462 YHVLFLGTDRGTVQKVVVLPtnnsvSGELILEELEVFKNHAPITTMKISSKKQQ--LYVSSNEGVSQ 526
Cdd:cd11259   406 YDVMFISTDRGALHKAISLE-----NEVHIIEETQLFPDFEPVQTLLLSSKKGRrfLYAGSNSGVVQ 467
Sema_4E cd11260
The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed ...
71-529 3.03e-105

The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed in the epithelial cells that line the pharyngeal arches in zebrafish. It may act as a guidance molecule to restrict the branchiomotor axons to the mesenchymal cells. Gain-of-function and loss-of-function studies demonstrate that Sema4E is essential for the guidance of facial axons from the hindbrain into their pharyngeal arch targets and is sufficient for guidance of gill motor axons. Sema4E guides facial motor axons by a repulsive action. Sema4E belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200521 [Multi-domain]  Cd Length: 456  Bit Score: 330.33  E-value: 3.03e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  71 DYRILLMDEDQDRIYVGSKDHILSLNINNISQEALSVFWPASTIKVEECKMAGKDPTHGCGNFVRVIQTFNRTHLYVCGS 150
Cdd:cd11260     8 NYSTMLLREDLGLLVLGAREAVFALDLNDISVKRAKVLWEVTEEKQKDCTNKGKHADIDCHNYIRILHKMNDSRMYVCGT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 151 GAFSPVCTYLNrgrrSEDQVFMIDSKCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSltKRNAVRTdQ 230
Cdd:cd11260    88 NAFSPTCDYIS----YDDGQLTLEGKQEDGKGKCPFDPFQRYSSVMVDQDLYSATSMNFLGSEPVIMRS--SPITIRT-E 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 231 HNSKWLSEPMFVDAHVIPDGTDP---NDAKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTFLKARLV 307
Cdd:cd11260   161 FKSSWLNEPNFIYMAAVPESEDSpegDDDKIYLFFSETAVEYDFYNKLVVSRVARVCKGDLGGQRTLQKKWTSFLKARLD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 308 CSVtdedgPETHFDEL-EDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFN-----GPFAhKEGPNHQL 381
Cdd:cd11260   241 CSV-----PEPSLPYViQDVFHVCHQDWRKCVFYAVFTSQSDSSQSSAVCAYNVTDISNVFSrgkfkTPVA-VETSFVKW 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 382 ISYQGRIPYPRPGTC-PGGAFTPNMRTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTdyKYTKIAVDRVNAADG 460
Cdd:cd11260   315 VMYSGELPVPRPGACiNNAARTSGIKKSLNLPDKTLQFVKDKPLMDQAVHPITGKPLLVKRGA--LFTRIVVDMVTAADG 392
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189690239 461 -RYHVLFLGTDRGTVQKVVvlptnnSVSGEL-ILEELEVFKNHAPITTMKISSKkqQLYVSSNEGVSQVSL 529
Cdd:cd11260   393 qSYPVMFIGTANGYVLKAV------NYDGEMhIIEEVQLFEPEEPIDILRLSQN--QLYAGSASGVVQMPV 455
Sema_1A cd11237
The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a ...
71-532 2.15e-100

The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a transmembrane protein. It has been shown to mediate the defasciculation of motor axon bundles at specific choice points. Sema1A binds to its receptor plexin A (PlexA), which in turn triggers downstream signaling events involving the receptor tyrosine kinase Otk, the evolutionarily conserved flavoprotein monooxygenase molecule interacting with CasL (MICAL), and the A kinase anchoring protein Nervy, leading to repulsive growth-cone response. Sema1A has also been shown to be involved in synaptic formation. It is a member of the semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200498  Cd Length: 446  Bit Score: 316.97  E-value: 2.15e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  71 DYRILLmDEDQDRIYVGSKDHILSLNINNISqEALSVFWPASTIKVEECKMAGKDPTHgCGNFVRVIQTFNRTHLYVCGS 150
Cdd:cd11237     5 DHFKLL-DQDGNSLLVGARNAVYNISLSDLT-ENQRIEWPSSDAHREMCLLKGKSEDD-CQNYIRVLAKKSAGRLLVCGT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 151 GAFSPVCTYLNR---GRRSEDQVfmidskceSGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRsltkrNAVR 227
Cdd:cd11237    82 NAYKPLCREYTVkdgGYRVEREF--------DGQGLCPYDPKHNSTAVYADGQLYSATVADFSGADPLIYR-----EPLR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 228 TDQHNSKWLSEPMFVDAhvIPDGtdpndAKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTFLKARLV 307
Cdd:cd11237   149 TERYDLKQLNAPNFVSS--FAYG-----DYVYFFFRETAVEYINCGKAIYSRVARVCKNDKGGPHPFRDRWTSFLKARLN 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 308 CSVTDeDGPeTHFDELEDVF-LLET--DNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPN-HQLIS 383
Cdd:cd11237   222 CSVPG-EYP-FYFNEIQSTSdIVEGgyGGKSAKLIYGVFTTPVNSISGSAVCAFSLQDILEVFDGSFKEQQDINsNWLPV 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 384 YQGRIPYPRPGTCpggafTPNMRTtkeFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDYKYTKIAVD-RVNAADGRY 462
Cdd:cd11237   300 PSNKVPEPRPGQC-----VNDSRT---LPDVTVNFIKSHPLMDEAVPSFFGRPILVRTSLQYRFTQIAVDpQVKALDGKY 371
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189690239 463 H-VLFLGTDRGTVQKVVVLPTNNSVSG--ELILEELEVFKNHAPITTMKISSKKQQ--LYVSSNEGVSQVSLHRC 532
Cdd:cd11237   372 YdVLFIGTDDGKVLKAVNIASADTVDKvsPVVIEETQVFPRGVPIRNLLIVRGKDDgrLVVVSDDEIVSIPLHRC 446
Sema_4B cd11257
The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in ...
68-529 1.75e-99

The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in T and B cells, is an immune semaphorin. It functions as a negative regulatory of basophils through T cell-basophil contacts and it significantly inhibits IL-4 and IL-6 production from basophils in response to various stimuli, including IL-3 and papain. In addition, T cell-derived Sema4B suppresses basophil-mediated Th2 skewing and humoral memory responses. Sema4B may be also involved in lung cancer cell mobility by inducing the degradation of CLCP1 (CUB, LCCL-homology, coagulation factor V/VIII homology domains protein). Sema4B is characterized by a PDZ-binding motif at the carboxy-terminus, which mediates interaction with the post-synaptic density protein PSD-95/SAP90, which is thought to play a central role during synaptogenesis and in the structure and function of post-synaptic specializations of excitatory synapses. Sema4B belongs to class 4 transmembrane semaphorin family proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200518 [Multi-domain]  Cd Length: 464  Bit Score: 315.26  E-value: 1.75e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  68 HPLDYRILLMDEDQDRIYVGSKDHILSLNINNIS--QEALSVFWPASTIKVEECKMAGKDPTHGCGNFVRVIQTFNRTHL 145
Cdd:cd11257     6 GVSNYTALLLSKDGNMLYVGARETLFALSSNDISptGEQQELTWSADEEKKQECSFKGKDPQRDCQNYIKILLRLNSTHL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 146 YVCGSGAFSPVCTYLNrgrrSEDQVFMIDSK----CESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLT 221
Cdd:cd11257    86 FTCGTYAFSPICTYIV----MTNFSLERDEKgeplLEDGKGRCPFDPEYKSTAIMVDGELYTGTVSNFQGNDPIIYRSLG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 222 KRNAVRTDqhNS-KWLSEPMFVDAHVIPdGTDP----NDAKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVN 296
Cdd:cd11257   162 SGTPLKTE--NSlNWLQDPAFVGSAYIQ-ESLPklvgDDDKIYFFFSETGKEFDFFENTIVSRIARVCKGDEGGERVLQK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 297 KWTTFLKARLVCSVTDEDGPethFDELEDVFLL--ETDNPRTTLVYGIFTT--SSSVFKGSAVCVYHLSDIQTVFNGPFA 372
Cdd:cd11257   239 RWTTFLKAQLLCSLPDDGFP---FNVLQDVFVLtpSPEDWKDTLFYGVFTSqwHKGTAGSSAVCVFTMDQVQRAFNGLYK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 373 HKEGPNHQLISYQGRIPYPRPGTC-PGGAFTPNMRTTKEFPDDVVTFIRNHPLMYNsiyPIHKRPLIVRigTDYKYTKIA 451
Cdd:cd11257   316 EVNRETQQWYTYTHPVPEPRPGACiTNSARERKINSSLHMPDRVLNFVKDHFLMDG---QVRSQPLLLQ--PQVRYTQIA 390
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189690239 452 VDRVNAADGRYHVLFLGTDRGTVQKVVvlptnnSVSGEL-ILEELEVFKNHAPITTMKISSKKQQLYVSSNEGVSQVSL 529
Cdd:cd11257   391 VHRVKGLHKTYDVLFLGTDDGRLHKAV------SVGPMVhIIEELQIFSEGQPVQNLLLDTHKGLLYASSHSGVVQVPV 463
Sema_6 cd11242
The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 ...
66-502 3.41e-95

