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Conserved domains on  [gi|8894934|gb|AAF80660|]
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semaphorin M, partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Sema4F_C pfam19428
Semaphorin 4F C-terminal; Semaphorins are a large and diverse family of proteins, widely ...
230-424 1.32e-118

Semaphorin 4F C-terminal; Semaphorins are a large and diverse family of proteins, widely expressed across divergent animal phyla. They are secreted and membrane-associated proteins, conserved both structurally and functionally, and they are divided in eight classes (1-7 and V). They are involved in axon guidance and influence the migration of neurons and glial cells. This entry represents the C-terminal domain of Semaphorin 4F (also known as Semaphorin-W) which plays a role in visual system development and in oligodendrocyte precursor migration and differentiation. Like other Semaphorin 4 members, it includes a Ig-like domain, adjacent the PSI domain (plexin-semaphorin-integrin domain, conserved across all semaphorins), a transmembrane region and a short intracellular tail. The latter is rich in proline residues similar to other transmembrane semaphorins suggesting that it may interact with cytoskeletal or signalling proteins. It also contains a cyclic nucleotide-dependent protein kinase phosphorylation site, involved in signal transduction into the cell. Sema4F is found in glutamatergic synapses, preferentially in postsynaptic dendrites, attached to SAP90/PSD-95-scaffolding protein. Sema4F interacts with SAP90/PSD-95 PDZ domains through the critical last last three C-terminal amino acids.


:

Pssm-ID: 437260  Cd Length: 197  Bit Score: 343.83  E-value: 1.32e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    230 PVATAAHVVLPCSPSSAWASCVWHQPSGV-TALTPRRDGLEVVVTPGAMGAYACECQEGGAAHVVAAYSLVWGSQRDAPS 308
Cdd:pfam19428   1 PVSLAARVVLPCSPPSAWATCTWQRPSGDaTAYTPRRDGLEVTVTPGALGDYACECQEGGAGAVVASYSLVWGSAWQETR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    309 RAHTVGAGLAGFFLGILAASLTLILIGRRQQRRRQRELLARDKVGLDLGAPPSGTTSYSQDPPSP-SPEDERLPLALAKR 387
Cdd:pfam19428  81 RAYSVGAGLAGFFLGLVAGSLTLFLLGRRRQRRQQRELLAREKVGLDLGAPPSGTTSCSHDPPSPsSPEDERLPLALAKR 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 8894934    388 GSGFGGFSPPFLLDPCPSPAHIRLTGAPLATCDETSI 424
Cdd:pfam19428 161 GSNLNGFPPLFLLELDPDPAHIRLTGAPLATCDETSI 197
Sema super family cl15693
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
1-165 3.39e-116

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.


The actual alignment was detected with superfamily member cd11261:

Pssm-ID: 472829 [Multi-domain]  Cd Length: 460  Bit Score: 347.26  E-value: 3.39e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    1 PQDIRTVLNGPFRELKHDCNRGLPVVDNDVPQPRPGECITNNMKLRHFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPL 80
Cdd:cd11261 296 PQDIRRVMNGPFREFKHDCNRGLPVMDSDVPQPRPGECITNNMKLLGFGSSLSLPDRVLTFVRDHPLMDRPVFPADGHPL 375
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   81 LVTTDTAYLRVVAHRVTSLSGKEYDVLYLGTEDGHLHRAVRIGAQLSVLEDLALFPEPQPVENMKLYHSWLLVGSRTEVT 160
Cdd:cd11261 376 LVTTDTAYLRVAAHRVTSLSGKEYDVLYLGTEDGHLHRAVRIGAQLSVLEDLALFPEPQPVENLQLHHNWLLVGSDTEVT 455

                ....*
gi 8894934  161 QVNTT 165
Cdd:cd11261 456 QINTS 460
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
166-217 2.63e-07