The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 semaphorins (Sema6s) are membrane associated semaphorins. There are 6 subfamilies named 6A to 6D. Sema6s bind to plexin As in a neuropilin independent fashion. Sema6-plexin A signaling plays important roles in lamina-specific axon projections. Interactions between plexin A2, plexin A4, and Sema6A control lamina-restricted projection of hippocampal mossy fibers. Interactions between Sema6C, Sema6D and plexin A1 shape the stereotypic trajectories of sensory axons in the spinal cord. In addition to axon targeting, Sema6D-plexin A1 interactions influence a wide range of other biological processes. During cardiac development, Sema6D attracts or repels endothelial cells in the cardiac tube depending on the expression patterns of specific coreceptors in addition to plexin A1. Furthermore, Sema6D binds a receptor complex comprising of plexin A1, Trem2 (triggering receptor expressed on myeloid cells 2), and DAP12 on dendritic cells and osteoclasts to mediate T-cell-DC interactions and to control bone development, respectively. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200503 [Multi-domain]  Cd Length: 465  Bit Score: 304.05  E-value: 3.41e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  66 SHHPLDY-RILLMDedqDRIYVGSKDHILSLNINNISQEAL----SVFWPASTIKVEECKMAGKDpTHGCGNFVRVIQTF 140
Cdd:cd11242     5 ARHRLDFqRMLRIN---RTLYIAARDHVYTVDLDASHTEEIvpskKLTWRSRQADVENCRMKGKH-KDECHNFIKVLVPR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 141 NRTHLYVCGSGAFSPVCTylNRGRRSEDQvfmiDSKCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSL 220
Cdd:cd11242    81 NDETLFVCGTNAFNPVCR--NYRIDTLEQ----DGEEISGMARCPFDAKQANVALFADGKLYSATVTDFLASDAVIYRSL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 221 TKRNAVRTDQHNSKWLSEPMFVdaHVIPDGTdpndaKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGL-RSLVNKWT 299
Cdd:cd11242   155 GDSPTLRTVKYDSKWLKEPHFV--HAVEYGD-----YVYFFFREIAVEYNTLGKVVFSRVARVCKNDMGGSpRVLEKQWT 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 300 TFLKARLVCSVTDEDgpETHFDELEDVFLLETDNPRTTlVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNH 379
Cdd:cd11242   228 SFLKARLNCSVPGDS--HFYFDVLQAVTDVIRINGRPV-VLGVFTTQYNSIPGSAVCAFDMDDIEKVFEGRFKEQKSPDS 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 380 QLISY-QGRIPYPRPGTCPGGAFTPNMRTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDYKYTKIAVDRVNAA 458
Cdd:cd11242   305 AWTPVpEDRVPKPRPGCCAGSGSAEKYKTSNDFPDDTLNFIKTHPLMDEAVPSIINRPWFTRTMVRYRLTQIAVDNAAGP 384
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1189690239 459 DGRYHVLFLGTDRGTVQKVVVLPTNNSVSGELILEELEVFkNHA 502
Cdd:cd11242   385 YQNYTVVFLGSEAGTVLKFLARIGPSGSNGSVFLEEIDVY-NPA 427
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
71-529 4.67e-94

The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a Plexin B2 ligand to regulate the development of cerebellar granule cells and to modulate ureteric branching in the developing kidney. The binding of Sema4C to Plexin B2 results the phosphorylation of downstream regulator ErbB-2 and the plexin protein itself. The cytoplasmic region of Sema4C binds a neurite-outgrowth-related protein SFAP75, suggesting that Sema4C may also play a role in neural function. Sema4C belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200519 [Multi-domain]  Cd Length: 458  Bit Score: 300.95  E-value: 4.67e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  71 DYRILLMDEDQDRIYVGSKDHILSLNINNIS-QEALSvfWPASTIKVEECKMAGKDPTHGCGNFVRVIQTFNRTHLYVCG 149
Cdd:cd11258    11 NYTTLTLAEHRGLLYVGAREAIFALSLSNIElQPPIS--WEAPAEKKTECAQKGKSNQTECFNYIRFLQPYNQSHLYTCG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 150 SGAFSPVCTYLNRgrrsedQVFMIDS-KCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTKRNAVRT 228
Cdd:cd11258    89 TYAFQPKCAYINM------LTFTLDRaEFEDGKGKCPYDPAKGHTGLIVDGELYSATLNNFLGTEPVILRNLGQHYSMKT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 229 dQHNSKWLSEPMFVDAHVIPDGT---DPNDAKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTFLKAR 305
Cdd:cd11258   163 -EYLAFWLNEPHFVGSAFVPESVgsfTGDDDKIYFFFSERAVEYDCDSEQVVARVARVCKGDLGGARTLQKKWTTFLKAR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 306 LVCSVTDEdgpETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNHQLISYQ 385
Cdd:cd11258   242 LLCSIPEW---QLYFNQLKAVFTLEGASWRNTTFFAVFQARWGDMDVSAVCEYQLGEIQQVFEGPYKEYSEQAQKWGRYT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 386 GRIPYPRPGTCPGGAFTPN-MRTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDykYTKIAVDRVNAADGR-YH 463
Cdd:cd11258   319 DPVPSPRPGSCINNWHRDHgYTSSLELPDNTLNFVKKHPLMEDRVKPRLGRPLLVPCNSN--FTHVVWTRVLGLDGEtYS 396
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189690239 464 VLFLGTDRGTVQKVVVLPtnnsvSGELILEELEVFKNHAPITTMKISSKKQQLYVSSNEGVSQVSL 529
Cdd:cd11258   397 VLFIGTLDGWLIKAVSLG-----SWVHMIEELQVFDQEPPESLVVSQSSKKLLFAGSRSELLQLPW 457
Sema_2A cd11238
The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted ...
70-529 1.58e-91

The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted semaphorin, signals through its receptor plexin B (PlexB) to regulate central and peripheral axon pathfinding. In the Drosophila embryo, Sema2A secreted by oenocytes interacts with PlexB to guide sensory axons. Sema2A is a member of the semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200499 [Multi-domain]  Cd Length: 452  Bit Score: 293.95  E-value: 1.58e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  70 LDYRILLMDEDQDRIYVGSKDHILSLNINNISQEAL---SVFWPASTIKVEECKMAGKDPTHGCGNFVRVIQ-TFNRTHL 145
Cdd:cd11238     1 LYYRTLLLDEKRNALYVGAMDRVFRLNLYNINDTGNncaRDELTLSPSDVSECVSKGKDEEYECRNHVRVIQpMGDGQTL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 146 YVCGSGAFSPVCTYLNRGRRSEDQVFmidSKCESGKGRCSFNPNVNTVSVMI---NEE----LFSGMYIDFMGTDAAIFR 218
Cdd:cd11238    81 YVCSTNAMNPKDRVLDANLLHLPEYV---PGPGNGIGKCPYDPDDNSTAVWVewgNPGdlpaLYSGTRTEFTKANTVIYR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 219 S-LTKRNA------VRTDQHNSKWLSEPMFVDAHVIPDgtdpndaKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGL 291
Cdd:cd11238   158 PpLYNNTKgrhesfMRTLKYDSKWLDEPNFVGSFDIGD-------YVYFFFRETAVEYINCGKVVYSRVARVCKKDTGGK 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 292 RSLVNKWTTFLKARLVCSVTDEdGPeTHFDELEDVFllETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFN-GP 370
Cdd:cd11238   231 NVLRQNWTTFLKARLNCSISGE-FP-FYFNEIQSVY--KVPGRDDTLFYATFTTSENGFTGSAVCVFTLSDINAAFDtGK 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 371 FAHKEGPNH-QLISYQGRIPYPRPGTCpggaftpnMRTTKEFPDDVVTFIRNHPLMYNSIYpiHKRPLIVRigTDYKYTK 449
Cdd:cd11238   307 FKEQASSSSaWLPVLSSEVPEPRPGTC--------VNDSATLSDTVLHFARTHPLMDDAVS--HGPPLLYL--RDVVFTH 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 450 IAVDRVNAADGRYHVLFLGTDRGTVQKVVVLPTNNSVSGELiLEELEVfKNHAPITTMKIsSKKQQLYVSSNEGVSQVSL 529
Cdd:cd11238   375 LVVDKLRIDDQEYVVFYAGSNDGKVYKIVHWKDAGESKSNL-LDVFEL-TPGEPIRAMEL-LPGEFLYVASDHRVSQIDL 451
Sema_4A cd11256
The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed ...
71-552 1.95e-88

The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed in immune cells and is thus termed an "immune semaphorin". It plays critical roles in T cell-DC interactions in the immune response. It has been reported to enhance activation and differentiation of T cells in vitro and generation of antigen-specific T cells in vivo. The function of Sema4A in the immune response implicates its role in infectious and noninfectious diseases. Sema4A exerts its function through three receptors, namely Plexin B, Plexin D1, and Tim-2. Sema4A belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. TThe Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200517 [Multi-domain]  Cd Length: 447  Bit Score: 285.65  E-value: 1.95e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  71 DYRILLMDEDQDRIYVGSKDHILSLNINNISQEAL--SVFWPASTIKVEECKMAGKDPTHGCGNFVRVIQTFNRTHLYVC 148
Cdd:cd11256     9 NYDQLLLSPDETTLYVGARDNILALGIRTPGPIRLkhQIPWPANDSKISECAFKKKSNETECFNFIRVLVPVNGTHLYTC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 149 GSGAFSPVCTYLNRGRRS-----EDQVFMidskceSGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTKR 223
Cdd:cd11256    89 GTYAFSPACTYIELDHFSlpppnGTIITM------DGKGQSPFDPQHNYTAILVDGELYTGTMNNFRGNEPIIFRNLGTK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 224 NAVRTDQHNsKWLSEpmfvDAHVIPDGTDPNDAKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTFLK 303
Cdd:cd11256   163 VSLKTDGFL-RWLNA----DAVFVASFNPQGDSKVYFFFEETAREFDFFEKLTVARVARVCKNDVGGEKLLQKKWTTFLK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 304 ARLVCSVTDedgpETHFDELEDVFLLETDNPRTTLVYGIFTTSSSV--FKGSAVCVYHLSDIQTVFNGPFAHKEGPNHQL 381
Cdd:cd11256   238 AQLTCSQQG----HFPFNVIHHVALLNQPDPNNSVFYAVFTSQWQLggRRSSAVCAYKLNDIEKVFNGKYKELNKESSRW 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 382 ISYQGRIPYPRPGTCPGGAFTpnmrttkefpDDVVTFIRNHPLMYNSIYPIHKRPLIVRigTDYKYTKIAVDRVNAADGR 461
Cdd:cd11256   314 TRYMGPVSDPRPGSCSGGKSS----------DKALNFMKDHFLMDEVVLPGAGRPLLVK--SNVQYTRIAVDSVQGVSGH 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 462 YH-VLFLGTDRGTVQKVVVlpTNNSVSgeLILEELEVFKNHAPIttmkisskkQQLYVSSNEGvsqvslhrchiygtaca 540
Cdd:cd11256   382 NYtVMFLGTDKGFLHKAVL--MGGSES--HIIEEIELLTPPEPV---------ENLLLAANEG----------------- 431
                         490
                  ....*....|..
gi 1189690239 541 dCCLARDPYCAW 552
Cdd:cd11256   432 -VVYIGYSAGVW 442
Sema_6D cd11269
The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed ...
66-502 1.78e-87

The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed predominantly in the nervous system during embryogenesis and it uses Plexin-A1 as a receptor. It displays repellent activity for dorsal root ganglion axons. Sema6D also acts as a regulator of late phase primary immune responses. In addition, Sema6D is overexpressed in gastric carcinoma, indicating that it may have an important role in the occurrence and development of the cancer. Sema6D is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200530 [Multi-domain]  Cd Length: 465  Bit Score: 283.84  E-value: 1.78e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  66 SHHPLDYRilLMDEDQDRIYVGSKDHILSLNINNISQEALS----VFWPASTIKVEECKMAGKDPTHgCGNFVRVIQTFN 141
Cdd:cd11269     5 SQHRLDFQ--LMLKIRDTLYIAGRDQVYTVNLNEVPKTEVTpsrkLTWRSRQQDRENCAMKGKHKDE-CHNFIKVFVPRN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 142 RTHLYVCGSGAFSPVCTYLNRgrrsedQVFMIDSKCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLT 221
Cdd:cd11269    82 DEMVFVCGTNAFNPMCRYYRL------STLEYDGEEISGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 222 KRNAVRTDQHNSKWLSEPMFVdaHVIPDGTdpndaKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNK-WTT 300
Cdd:cd11269   156 DGSALRTIKYDSKWIKEPHFL--HAIEYGN-----YVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSQRVLEKhWTS 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 301 FLKARLVCSVTDEDGpeTHFDELEDVFLLETDNPRTTLVyGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNHQ 380
Cdd:cd11269   229 FLKARLNCSVPGDSF--FYFDVLQSITDIIEINGIPTVV-GVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSV 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 381 LISY-QGRIPYPRPGTCPGGAFTPNMRTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDYKYTKIAVDRVNAAD 459
Cdd:cd11269   306 WTAVpEDKVPKPRPGCCAKHGLAEAYKTSIDFPDETLSFIKSHPLMDSAVPSIIEEPWFTKTRVRYRLTAIAVDHAAGPH 385
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1189690239 460 GRYHVLFLGTDRGTVQKVVVLPTNNSVSGELILEELEVFkNHA 502
Cdd:cd11269   386 QNYTVIFVGSEAGVVLKILAKTSPFSLNDSVLLEEIEAY-NHA 427
Sema_5 cd11241
The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins ...
69-529 9.35e-87

The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins are transmembrane glycoproteins characterized by unique thrombospondin specific repeats in the extracellular region of the protein. There are three subfamilies in class 5 semaphorins, namely 5A, 5B and 5C. Sema5A and Sema5B function as guidance cues for optic and corticofugal nerve development, respectively. Sema5A-induced cell migration requires Met signaling. Sema5C is an early development gene and may play a role in odor-guided behavior. Sema5A is also implicated in cancer. In a screening model for metastasis, the Drosophila Sema5A ortholog, Dsema-5C, has been found to be required in tumorigenicity and metastasis. Sema5A is highly expressed in human pancreatic cancer cells and is associated with tumor growth, invasion and metastasis. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200502  Cd Length: 438  Bit Score: 280.98  E-value: 9.35e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  69 PLDYRILLMDEDQDRIYVGSKDHILSLNINNISQ-EALSvfWPASTIKVEECKMAGKDpTHGCGNFVRVIQTFNRThLYV 147
Cdd:cd11241     6 VSDFSRLVLDPTHDQLIVGARNYLFRLRLQSLSLlQAVP--WNSDEDTKRQCQSKGKS-VEECQNYVRVLLVVGKN-LFT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 148 CGSGAFSPVCTYlnrgRRSEDQVFMIDSKceSGKGRCSFNPNVNTVSVMINE-ELFSGMYIDFMGTDAAIFRSLTKRNAV 226
Cdd:cd11241    82 CGTYAFSPVCTI----RKLSNLTQILDTI--SGVARCPYSPAHNSTALISASgELYAGTVYDFSGRDPAIYRSLGGKPPL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 227 RTDQHNSKWLSEPMFVDAHVIPDGTdpndakvYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTFLKARL 306
Cdd:cd11241   156 RTAQYNSKWLNEPNFVGSYEIGNHT-------YFFFRENAVEHQDCGKTVYSRIARVCKNDIGGRFLLEDTWTTFMKARL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 307 VCSVTDEdgPETHFDELEDVFLLetdnPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNhqliSYQG 386
Cdd:cd11241   229 NCSLPGE--FPFYYNEIQGTFYL----PETDLIYAVFTTNVNGIAGSAICAFNLSAINQAFNGPFKYQENNG----SAWL 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 387 RIPYPRPGTCPGGAFT--PNMRTTKEFPDDVVTFIrnhpLMYNSIYPIHKRPLIVRigTDYKYTKIAVDRVNAADGR-YH 463
Cdd:cd11241   299 PTPNPHPNFQCTTSIDrgQPANTTERDLQDAQKYQ----LMAEVVQPVTKIPLVTM--DDVRFSKLAVDVVQGRGTQlVH 372
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189690239 464 VLFLGTDRGTVQKVVVLPTNnsvSGELILEELEVF--KNHAPITTMKISSKKQQLYVSSNEGVSQVSL 529
Cdd:cd11241   373 IFYVGTDYGTILKMYQPHRS---QKSCTLEEIKILpaMKGEPITSLQFLKSEKSLFVGLETGVLRIPL 437
Sema_4F cd11261
The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in ...
68-527 1.31e-83