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 some members show 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: 46.93  E-value: 2.63e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 8894934    166 NCGRLQSCSECILAQDPVCAWSFRLDECVAHA--GEHRGLVQDIESAdvSSLCP 217
Cdd:pfam01437   1 RCSQYTSCSSCLAARDPYCGWCSSEGRCVRRSacGAPEGNCEEWEQA--SSKCP 52
 
Name Accession Description Interval E-value
Sema4F_C pfam19428
Semaphorin 4F C-terminal; Semaphorins are a large and diverse family of proteins, widely ...
230-424 1.32e-118

Semaphorin 4F C-terminal; Semaphorins are a large and diverse family of proteins, widely expressed across divergent animal phyla. They are secreted and membrane-associated proteins, conserved both structurally and functionally, and they are divided in eight classes (1-7 and V). They are involved in axon guidance and influence the migration of neurons and glial cells. This entry represents the C-terminal domain of Semaphorin 4F (also known as Semaphorin-W) which plays a role in visual system development and in oligodendrocyte precursor migration and differentiation. Like other Semaphorin 4 members, it includes a Ig-like domain, adjacent the PSI domain (plexin-semaphorin-integrin domain, conserved across all semaphorins), a transmembrane region and a short intracellular tail. The latter is rich in proline residues similar to other transmembrane semaphorins suggesting that it may interact with cytoskeletal or signalling proteins. It also contains a cyclic nucleotide-dependent protein kinase phosphorylation site, involved in signal transduction into the cell. Sema4F is found in glutamatergic synapses, preferentially in postsynaptic dendrites, attached to SAP90/PSD-95-scaffolding protein. Sema4F interacts with SAP90/PSD-95 PDZ domains through the critical last last three C-terminal amino acids.


Pssm-ID: 437260  Cd Length: 197  Bit Score: 343.83  E-value: 1.32e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    230 PVATAAHVVLPCSPSSAWASCVWHQPSGV-TALTPRRDGLEVVVTPGAMGAYACECQEGGAAHVVAAYSLVWGSQRDAPS 308
Cdd:pfam19428   1 PVSLAARVVLPCSPPSAWATCTWQRPSGDaTAYTPRRDGLEVTVTPGALGDYACECQEGGAGAVVASYSLVWGSAWQETR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    309 RAHTVGAGLAGFFLGILAASLTLILIGRRQQRRRQRELLARDKVGLDLGAPPSGTTSYSQDPPSP-SPEDERLPLALAKR 387
Cdd:pfam19428  81 RAYSVGAGLAGFFLGLVAGSLTLFLLGRRRQRRQQRELLAREKVGLDLGAPPSGTTSCSHDPPSPsSPEDERLPLALAKR 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 8894934    388 GSGFGGFSPPFLLDPCPSPAHIRLTGAPLATCDETSI 424
Cdd:pfam19428 161 GSNLNGFPPLFLLELDPDPAHIRLTGAPLATCDETSI 197
Sema_4F cd11261
The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in ...
1-165 3.39e-116

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: 347.26  E-value: 3.39e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    1 PQDIRTVLNGPFRELKHDCNRGLPVVDNDVPQPRPGECITNNMKLRHFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPL 80
Cdd:cd11261 296 PQDIRRVMNGPFREFKHDCNRGLPVMDSDVPQPRPGECITNNMKLLGFGSSLSLPDRVLTFVRDHPLMDRPVFPADGHPL 375
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   81 LVTTDTAYLRVVAHRVTSLSGKEYDVLYLGTEDGHLHRAVRIGAQLSVLEDLALFPEPQPVENMKLYHSWLLVGSRTEVT 160
Cdd:cd11261 376 LVTTDTAYLRVAAHRVTSLSGKEYDVLYLGTEDGHLHRAVRIGAQLSVLEDLALFPEPQPVENLQLHHNWLLVGSDTEVT 455

                ....*
gi 8894934  161 QVNTT 165
Cdd:cd11261 456 QINTS 460
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
2-148 5.90e-49