The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in heterotypic cell-cell contacts and controls cell proliferation and suppresses tumorigenesis. In neurofibromatosis type 1 (NF1) patients, reduced Sema4F level disrupts Schwann cell/axonal interactions. Experiments using a yeast two-hybrid system show that the extreme C-terminus of Sema4F interacts with the PDZ domains of post-synaptic density protein SAP90/PSD-95, indicating possible functional involvement of Semas4F at glutamatergic synapses. Recent work also suggests a role for Sema4F in the injury response of intramedullary axotomized motoneuron. Sema4F belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulator molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200522 [Multi-domain]  Cd Length: 460  Bit Score: 273.68  E-value: 1.31e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  68 HPLDYRILLMDEDQDRIYVGSKDHILSLNINNISQEALSVFWPASTIKVEECKMAGKDPTHgCGNFVRVIQTFNRTHLYV 147
Cdd:cd11261    10 HTYNYSVLLVDPASHTLYVGARDAIFALTLPFSGERPRRIDWMVPEAHRQNCRKKGKKEAE-CHNFIRILAIANASHLLT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 148 CGSGAFSPVCTYLNRGRrsedqvFMIDSKCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTK-RNAV 226
Cdd:cd11261    89 CGTFAFDPKCGVIDVSS------FQQVERLESGRGKCPFEPAQRSAAIMAGGVLYAATVKNFLGTEPIISRAVGRaEEWI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 227 RTDQHNSkWLSEPMFVDAHVI---PDGTDPNDAKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTFLK 303
Cdd:cd11261   163 RTETLPS-WLNAPAFVAAVFLspaEWGDEDGDDEIYFFFTETAREYDSYERIKVPRVARVCAGDLGGRKTLQQRWTTFLK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 304 ARLVCSvtdedGPE--THFDELEDVFLLET-DNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAH-KEGPNH 379
Cdd:cd11261   242 ADLLCP-----GPEhgRASSILQDVTTLRPlPGAGTPIFYGIFSSQWEGASISAVCAFRPQDIRRVMNGPFREfKHDCNR 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 380 QLISYQGRIPYPRPGTCpggaFTPNMR-----TTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVriGTDYKYTKIAVDR 454
Cdd:cd11261   317 GLPVMDSDVPQPRPGEC----ITNNMKllgfgSSLSLPDRVLTFVRDHPLMDRPVFPADGHPLLV--TTDTAYLRVAAHR 390
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189690239 455 VNAADGR-YHVLFLGTDRGTVQKVVVLPTNNSVsgeliLEELEVFKNHAPITTMKIssKKQQLYVSSNEGVSQV 527
Cdd:cd11261   391 VTSLSGKeYDVLYLGTEDGHLHRAVRIGAQLSV-----LEDLALFPEPQPVENLQL--HHNWLLVGSDTEVTQI 457
Sema_6A cd11266
The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, ...
64-529 3.12e-82

The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, Sema6A-plexin A2 signaling modulates granule cell migration by controlling centrosome positioning. Besides plexin A2, plexin A4 is also found to be a receptor of Sema6A. Interactions between plexin A2, plexin A4, and Sema6A control lamina-restricted projection of hippocampal mossy fibers. It is required for the clustering of boundary cap cells at the PNS/CNS interface and thus, prevents motoneurons from streaming out of the ventral spinal cord. At the dorsal root entry site, it organizes the segregation of dorsal roots. Sema6A may also be involved in axonal pathfinding processes in the periinfarct and homotopic contralateral cortex. Sema6A is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200527 [Multi-domain]  Cd Length: 466  Bit Score: 269.98  E-value: 3.12e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  64 SLSHHPLDYRILLMDEDQdrIYVGSKDHILSLNINNISQEAL----SVFWPASTIKVEECKMAGKDPTHgCGNFVRVIQT 139
Cdd:cd11266     3 TTQRHRLDIQMIMIMNRT--LYIAARDHIYTVDIDTSHTEEIyfskKLTWKSRQADVDTCRMKGKHKDE-CHNFIKVLLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 140 FNRTHLYVCGSGAFSPVCtylnRGRRSEDQVFMIDSKceSGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRS 219
Cdd:cd11266    80 RNDDTLFVCGTNAFNPSC----RNYKMDTLEFFGDEF--SGMARCPYDAKHANVALFADGKLYSATVTDFLAIDAVIYRS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 220 LTKRNAVRTDQHNSKWLSEPMFVDAhvipdgTDPNDAkVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGG-LRSLVNKW 298
Cdd:cd11266   154 LGDSPTLRTVKHDSKWLKEPYFVQA------VDYGDY-IYFFFREIAVEYNSMGKVVFPRVAQVCKNDMGGsQRVLEKQW 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 299 TTFLKARLVCSVTDEDgpETHFDELEDVFLLETDNPRTtLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPN 378
Cdd:cd11266   227 TSFLKARLNCSVPGDS--HFYFNILQAVTDVIHINGRD-VVLATFSTPYNSIPGSAVCAYDMLDIASVFTGRFKEQKSPD 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 379 HQLISY-QGRIPYPRPGTCPGGAFTPNMRTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDYKYTKIAVDRVNA 457
Cdd:cd11266   304 STWTPVpDERVPKPRPGCCAGSSSLEKYATSNEFPDDTLNFIKTHPLMDEAVPSIINRPWFLRTMVRYRLTKIAVDNAAG 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 458 ADGRYHVLFLGTDRGTVQKVVVLPTNNS-VSGELILEELEVFKNH---------APITTMKISSKKQQLYVSSNEGVSQV 527
Cdd:cd11266   384 PYQNHTVVFLGSEKGIILKFLARTGNSGfLNDSLFLEEMNVYNSEkcsydgvedKRIMGMQLDKASSALYVAFSTCVIKV 463

                  ..
gi 1189690239 528 SL 529
Cdd:cd11266   464 PL 465
Sema_5A cd11263
The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse ...
70-529 1.40e-80

The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse Sema5A was identified as a protein that induces inhibitory responses during optic nerve development. Recent studies show that Sema5A controls innate immunity in mice. It also has been identified as a candidate gene for causing idiopathic autism in humans. Plexin B3 functions as a binding partner and receptor for Sema5A. Furthermore, Sema5A is also implicated in cancer. The role of the Drosophila Sema5A ortholog, Dsema-5C, in tumorigenicity and metastasis has been reported. Sema5A is highly expressed in human pancreatic cancer cells and is associated with tumor growth, invasion and metastasis. Sema5A belongs to class 5 semaphorin family of proteins, which are transmembrane glycoproteins characterized by unique thrombospondin specific repeats in the extracellular region of the protein. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200524 [Multi-domain]  Cd Length: 436  Bit Score: 264.58  E-value: 1.40e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  70 LDYRILLMDEDQDRIYVGSKDHILSLNINNIS--QEalsVFWPASTIKVEECKMAGKDPTHgCGNFVRVIqTFNRTHLYV 147
Cdd:cd11263     7 VDFSQLTFDPGQKELIVGARNYLFRLQLEDLSliQA---VEWECDEATKKACYSKGKSKEE-CQNYIRVL-LVGGDRLFT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 148 CGSGAFSPVCT--YLNRGRRSEDQVfmidskceSGKGRCSFNPNVNTVSVMINE-ELFSGMYIDFMGTDAAIFRSLTKRN 224
Cdd:cd11263    82 CGTNAFTPICTnrTLNNLTEIHDQI--------SGMARCPYSPQHNSTALLTSSgELYAATAMDFPGRDPAIYRSLGILP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 225 AVRTDQHNSKWLSEPMFVDAHVIPDGTdpndakvYFFFKEKLTDNNrSTKQIHSMIARICPNDTGGLRSLVNKWTTFLKA 304
Cdd:cd11263   154 PLRTAQYNSKWLNEPNFVSSYDIGNFT-------YFFFRENAVEHD-CGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKA 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 305 RLVCSVTDEdgPETHFDELEDVFLLetdnPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGpnhqliSY 384
Cdd:cd11263   226 RLNCSRPGE--IPFYYNELQSTFFL----PELDLIYGIFTTNVNSIAASAVCVFNLSAISQAFNGPFKYQEN------SR 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 385 QGRIPYPRP------GTCPGGAFtpnMRTTKEFPDDVVTFIrnhpLMYNSIYPIHKRPLIVRigTDYKYTKIAVDRVNAA 458
Cdd:cd11263   294 SAWLPYPNPnpnfqcGTMDQGLY---VNLTERNLQDAQKFI----LMHEVVQPVTPVPYFME--DNSRFSHVAVDVVQGK 364
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189690239 459 DGRYHVLFLGTDRGTVQKVVVlPTNNSvSGELILEELEVF--KNHAPITTMKISSKKQQLYVSSNEGVSQVSL 529
Cdd:cd11263   365 DMLFHIIYLATDYGTIKKVLA-PLNQS-SSSCLLEEIELFpkRQREPIRSLQILHSQSVLFVGLQEHVIKIPL 435
Sema_5B cd11264
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed ...
71-529 1.93e-80