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 Swiss:P51805


Pssm-ID: 460197 [Multi-domain]  Cd Length: 180  Bit Score: 164.37  E-value: 5.90e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934      2 QDIRTVLNGPFRELKHDCNRGLPVvDNDVPQPRPGECITNNMKLrhfgsslSLPDRVLTFIRDHPLMDRPVFPADGHPLL 81
Cdd:pfam01403  42 SDINAVFEGPFKEQEKSDSKWLPY-TGKVPYPRPGTCINDPLRL-------DLPDSVLNFVKDHPLMDEAVQPVGGRPLL 113
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8894934     82 VTTDTAYLRVVAHRVTSLSGkEYDVLYLGTEDGHLHRAVRIGAQLSV-LEDLALFPEPQPVENMKLYH 148
Cdd:pfam01403 114 VRTGVRLTSIAVDRVQALDG-NYTVLFLGTDDGRLHKVVLVGSEESHiIEEIQVFPEPQPVLNLLLSS 180
Sema smart00630
semaphorin domain;
2-141 3.29e-34

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 131.34  E-value: 3.29e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934       2 QDIRTVLNGPFRELKHDCNRGLPVVDNDVPQPRPGECITNNMklrhfgSSLSLPDRVLTFIRDHPLMDRPVFPADGHPLL 81
Cdd:smart00630 252 SDINAVFNGPFKECETSTSQWLPYSRGKVPYPRPGTCPNKPP------SSKDLPDETLNFIKSHPLMDEVVQPLTGRPLF 325
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8894934      82 VTTDTAYL--RVVAHRVTslSGKEYDVLYLGTEDGHLHRAVRIGAQLS----VLEDLALFPEPQPV 141
Cdd:smart00630 326 VKTDSNYLltSIAVDRVA--TDGNYTVLFLGTSDGRILKVVLSESSSSsesvVLEEISVFPDGSPI 389
Ig_Sema4B_like cd05872
Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are ...
223-303 1.41e-26

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: 102.13  E-value: 1.41e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934  223 RPVVFEVPVAtAAHVVLPCSPSSAWASCVWHQPSGVT-----ALTPRRDGLEVVVT-PGAMGAYACECQEGGAAHVVAAY 296
Cdd:cd05872   1 LPVKFRTVVA-GADVVLPCQLRSNLASPVWLFNGTPLnaqfsYLRLGTDGLLILVTsPEHSGTYRCYSEEEGFQQLVASY 79

                ....*..
gi 8894934  297 SLVWGSQ 303
Cdd:cd05872  80 SLNVVEQ 86
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
166-217 2.63e-07

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 some members show 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: 46.93  E-value: 2.63e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 8894934    166 NCGRLQSCSECILAQDPVCAWSFRLDECVAHA--GEHRGLVQDIESAdvSSLCP 217
Cdd:pfam01437   1 RCSQYTSCSSCLAARDPYCGWCSSEGRCVRRSacGAPEGNCEEWEQA--SSKCP 52
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
166-195 1.92e-06

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 44.46  E-value: 1.92e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 8894934     166 NCGRLQSCSECILAQDPVCAWSFRLDECVA 195
Cdd:smart00423   1 RCSKYTSCSECLLARDPYCAWCSSQGRCTS 30
 
Name Accession Description Interval E-value
Sema4F_C pfam19428
Semaphorin 4F C-terminal; Semaphorins are a large and diverse family of proteins, widely ...
230-424 1.32e-118

Semaphorin 4F C-terminal; Semaphorins are a large and diverse family of proteins, widely expressed across divergent animal phyla. They are secreted and membrane-associated proteins, conserved both structurally and functionally, and they are divided in eight classes (1-7 and V). They are involved in axon guidance and influence the migration of neurons and glial cells. This entry represents the C-terminal domain of Semaphorin 4F (also known as Semaphorin-W) which plays a role in visual system development and in oligodendrocyte precursor migration and differentiation. Like other Semaphorin 4 members, it includes a Ig-like domain, adjacent the PSI domain (plexin-semaphorin-integrin domain, conserved across all semaphorins), a transmembrane region and a short intracellular tail. The latter is rich in proline residues similar to other transmembrane semaphorins suggesting that it may interact with cytoskeletal or signalling proteins. It also contains a cyclic nucleotide-dependent protein kinase phosphorylation site, involved in signal transduction into the cell. Sema4F is found in glutamatergic synapses, preferentially in postsynaptic dendrites, attached to SAP90/PSD-95-scaffolding protein. Sema4F interacts with SAP90/PSD-95 PDZ domains through the critical last last three C-terminal amino acids.


Pssm-ID: 437260  Cd Length: 197  Bit Score: 343.83  E-value: 1.32e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    230 PVATAAHVVLPCSPSSAWASCVWHQPSGV-TALTPRRDGLEVVVTPGAMGAYACECQEGGAAHVVAAYSLVWGSQRDAPS 308
Cdd:pfam19428   1 PVSLAARVVLPCSPPSAWATCTWQRPSGDaTAYTPRRDGLEVTVTPGALGDYACECQEGGAGAVVASYSLVWGSAWQETR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    309 RAHTVGAGLAGFFLGILAASLTLILIGRRQQRRRQRELLARDKVGLDLGAPPSGTTSYSQDPPSP-SPEDERLPLALAKR 387
Cdd:pfam19428  81 RAYSVGAGLAGFFLGLVAGSLTLFLLGRRRQRRQQRELLAREKVGLDLGAPPSGTTSCSHDPPSPsSPEDERLPLALAKR 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 8894934    388 GSGFGGFSPPFLLDPCPSPAHIRLTGAPLATCDETSI 424
Cdd:pfam19428 161 GSNLNGFPPLFLLELDPDPAHIRLTGAPLATCDETSI 197
Sema_4F cd11261
The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in ...
1-165 3.39e-116

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: 347.26  E-value: 3.39e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    1 PQDIRTVLNGPFRELKHDCNRGLPVVDNDVPQPRPGECITNNMKLRHFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPL 80
Cdd:cd11261 296 PQDIRRVMNGPFREFKHDCNRGLPVMDSDVPQPRPGECITNNMKLLGFGSSLSLPDRVLTFVRDHPLMDRPVFPADGHPL 375
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   81 LVTTDTAYLRVVAHRVTSLSGKEYDVLYLGTEDGHLHRAVRIGAQLSVLEDLALFPEPQPVENMKLYHSWLLVGSRTEVT 160
Cdd:cd11261 376 LVTTDTAYLRVAAHRVTSLSGKEYDVLYLGTEDGHLHRAVRIGAQLSVLEDLALFPEPQPVENLQLHHNWLLVGSDTEVT 455

                ....*
gi 8894934  161 QVNTT 165
Cdd:cd11261 456 QINTS 460
Sema_4 cd11240
The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 ...
3-162 3.65e-58

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: 197.25  E-value: 3.65e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    3 DIRTVLNGPFRELKHDCNRGLPVVdNDVPQPRPGECITNNMKLRHFGSSLSLPDRVLTFIRDHPLMDRPVFPADgHPLLV 82
Cdd:cd11240 294 DIKKVFSGKYKEFNRETSKWSRYT-GPVPDPRPGACITNSARSQGITSSLNLPDNVLTFVKDHPLMDEQVHPIN-RPLLV 371
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   83 TTDTAYLRVVAHRVTSLSGKEYDVLYLGTEDGHLHRAVRIGAQLSVLEDLALFPEPQPVENMKLYHS--WLLVGSRTEVT 160
Cdd:cd11240 372 KSGVNYTRIAVHRVQALDGQTYTVLFLGTEDGFLHKAVSLDGGMHIIEEIQLFDQPQPVKNLLLSSSkgVLYVGSSSGVV 451