The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed in regions of the basal telencephalon in rat. Sema5B is an inhibitory cue for corticofugal axons and acts as a source of repulsion for the appropriate guidance of cortical axons away from structures such as the ventricular zone as they navigate toward and within subcortical regions. In addition to its role as a guidance cue, Sema5B regulates the development and maintenance of synapse size and number in hippocampal neurons. In addition, the sema domain of Sema5B can be cleaved of the whole protein and exerts its function in regulation of synapse morphology. Sema5B belongs to the class 5 semaphorin family of proteins, which are transmembrane glycoproteins characterized by unique thrombospondin specific repeats in the extracellular region of the protein. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200525 [Multi-domain]  Cd Length: 437  Bit Score: 264.54  E-value: 1.93e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  71 DYRILLMDEDQDRIYVGSKDHILSLNINNISQeALSVFWPASTIKVEECKMAGKDPTHgCGNFVRVIqTFNRTHLYVCGS 150
Cdd:cd11264     8 DFSQLALDLNRNQLIVGARNYLFRLSLHNVSL-IQATEWGSDEDTRRSCQSKGKTEEE-CQNYVRVL-IVYGKKVFTCGT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 151 GAFSPVCTYLNRGRRSEdqvfMIDSKceSGKGRCSFNPNVNTVSVMINE-ELFSGMYIDFMGTDAAIFRSLTKRNAVRTD 229
Cdd:cd11264    85 NAFSPVCTSRQVGNLSK----VIERI--NGVARCPYDPRHNSTAVITSRgELYAATVIDFSGRDPAIYRSLGSVPPLRTA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 230 QHNSKWLSEPMFVDAHVIPDGTdpndakvYFFFKEKLTDNNrSTKQIHSMIARICPNDTGGLRSLVNKWTTFLKARLVCS 309
Cdd:cd11264   159 QYNSKWLNEPNFIAAYDIGLFT-------YFFFRENAVEHD-CGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCS 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 310 VTDEdgPETHFDELEDVFLLetdnPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNHQLISYQGRIP 389
Cdd:cd11264   231 RPGE--IPFYYNELQSTFYL----PEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIP 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 390 YPRPGTCPGGAftPNMRTTKEFPDDVVTFIrnhpLMYNSIYPIHKRPLIVRigTDYKYTKIAVDRVNAADGRYHVLFLGT 469
Cdd:cd11264   305 NFQCGTLSDDS--PNENLTERSLQDAQRLF----LMNDVVQPVTVDPLVTQ--DSVRFSKLVVDIVQGKDTLYHVMYIGT 376
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189690239 470 DRGTVQKVVVlPTNNSVSGeLILEELEVFK--NHAPITTMKISSKKQQLYVSSNEGVSQVSL 529
Cdd:cd11264   377 EYGTILKALS-TTNRSLRS-CYLEEMQILPpgQREPIRSLQILHSDRSLFVGLNNGVLKIPL 436
Sema_6B cd11267
The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as ...
84-499 1.65e-76

The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as repellents for axon growth; this repulsive activity is mediated by its receptor Plexin A4. Sema6B is expressed in CA3, and repels mossy fibers in a Plexin A4 dependent manner. In human, it was shown that peroxisome proliferator-activated receptors (PPARs) and 9-cis-retinoic acid receptor (RXR) regulate human semaphorin 6B (Sema6B) gene expression. Sema6B is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200528 [Multi-domain]  Cd Length: 466  Bit Score: 254.76  E-value: 1.65e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  84 IYVGSKDHILSLNINNISQEAL----SVFWPASTIKVEECKMAGKDPTHgCGNFVRVIQTFNRTHLYVCGSGAFSPVCty 159
Cdd:cd11267    21 LYIGDRDNLYRVELDPTAGTEMryhkKLTWRSNKNDINVCRMKGKHEGE-CRNFIKVLLLRDYGTLFVCGTNAFNPVC-- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 160 lnrGRRSEDQVFMIDSKCeSGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTKRNAVRTDQHNSKWLSEP 239
Cdd:cd11267    98 ---ANYSIDTLEPVGDNI-SGMARCPYDPKHANVALFADGMLFTATVTDFLAIDAVIYRSLGDSPALRTVKHDSKWFKEP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 240 MFVdaHVIPDGTdpndaKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGG-LRSLVNKWTTFLKARLVCSVTDEDgpET 318
Cdd:cd11267   174 YFV--HAVEWGS-----HVYFFFREIAMEFNYLEKVVVSRVARVCKNDMGGsQRVLEKQWTSFLKARLNCSVPGDS--HF 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 319 HFDELEDVFLLETDNPRTtLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNHQLISY-QGRIPYPRPGTCP 397
Cdd:cd11267   245 YFNVLQAVSDILNLGGRP-VVLAVFSTPTNSIPGSAVCAFDMTQVAAVFEGRFREQKSPESIWTPVpEELVPRPRPGCCA 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 398 GgaftPNMR--TTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDYKYTKIAVDRVNAADGRYHVLFLGTDRGTVQ 475
Cdd:cd11267   324 A----PGMRynSSSTLPDEVLNFVKTHPLMDEAVPSLGHAPWIVRTMTRYQLTHMVVDTEAGPHGNHTVVFLGSTRGTVL 399
                         410       420
                  ....*....|....*....|....*..
gi 1189690239 476 KVVVLPTNNSVSG---ELILEELEVFK 499
Cdd:cd11267   400 KFLIIPNASSSEIsnqSVFLEELETYN 426
Sema_5C cd11265
The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, ...
69-524 1.42e-73

The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, Sema5C was identified as an early development gene, which is expressed in stage 2 embryos with a striped pattern emerging at later stages. Sema5c may play a role in odor-guided behavior and in tumorigenesis. Sema5C belongs to class 5 semaphorin family of proteins, which are transmembrane glycoproteins characterized by unique thrombospondin specific repeats in the extracellular region of the protein. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200526 [Multi-domain]  Cd Length: 433  Bit Score: 245.85  E-value: 1.42e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  69 PLDYRILLMDEDQDRIYVGSKDHILSLNINNISQ-EALSvfWPASTIKVEECKMAGKDpTHGCGNFVRVIQTfNRTHLYV 147
Cdd:cd11265     6 VTSYSQMLFDVARNQVIVGARDNLYRLSLDGLELlERAS--WPAAESKVALCQNKGQS-EEDCHNYVKVLLS-YGKQLFA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 148 CGSGAFSPVCTYlnrgRRSEDqvfmIDSKCE--SGKGRCSFNPNVNTVSVM-INEELFSGMYIDFMGTDAAIFRSLTKRN 224
Cdd:cd11265    82 CGTNAFSPRCSW----REMEN----LTSVTEwdSGVAKCPYSPHANITALLsSSGQLFVGSPTDFSGSDSAIYRTLGTSN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 225 A--VRTDQHNSKWLSEPMFVdahvipdGTDPNDAKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLV-NKWTTF 301
Cdd:cd11265   154 KsfLRTKQYNSKWLNEPQFV-------GSFETGNFVYFLFRESAVEYMNCGKVIYSRIARVCKNDVGGGTMLLkDNWTTF 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 302 LKARLVCSVTDEdgPETHFDELEDVFLLETDNprttLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNhql 381
Cdd:cd11265   227 LKARLNCSLPGE--YPFYFDEIQGMTYLPDEG----ILYATFTTPENSIAGSAVCAFNLSSINAAFDGPFKHQESSG--- 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 382 iSYQGRIPYP---RPGTCPGGAFTPNMRTTKefpddvvtfirnHPLMYNSIYPIHKRPLIVRigTDYKYTKIAVDRVNAA 458
Cdd:cd11265   298 -AAWERVNVNhrdHFNQCSSSSSSHLLESSR------------YQLMDEAVQPITLEPLHHA--KLERFSHIAVDVIPTK 362
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189690239 459 -DGRYHVLFLGTDRGTVQKVVVLPTNNSVSgelILEELEVFKNHA-PITTMKISSKKQQLYVSSNEGV 524
Cdd:cd11265   363 iHQSVHVLYVATTGGLIKKISVLPRTQETC---LVEIWQPLPTPDsPIKTMQYLKVTDSLYVGTELAL 427
Sema_6E cd11270
The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed ...
66-529 4.39e-71

The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed predominantly in the nervous system during embryogenesis. It binds Plexin A1 and might utilize it as a receptor to repel axons of specific types during development. Sema6E acts as a repellent to dorsal root ganglion axons as well as sympathetic axons. Sema6E is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200531 [Multi-domain]  Cd Length: 462  Bit Score: 240.01  E-value: 4.39e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  66 SHHPLDYRILLmdEDQDRIYVGSKDHILSLNINNiSQEAL----SVFWpaSTIKVEECKMAGKDPTHgCGNFVRVIQTFN 141
Cdd:cd11270     5 ARLGLDFQRML--RINHMVYIAARDHVFAINLSA-SLERIvpqqKLTW--KTKDVEKCTVRGKNSDE-CYNYIKVLVPRN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 142 RTHLYVCGSGAFSPVC-TYLNRGRRSEDQVFmidskceSGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSL 220
Cdd:cd11270    79 DETLFACGTNAFNPTCrNYKMSSLEQDGEEV-------IGQARCPFESRQSNVGLFAGGDFYSATMTDFLASDAVIYRSL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 221 TKRNAV-RTDQHNSKWLSEPMFVdaHVIPDGTdpndaKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGL-RSLVNKW 298
Cdd:cd11270   152 GESSPVlRTVKYDSKWLREPHFL--HAIEYGN-----YVYFFLSEIAVEYTTLGKVVFSRVARVCKNDNGGSpRVLERYW 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 299 TTFLKARLVCSVTDEDGpeTHFDELEDVFLLETDNPRTTLVyGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPN 378
Cdd:cd11270   225 TSFLKARLNCSVPGDSF--FYFDVLQSLTNVMQINHRPAVL-GVFTTQANSITGSAVCAFYMDDIEKVFNGKFKEQRNSE 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 379 HQLISY-QGRIPYPRPGTCPGGAFTPNMRTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDYKYTKIAVDRVNA 457
Cdd:cd11270   302 SAWTPVpDEAVPKPRPGSCAGDGPAAGYKSSTNFPDETLTFIKSYPLMDEAVPSVNNRPCFTRTTSRFKLTQIAVDTAAG 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 458 ADGRYHVLFLGTDRGTVQKVVVLPTNNSVSGELILEELEVF--------KNHAPITTMKISSKKQQLYVSSNEGVSQVSL 529
Cdd:cd11270   382 PYKNYTVVFLGSENGHVLKVLASMHPNSSYSTQVLEDIDVYnpnkcnvrGEDRRILGLELDKDHHALFVAFTGCVIRVPL 461
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
72-529 9.12e-70

The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); Sema7A plays regulatory roles in both immune and nervous systems. Unlike other semaphorins, which act as repulsive guidance cues, Sema7A enhances central and peripheral axon growth and is required for proper axon tract formation during embryonic development. Sema7A also plays a critical role in the negative regulation of T cell activation and function. Sema7A is a membrane-anchored member of the semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200504 [Multi-domain]  Cd Length: 414  Bit Score: 235.12  E-value: 9.12e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  72 YRILLMDEDQDRIYVGSKDHILSLNI--NNISQEalsvfwpasTIKVEECKMAGKDPTHG--CGNFVRVIQTFNRThLYV 147
Cdd:cd11243     4 YPVFFHEAGSSSVYVGGQGALYLLDFtgSAVIVK---------KIPDEKTEKDCKKRATLddCENYITLIKKLDYR-LLV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 148 CGSGAFSPVCTYLNRGRRSEDQvfmidskceSGKGRCSFNPNVNTVSVMINEELFSGmyIDFMGTDAAIFRSLTKRNAVR 227
Cdd:cd11243    74 CGTNAGSPKCWFLVNQTLVTLS---------ADRGVAPFLPDENSLVLIEGNNVYST--ISGKKGNIPRFRRYGGKKELY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 228 TDqhnSKWLSEPMFVDAHVIPDgTDPNDAKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSL-VNKWTTFLKARL 306
Cdd:cd11243   143 TS---DTVMQKPQFVKATLLPE-DEQYQDKIYYFFREDNEDKGPEAEPNISRVARLCKEDQGGTSSLsTSKWSTFLKARL 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 307 VCSVTDEDGpetHFDELEDVFLLETDNPRTTLVYGIFTtssSVFKGSAVCVYHLSDIQTVFNgpfahkegpNHQLISYQG 386
Cdd:cd11243   219 VCGDPATPM---NFNRLQDVFLLPKEEWREAVVYGVFS---NTWGSSAVCSYSLGDIDKVFR---------TSSLKGYSG 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 387 RIPYPRPGTCpggafTPNMRTTkefPDDVVTFIRNHPLMYNSIYPIHKRPLIVrIGTDYKYTKIAVDRVNAADGR-YHVL 465
Cdd:cd11243   284 SLPNPRPGTC-----VPPEQTH---PSETFSFADEHPELDDRIEPDEPRKLPV-FQNKDHYQKVVVDEVRASDGVsYDVL 354
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189690239 466 FLGTDRGTVQKVVVLPtnnsvSGELILEELEVFKNHAPITTMKISSKKQQLYVSSNEGVSQVSL 529
Cdd:cd11243   355 YLATDKGKIHKVVESK-----GQTHNIMEIQPFKEQEPIQSMILDAERSHLYVGTKAEVTRLPL 413
Sema_6C cd11268
The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called ...
84-498 9.67e-65

The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called semaphorin Y); Sema6C is highly expressed in adult brain and skeletal muscle and it shows growth cone collapsing activity. It may play a role in the maintenance and remodelling of neuronal connections. In adult skeletal muscle, this role includes prevention of motor neuron sprouting and uncontrolled motor neuron growth. The expression of Sema6C in adult skeletal muscle is down-regulated following denervation. Sema6C is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200529 [Multi-domain]  Cd Length: 465  Bit Score: 223.04  E-value: 9.67e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  84 IYVGSKDHILSLNINniSQEALSVFWPASTIK-----VEECKMAGKdPTHGCGNFVRVIQTFNRTHLYVCGSGAFSPVCT 158
Cdd:cd11268    21 LLVAARDHVFSFDLQ--AEEEGEGLVPNKYLTwrsqdVENCAVRGK-LTDECYNYIRVLVPWDSQTLLACGTNSFSPVCR 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 159 ylNRGRRSEDQvfmiDSKCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTKRNAVRTDQHNSKWLSE 238
Cdd:cd11268    98 --SYGITSLQQ----EGEELSGQARCPFDATQSNVAIFAEGSLYSATAADFQASDAVVYRSLGPQPPLRSAKYDSKWLRE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 239 PMFVdaHVIPDGTdpndaKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGL-RSLVNKWTTFLKARLVCSVTDEDgpE 317
Cdd:cd11268   172 PHFV--QALEHGD-----HVYFFFREVSVEDARLGRVQFSRVARVCKRDMGGSpRALDRHWTSFLKLRLNCSVPGDS--T 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 318 THFDELEDVFLLETDNPRTTLvYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNHQLISY-QGRIPYPRPGTC 396
Cdd:cd11268   243 FYFDVLQALTGPVNLHGRSAL-FGVFTTQTNSIPGSAVCAFYLDEIERGFEGKFKEQRSLDGAWTPVsEDRVPSPRPGSC 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 397 PGGAFTPNMRTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVrIGTDYKYTKIAVDRVNAADGRYHVLFLGTDRGTVQK 476
Cdd:cd11268   322 AGVGGAALFSSSRDLPDDVLTFIKAHPLLDPAVPPVTHQPLLT-LTSRALLTQVAVDGMAGPHSNITVMFLGSNDGTVLK 400
                         410       420
                  ....*....|....*....|....
gi 1189690239 477 vvVLPTNNSVSG--ELILEELEVF 498
Cdd:cd11268   401 --VLPPGGRSGGpePILLEEIDAY 422
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
71-529 9.69e-63

The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins and plexins have a Sema domain on their N-termini. Plexins function as receptors for the semaphorins. Evolutionarily, plexins may be the ancestor of semaphorins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems, and cancer. Semaphorins can be divided into 7 classes. Vertebrates have members in classes 3-7, whereas classes 1 and 2 are known only in invertebrates. Class 2 and 3 semaphorins are secreted; classes 1 and 4 through 6 are transmembrane proteins; and class 7 is membrane associated via glycosylphosphatidylinositol (GPI) linkage. Plexins are a large family of transmembrane proteins, which are divided into four types (A-D) according to sequence similarity. In vertebrates, type A plexins serve as co-receptors for neuropilins to mediate the signalling of class 3 semaphorins. Plexins serve as direct receptors for several other members of the semaphorin family: class 6 semaphorins signal through type A plexins and class 4 semaphorins through type B plexins. This family also includes the MET and RON receptor tyrosine kinases. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves to recognize and bind receptors.