                ..
gi 8894934  161 QV 162
Cdd:cd11240 452 QV 453
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
2-148 5.90e-49

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 Swiss:P51805


Pssm-ID: 460197 [Multi-domain]  Cd Length: 180  Bit Score: 164.37  E-value: 5.90e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934      2 QDIRTVLNGPFRELKHDCNRGLPVvDNDVPQPRPGECITNNMKLrhfgsslSLPDRVLTFIRDHPLMDRPVFPADGHPLL 81
Cdd:pfam01403  42 SDINAVFEGPFKEQEKSDSKWLPY-TGKVPYPRPGTCINDPLRL-------DLPDSVLNFVKDHPLMDEAVQPVGGRPLL 113
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8894934     82 VTTDTAYLRVVAHRVTSLSGkEYDVLYLGTEDGHLHRAVRIGAQLSV-LEDLALFPEPQPVENMKLYH 148
Cdd:pfam01403 114 VRTGVRLTSIAVDRVQALDG-NYTVLFLGTDDGRLHKVVLVGSEESHiIEEIQVFPEPQPVLNLLLSS 180
Sema_4G cd11262
The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and ...
3-162 4.15e-48

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: 170.33  E-value: 4.15e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    3 DIRTVLNGPFRELKhDCNRGLPVVDNDVPQPRPGECITNNMKLRHFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPLLV 82
Cdd:cd11262 294 DIQTAFEGPYMEYQ-DSSSKWSRYTGKVPEPRPGSCITDEHRSQGINSSQDLPDNVLDFVRRHPLMAEQVLPVEGRPLLF 372
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   83 TTDTAYLRVVAHRVTSLSGKEYDVLYLGTEDGHLHRAVRIGAQLSVLEDLALFPEPQPVENM---KLYHSwLLVGSRTEV 159
Cdd:cd11262 373 KRNVIYTKIAVQTVRGLDGRVYDVLFLGTDEGWLHKAVVIGSAVHIIEELQVFREPQPVENLvisKKQNS-LYVGARSGV 451

                ...
gi 8894934  160 TQV 162
Cdd:cd11262 452 VQV 454
Sema_4B cd11257
The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in ...
3-162 4.06e-38

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: 143.46  E-value: 4.06e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    3 DIRTVLNGPFRELKHDCNRGLpVVDNDVPQPRPGECITNNMKLRHFGSSLSLPDRVLTFIRDHPLMDRPVfpaDGHPLLV 82
Cdd:cd11257 305 QVQRAFNGLYKEVNRETQQWY-TYTHPVPEPRPGACITNSARERKINSSLHMPDRVLNFVKDHFLMDGQV---RSQPLLL 380
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   83 TTDTAYLRVVAHRVTSLSgKEYDVLYLGTEDGHLHRAVRIGAQLSVLEDLALFPEPQPVENMKL--YHSWLLVGSRTEVT 160
Cdd:cd11257 381 QPQVRYTQIAVHRVKGLH-KTYDVLFLGTDDGRLHKAVSVGPMVHIIEELQIFSEGQPVQNLLLdtHKGLLYASSHSGVV 459

                ..
gi 8894934  161 QV 162
Cdd:cd11257 460 QV 461
Sema smart00630
semaphorin domain;
2-141 3.29e-34

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 131.34  E-value: 3.29e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934       2 QDIRTVLNGPFRELKHDCNRGLPVVDNDVPQPRPGECITNNMklrhfgSSLSLPDRVLTFIRDHPLMDRPVFPADGHPLL 81
Cdd:smart00630 252 SDINAVFNGPFKECETSTSQWLPYSRGKVPYPRPGTCPNKPP------SSKDLPDETLNFIKSHPLMDEVVQPLTGRPLF 325
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8894934      82 VTTDTAYL--RVVAHRVTslSGKEYDVLYLGTEDGHLHRAVRIGAQLS----VLEDLALFPEPQPV 141
Cdd:smart00630 326 VKTDSNYLltSIAVDRVA--TDGNYTVLFLGTSDGRILKVVLSESSSSsesvVLEEISVFPDGSPI 389
Sema_4D cd11259
The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); ...
29-161 3.80e-32