Pssm-ID: 200495 [Multi-domain]  Cd Length: 392  Bit Score: 215.53  E-value: 9.69e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  71 DYRILLMDEDQDRIYVGSKDHILSLNINNISQEAL----SVFWPASTIKVEECKMAGKDPTHgCGNFVRVIQTFNR-THL 145
Cdd:cd09295     1 DDDKILVSFRKDTIYVGAIARIYKVDGGGTRLLLScispELNFGFNEDQKAFCPLRRGKWTE-CINYIKVLQQKGDlDIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 146 YVCGSGAFSPVCTYLnrgrRSEDQVFMIDSKCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFM-GTDAAIFRSLTKRN 224
Cdd:cd09295    80 AVCGSNAAQPSCGSY----RLDVLVELGKVRWPSGRPRCPIDNKHSNMGVNVDSKLYSATDHDFKdGDRPALSRRSSNVH 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 225 AVRTDQHNSKWLSEPMFVDAHVipdGTDPNDaKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTFLKA 304
Cdd:cd09295   156 YLRIVVDSSTGLDEITFVYAFV---SGDDDD-EVYFFFRQEPVEYLKKGMVYVPRIARVCKLDVGGCHRLKKKLTSFLKA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 305 RLVCSVTDEDgpeTHFDELEDVFLLETDNPRtTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFngpfahkegpnhqlisy 384
Cdd:cd09295   232 DLNCSRPQSG---FAFNLLQDATGDTKNLIQ-DVKFAIFSSCLNKSVESAVCAYLFTDINNVF----------------- 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 385 qgripyprpgtcpggaftpnmrttkefpDDVVTFIRNhplmynsiypihkRPLIVRIGTDYKYTKIAVDRVNAADGRYHV 464
Cdd:cd09295   291 ----------------------------DDPVEAINN-------------RPLYAHQNQRSRLTSIAVDATKQKSVGYQV 329
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189690239 465 LFLGTDRGTVQKVVVLptnNSVSGELILEELEVFKNHAPITTMKISSKKQQLYVSSNEGVSQVSL 529
Cdd:cd09295   330 VFLGLKLGSLGKALAF---FFLYKGHIIEEWKVFKDSSRITNLDLSRPPLYLYVGSESGVLGVPV 391
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
592-682 1.81e-43

Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed of the immunoglobulin (Ig)-like domain of Sema3 and similar proteins. Semaphorins are classified based on structural features additional to the Sema domain. Sema3 is a Class III semaphorin that is secreted. It is a vertebrate class having a Sema domain, an Ig domain, a short basic domain. They have been shown to be axonal guidance cues and have a part in the regulation of the cardiovascular, immune, and respiratory systems. Sema3A, the prototype member of this class III subfamily, induces growth cone collapse and is an inhibitor of axonal sprouting. In perinatal rat cortex, it acts as a chemoattractant and functions to direct the orientated extension of apical dendrites. It may play a role, prior to the development of apical dendrites, in signaling the radial migration of newborn cortical neurons towards the upper layers. Sema3A selectively inhibits vascular endothelial growth factor receptor (VEGF)-induced angiogenesis and induces microvascular permeability. This group also includes Sema3B, -C, -D, -E, -G.


Pssm-ID: 409455  Cd Length: 92  Bit Score: 151.73  E-value: 1.81e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 592 NAAEIVQYGVKNNTTFLECAPKSPQASIKWLLQKDKDRRK-EVKLNERIIATSQGLLIRSVQGSDQGLYHCIATENSFKQ 670
Cdd:cd05871     1 NAEEKVVYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKeEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQ 80
                          90
                  ....*....|..
gi 1189690239 671 TIAKINFKVLDS 682
Cdd:cd05871    81 TLVKIRLHVIEP 92
Sema_plexin_A2 cd11272
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
462-559 8.99e-11

The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor for class 6 semaphorins. Interactions between Plexin A2, A4 and semaphorins 6A and 6B control the lamina-restricted projection of hippocampal mossy fibers. Sema6B also repels the growth of mossy fibers in a Plexin A4 dependent manner. Plexin A2 does not suppress Sema6B function. In addition, studies have shown that Plexin A2 may be related to anxiety and other psychiatric disorders. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200533 [Multi-domain]  Cd Length: 515  Bit Score: 64.95  E-value: 8.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 462 YHVLFLGTDRGTVQKVVVlptNNSVSGELILEELEVFKNHAPI-TTMKISSKKQQLYVSSNEGVSQVSLHRCHIYgTACA 540
Cdd:cd11272   406 YSVVFVGTKSGKLKKIRA---DGPPHGGVQYEMVSVFKDGSPIlRDMAFSIDHKYLYVMSERQVSRVPVESCEQY-TTCG 481
                          90       100
                  ....*....|....*....|.
gi 1189690239 541 DCCLARDPYCAWDG--HSCSR 559
Cdd:cd11272   482 ECLSSGDPHCGWCAlhNMCSR 502
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
595-681 7.80e-09

Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are composed of the immunoglobulin (Ig)-like domain in semaphorins. Semaphorins are transmembrane protein that have important roles in a variety of tissues. Functionally, semaphorins were initially characterized for their importance in the development of the nervous system and in axonal guidance. Later they have been found to be important for the formation and functioning of the cardiovascular, endocrine, gastrointestinal, hepatic, immune, musculoskeletal, renal, reproductive, and respiratory systems. Semaphorins function through binding to their receptors and transmembrane semaphorins also serves as receptors themselves. Although molecular mechanism of semaphorins is poorly understood, the Ig-like domains may be involved in ligand binding or dimerization.


Pssm-ID: 409368  Cd Length: 88  Bit Score: 53.23  E-value: 7.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 595 EIVQYGvknNTTFLECAPKSPQASIKWLLQKdkdRRKEVKLNER-IIATSQGLLIRSVQGSDQGLYHCIATENSFKQTIA 673
Cdd:cd04979     6 ISVKEG---DTVILSCSVKSNNAPVTWIHNG---KKVPRYRSPRlVLKTERGLLIRSAQEADAGVYECHSGERVLGSTLR 79

                  ....*...
gi 1189690239 674 KINFKVLD 681
Cdd:cd04979    80 SVTLHVLE 87
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
531-568 1.40e-07

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 48.31  E-value: 1.40e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1189690239  531 RCHIYGTaCADCCLARDPYCAWD--GHSCSRFYPTGKRRS 568
Cdd:smart00423   1 RCSKYTS-CSECLLARDPYCAWCssQGRCTSGERCDSRRQ 39
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
580-664 1.59e-06

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 46.73  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 580 TQCRGFNLkayrnaaeIVQYGvkNNTTFLECAPKSPQASIKWLlqKDKDRRKEVKLNERIIATSQGLLIRSVQGSDQGLY 659
Cdd:cd20970     5 TPQPSFTV--------TAREG--ENATFMCRAEGSPEPEISWT--RNGNLIIEFNTRYIVRENGTTLTIRNIRRSDMGIY 72

                  ....*
gi 1189690239 660 HCIAT 664
Cdd:cd20970    73 LCIAS 77
Sema_plexin_like cd11236
The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine ...
75-530 9.53e-06