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: 126.90  E-value: 3.80e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   29 DVPQPRPGECITNNMKLRHFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPLLVTTDTAYLRVVAHRVTSLSGKEYDVLY 108
Cdd:cd11259 331 EVPKPRPGACINNEARAANYTSSLNLPDKTLQFVKDHPLMDDSVTPIGNRPRLIKKDVNYTQIVVDRVQALDGTIYDVMF 410
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 8894934  109 LGTEDGHLHRAVRIGAQLSVLEDLALFPEPQPVENMKLYHS----WLLVGSRTEVTQ 161
Cdd:cd11259 411 ISTDRGALHKAISLENEVHIIEETQLFPDFEPVQTLLLSSKkgrrFLYAGSNSGVVQ 467
Sema_semaphorin cd11235
The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator ...
3-162 9.74e-32

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: 125.21  E-value: 9.74e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    3 DIRTVLNGPFRElKHDCNRG-LPVVDNDVPQPRPGECitnnmklrhFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPLL 81
Cdd:cd11235 276 DIEAVFNGPFKE-QHSSNSAwLPVPDERVPEPRPGTC---------VDDSSPLPDDTLNFIKSHPLMDEAVTPILNRPLF 345
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   82 VTTDTAY--LRVVAHRVTSLSGKEYDVLYLGTEDGHLHRAV---RIGAQLS-VLEDLALFPEPQPVENMKL--YHSWLLV 153
Cdd:cd11235 346 IKTDVNYrfTKIAVDRVQAKLGQTYDVLFVGTDRGIILKVVslpEQGLQASnILEEMPVGPPPEPIQTMQLsrKRRSLYV 425

                ....*....
gi 8894934  154 GSRTEVTQV 162
Cdd:cd11235 426 GSETGVLQV 434
Sema_4E cd11260
The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed ...
29-162 1.60e-30

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: 122.32  E-value: 1.60e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   29 DVPQPRPGECITNNMKLRHFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPLLVTTDTAYLRVVAHRVTSLSGKEYDVLY 108
Cdd:cd11260 320 ELPVPRPGACINNAARTSGIKKSLNLPDKTLQFVKDKPLMDQAVHPITGKPLLVKRGALFTRIVVDMVTAADGQSYPVMF 399
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 8894934  109 LGTEDGHLHRAVRIGAQLSVLEDLALFPEPQPVENMKLYHSWLLVGSRTEVTQV 162
Cdd:cd11260 400 IGTANGYVLKAVNYDGEMHIIEEVQLFEPEEPIDILRLSQNQLYAGSASGVVQM 453
Sema_3 cd11239
The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins ...
2-167 1.32e-29

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: 119.77  E-value: 1.32e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    2 QDIRTVLNGPFRElKHDCNRGLPVVDNDVPQPRPGECITNNMKLRhFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPLL 81
Cdd:cd11239 300 ADIRAAFNGPFAH-KEGPNYQWVEYQGKVPYPRPGTCPSKTYGPL-YKSTKDFPDDVISFARSHPLMYNPVYPLHGRPLL 377
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   82 VTTDTAY--LRVVAHRVTSLSGkEYDVLYLGTEDGHLHRAVRI-----GAQLSVLEDLALFPEPQPVENMKLY--HSWLL 152
Cdd:cd11239 378 IRTNVPYrlTQIAVDRVEAEDG-QYDVLFIGTDSGTVLKVVSLpkenwEMEEVILEELQVFKHPSPITSMEISskRQQLY 456
                       170
                ....*....|....*
gi 8894934  153 VGSRTEVTQVNTTNC 167
Cdd:cd11239 457 VGSAEGVVQLPLHRC 471
Sema_1A cd11237
The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a ...
2-167 7.42e-28

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 [Multi-domain]  Cd Length: 446  Bit Score: 114.35  E-value: 7.42e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    2 QDIRTVLNGPFRELKHDCNRGLPVVDNDVPQPRPGECITNnmklrhfgsSLSLPDRVLTFIRDHPLMDRPVFPADGHPLL 81
Cdd:cd11237 276 QDILEVFDGSFKEQQDINSNWLPVPSNKVPEPRPGQCVND---------SRTLPDVTVNFIKSHPLMDEAVPSFFGRPIL 346
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   82 VTTDTAYlR----VVAHRVTSLSGKEYDVLYLGTEDGHLHRAVRIGAQLS-------VLEDLALFPEPQPVENMKLYHSW 150
Cdd:cd11237 347 VRTSLQY-RftqiAVDPQVKALDGKYYDVLFIGTDDGKVLKAVNIASADTvdkvspvVIEETQVFPRGVPIRNLLIVRGK 425
                       170       180
                ....*....|....*....|.
gi 8894934  151 ----LLVGSRTEVTQVNTTNC 167
Cdd:cd11237 426 ddgrLVVVSDDEIVSIPLHRC 446
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
2-162 3.39e-27

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: 112.97  E-value: 3.39e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    2 QDIRTVLNGPFRElkHDCNRGLPVVDND-VPQPRPGECITNNMKLRHFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPL 80
Cdd:cd11258 294 GEIQQVFEGPYKE--YSEQAQKWGRYTDpVPSPRPGSCINNWHRDHGYTSSLELPDNTLNFVKKHPLMEDRVKPRLGRPL 371
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   81 LVTTDTAYLRVVAHRVTSLSGKEYDVLYLGTEDGHLHRAVRIGAQLSVLEDLALFPEPQPVENMKLYHS--WLLVGSRTE 158
Cdd:cd11258 372 LVPCNSNFTHVVWTRVLGLDGETYSVLFIGTLDGWLIKAVSLGSWVHMIEELQVFDQEPPESLVVSQSSkkLLFAGSRSE 451

                ....
gi 8894934  159 VTQV 162
Cdd:cd11258 452 LLQL 455
Ig_Sema4B_like cd05872
Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are ...
223-303 1.41e-26

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: 102.13  E-value: 1.41e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934  223 RPVVFEVPVAtAAHVVLPCSPSSAWASCVWHQPSGVT-----ALTPRRDGLEVVVT-PGAMGAYACECQEGGAAHVVAAY 296
Cdd:cd05872   1 LPVKFRTVVA-GADVVLPCQLRSNLASPVWLFNGTPLnaqfsYLRLGTDGLLILVTsPEHSGTYRCYSEEEGFQQLVASY 79

                ....*..
gi 8894934  297 SLVWGSQ 303
Cdd:cd05872  80 SLNVVEQ 86
Sema_3G cd11255
The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is ...
3-167 1.71e-26

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: 111.16  E-value: 1.71e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    3 DIRTVLNGPFRElKHDCNRGLPVVDNDVPQPRPGEC--ITNNMKLRHFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPL 80
Cdd:cd11255 300 DIWEVFNGPFAH-KDGPDHQWGPYEGKVPYPRPGVCpsKITAQPGRAFRSTKDYPDEVLQFARAHPLMWRPVYPSHRRPV 378
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   81 LVTTDTAY--LRVVAHRVTSLSGkEYDVLYLGTEDGHLHRAVRIGAQLS------VLEDLALFPEPQPVENMKLY--HSW 150
Cdd:cd11255 379 LVKTGLPYrlTQIVVDRVEAEDG-YYDVMFIGTDSGSVLKVIVLQKGNSaageevTLEELQVFKVPTPITEMEISvkRQM 457
                       170
                ....*....|....*..
gi 8894934  151 LLVGSRTEVTQVNTTNC 167
Cdd:cd11255 458 LYVGSRTGVAQVPLHRC 474
Sema_3F cd11254
The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is ...
3-167 3.46e-24