The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine kinases; Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestor of semaphorins. Ligand binding activates signal transduction pathways controlling axon guidance in the nervous system and other developmental processes including cell migration and morphogenesis, immune function, and tumor progression. Plexins are divided into four types (A-D) according to sequence similarity. In vertebrates, type A Plexins serve as the co-receptors for neuropilins to mediate the signalling of class 3 semaphorins except Sema3E, which signals through Plexin D1. Plexins serve as direct receptors for several other members of the semaphorin family: class 6 semaphorins signal through type A plexins and class 4 semaphorins through type B. Plexin C1 serves as the receptor of Sema7A and plays regulation roles in both immune and nervous systems. This family also includes the Met and RON receptor tyrosine kinases. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200497 [Multi-domain]  Cd Length: 401  Bit Score: 48.48  E-value: 9.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239  75 LLMDEDQDRIYVGSKDHILSLNINNISQEALSV---------FWPASTIKVEEckmagKDPTHgcgNFVRVIQTFNR-TH 144
Cdd:cd11236     5 LAVDNSTGRVYVGAVNRLYQLDSSLLLEAEVSTgpvldsplcLPPGCCSCDHP-----RSPTD---NYNKILLIDYSsGR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 145 LYVCGSgAFSPVCTYLNRGRRSEDQVFMIDSkcesgkgRCSFNPNVNTVSVMINEELFSG--MYIdfmgtdAAIFRSLTK 222
Cdd:cd11236    77 LITCGS-LYQGVCQLRNLSNISVVVERSSTP-------VAANDPNASTVGFVGPGPYNNEnvLYV------GATYTNNGY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 223 RN---AVRTDQHNSKWLSEPMFVDAH---VIPDGTDPN-----------DAKVYFFFKEKLTDNNRSTkqIHSMIARICP 285
Cdd:cd11236   143 RDyrpAVSSRSLPPDDDFNAGSLTGGsaiSIDDEYRDRysikyvygfssGGFSYFVTVQRKSVDDESP--YISRLVRVCQ 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 286 NDtgglrslvNKWTTFLKARLVCsvtdEDGPETHFDELEDVF-------LLETDNPRTT--LVYGIFTTSSSVFKG---- 352
Cdd:cd11236   221 SD--------SNYYSYTEVPLQC----TGGDGTNYNLLQAAYvgkagsdLARSLGISTDddVLFGVFSKSKGPSAEpssk 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 353 SAVCVYHLSDIQTvfngpfahkegpnhqlisyqgripyprpgtcpggaftpnmrttkefpddvvTFIRNHPLmyNSIYPI 432
Cdd:cd11236   289 SALCVFSMKDIEA---------------------------------------------------AFNDNCPL--GGGVPI 315
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 433 HKRPLIVRIgtdyKYTKIAVDRVNaadgRYHVLFLGTDRGTVQKVVVlptnNSVSGELILEELEVFKNHAPITTMKISSK 512
Cdd:cd11236   316 TTSAVLSDS----LLTSVAVTTTR----NHTVAFLGTSDGQLKKVVL----ESSSSATQYETLLVDSGSPILPDMVFDPD 383
                         490
                  ....*....|....*...
gi 1189690239 513 KQQLYVSSNEGVSQVSLH 530
Cdd:cd11236   384 GEHLYVMTPKKVTKVPVE 401
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
608-671 8.15e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 41.72  E-value: 8.15e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189690239  608 LEC-APKSPQASIKWLlqkdKDRRKEVKLNERIIATSQG----LLIRSVQGSDQGLYHCIATENSFKQT 671
Cdd:smart00410  14 LSCeASGSPPPEVTWY----KQGGKLLAESGRFSVSRSGststLTISNVTPEDSGTYTCAATNSSGSAS 78
Ig_Sema4D_like cd05873
Immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins; The members ...
604-674 1.60e-04

Immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins. Sema4D is a Class IV semaphorin. Semaphorins are classified based on structural features additional to the Sema domain. Sema4D has extracellular Sema and Ig domains, a transmembrane domain, and a short cytoplasmic domain. Sema4D plays a part in the development of GABAergic synapses. Sema4D in addition is an immune semaphorin. It is abundant on resting T cells; its expression is weak on resting B cells and antigen presenting cells (APCs), but is upregulated by various stimuli. The receptor used by Sema4D in the immune system is CD72. Sem4D enhances the activation of B cells and DCs through binding CD72, perhaps by reducing CD72s inhibitory signals. The receptor used by Sema4D in the non-lymphatic tissues is plexin-B1. Sem4D is anchored to the cell surface but its extracellular domain can be released from the cell surface by a metalloprotease-dependent process. Sem4D may mediate its effects in its membrane-bound form and/or its cleaved form.


Pssm-ID: 409457  Cd Length: 87  Bit Score: 40.95  E-value: 1.60e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189690239 604 NTTFLECAPKSPQASIKWLLQKDKDRRKevklNERIIATSQGLLIRSVQGSDQGLYHCIATENS----FKQTIAK 674
Cdd:cd05873    12 GNAELKCSPKSNLARVVWKFQGKVLKAE----SPKYGLYGDGLLIFNASEADAGRYQCLSVEKSkaktFFQTVAK 82
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
608-675 1.64e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 40.39  E-value: 1.64e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189690239 608 LEC-APKSPQASIKWLLQkDKDRRKEVKLNERIIATSQGLLIRSVQGSDQGLYHCIAtENSFKQTIAKI 675
Cdd:cd00096     3 LTCsASGNPPPTITWYKN-GKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVA-SNSAGGSASAS 69
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
599-667 3.41e-04

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 40.22  E-value: 3.41e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189690239 599 YGVKNNTTFLEC-APKSPQASIKWllqkdkdRRKEVKLNER-IIATSQGLL-IRSVQGSDQGLYHCIAtENS 667
Cdd:cd04968    12 YALKGQTVTLECfALGNPVPQIKW-------RKVDGSPSSQwEITTSEPVLeIPNVQFEDEGTYECEA-ENS 75
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
531-560 4.10e-04

Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas shows 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 38.84  E-value: 4.10e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1189690239 531 RCHIYGTaCADCCLARDPYCAWD--GHSCSRF 560
Cdd:pfam01437   1 RCSQYTS-CSSCLAARDPYCGWCssEGRCVRR 31
I-set pfam07679
Immunoglobulin I-set domain;
605-679 4.73e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 39.55  E-value: 4.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 605 TTFLECAPK-SPQASIKWLlqkdKDRrKEVKLNERIIATSQG----LLIRSVQGSDQGLYHCIATeNSFKQTIAKINFKV 679
Cdd:pfam07679  17 SARFTCTVTgTPDPEVSWF----KDG-QPLRSSDRFKVTYEGgtytLTISNVQPDDSGKYTCVAT-NSAGEAEASAELTV 90
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
605-667 5.05e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 39.40  E-value: 5.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189690239 605 TTFLEC-APKSPQASIKWLlqkdKDRRKEVKLNERIIATSQGLL-IRSVQGSDQGLYHCIATENS 667
Cdd:cd20952    16 TVVLNCqATGEPVPTISWL----KDGVPLLGKDERITTLENGSLqIKGAEKSDTGEYTCVALNLS 76
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
608-664 6.97e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 39.31  E-value: 6.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 608 LECAPK--SPQASIKWLlqkdKDRRKEVKLNERIIATSQG-LLIRSVQGSDQGLYHCIAT 664
Cdd:cd05724    17 LECSPPrgHPEPTVSWR----KDGQPLNLDNERVRIVDDGnLLIAEARKSDEGTYKCVAT 72
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
605-679 7.91e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 38.91  E-value: 7.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189690239 605 TTFLEC-APKSPQASIKWL-----LQKDkdrrkevklNERIIATSQGLLIRSVQGSDQGLYHCIATeNSFKQTIAKINFK 678
Cdd:cd20978    18 DVTLPCqVTGVPQPKITWLhngkpLQGP---------MERATVEDGTLTIINVQPEDTGYYGCVAT-NEIGDIYTETLLH 87

                  .
gi 1189690239 679 V 679
Cdd:cd20978    88 V 88
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
600-668 9.40e-04

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 38.98  E-value: 9.40e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189690239 600 GVKNNTTFLECAPK-SPQASIKWllqkdKDRRKEVKLNERIIATSQG-LLIRSVQGSDQGLYHCIAtENSF 668
Cdd:cd04969    14 AAKGGDVIIECKPKaSPKPTISW-----SKGTELLTNSSRICILPDGsLKIKNVTKSDEGKYTCFA-VNFF 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
601-664 1.35e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 433584 [Multi-domain]  Cd Length: 75  Bit Score: 37.95  E-value: 1.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189690239 601 VKNNTTFLEC-APKSPQASIKWLlqkdKDRRKEVKLNERIIATSQGLLIRSVQGSDQGLYHCIAT 664
Cdd:pfam13927  14 VEGETVTLTCeASGSPPPTITWY----KNGGKLSSGRTSLVGGNGTLTISNVTREDSGTYTCTAS 74
Ig_Sema4B_like cd05872
Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are ...
601-673 5.48e-03

Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are composed of the immunoglobulin (Ig)-like domain of Sema4B and similar proteins. Sema4B is a Class IV semaphorin. Semaphorins are classified based on structural features additional to the Sema domain. Sema4B has extracellular Sema and Ig domains, a transmembrane domain, and a short cytoplasmic domain. Sema4B has been shown to preferentially regulate the development of the postsynaptic specialization at the glutamatergic synapses. This cytoplasmic domain includes a PDZ-binding motif upon which the synaptic localization of Sem4B is dependent. Sema4B is a ligand of CLCP1. CLCP1 was identified in an expression profiling analysis, which compared a highly metastic lung cancer subline with its low metastic parental line. Sema4B was shown to promote CLCP1 endocytosis and their interaction is a potential target for therapeutic intervention of metastasis.


Pssm-ID: 409456  Cd Length: 86  Bit Score: 36.65  E-value: 5.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189690239 601 VKNNTTFLECAPKSPQASIKWLLqkdkDRRKEVKLNERIIATSQGLLIRSVQGSDQGLYHCIATENSFKQTIA 673
Cdd:cd05872     9 VAGADVVLPCQLRSNLASPVWLF----NGTPLNAQFSYLRLGTDGLLILVTSPEHSGTYRCYSEEEGFQQLVA 77
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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