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: 104.13  E-value: 3.46e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    3 DIRTVLNGPFRElKHDCNRGLPVVDNDVPQPRPGEC----ITNNMKlrhfgSSLSLPDRVLTFIRDHPLMDRPVFPADGH 78
Cdd:cd11254 300 DIRMVFNGPFAH-KEGPNYQWMPYTGKIPYPRPGTCpggtFTPSMK-----STKDYPDEVINFMRTHPLMYNAVYPVHRR 373
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   79 PLLVTTDTAY--LRVVAHRVTSLSGkEYDVLYLGTEDGHLHRAVRIGAQLSVLEDLAL-----FPEPQPVENMKLY--HS 149
Cdd:cd11254 374 PLVVRTNVNYrfTTIAVDQVDAADG-RYEVLFLGTDRGTVQKVIVLPKDDLETEELTLeevevFKVPAPIKTMKISskRQ 452
                       170
                ....*....|....*...
gi 8894934  150 WLLVGSRTEVTQVNTTNC 167
Cdd:cd11254 453 QLYVSSAVGVTHLSLHRC 470
Sema_3C cd11251
The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted ...
3-167 3.64e-24

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: 104.20  E-value: 3.64e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    3 DIRTVLNGPFRElKHDCNRGLPVVDNDVPQPRPGEC----ITNNMKlrhfgSSLSLPDRVLTFIRDHPLMDRPVFPADGH 78
Cdd:cd11251 300 DIQTVFNGPFAH-KEGPNHQLIAYQGRIPYPRPGTCpggaFTPNMQ-----STKEFPDDVVTFIRNHPLMFNPIYPIGRR 373
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   79 PLLVT--TDTAYLRVVAHRVTSLSGKeYDVLYLGTEDGHLHRAVRIGAQLS-----VLEDLALFPEPQPVENMKLY--HS 149
Cdd:cd11251 374 PLLVRtgTDYKYTKIAVDRVNAADGR-YHVLFLGTDKGTVQKVVVLPTNGSlsgelILEELEVFKNHAPITNMKISskKQ 452
                       170
                ....*....|....*...
gi 8894934  150 WLLVGSRTEVTQVNTTNC 167
Cdd:cd11251 453 QLYVSSEEGISQVSLHRC 470
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
3-167 1.99e-23

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: 102.00  E-value: 1.99e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    3 DIRTVLNGPFRELKHDCNRGLPVvDNDVPQPRPGECITNNMKlrHFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPLLV 82
Cdd:cd11249 322 DIRRVFLGPYAHRDGPNYQWVPF-QGRVPYPRPGTCPSKTFG--GFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIII 398
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   83 TTDTAY--LRVVAHRVTSLSGkEYDVLYLGTEDGHLHRAVRIGAQL------SVLEDLALFPEPQPVENMKLY--HSWLL 152
Cdd:cd11249 399 KTDVDYqfTQIVVDRVEAEDG-QYDVMFIGTDMGTVLKVVSIPKETwhdleeVLLEEMTVFREPTAISAMELStkQQQLY 477
                       170
                ....*....|....*
gi 8894934  153 VGSRTEVTQVNTTNC 167
Cdd:cd11249 478 IGSAIGVSQLPLHRC 492
Sema_4A cd11256
The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed ...
3-186 5.20e-23

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: 100.37  E-value: 5.20e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    3 DIRTVLNGPFRELKHDCNRgLPVVDNDVPQPRPGECitnnmklrhfgSSLSLPDRVLTFIRDHPLMDRPVFPADGHPLLV 82
Cdd:cd11256 294 DIEKVFNGKYKELNKESSR-WTRYMGPVSDPRPGSC-----------SGGKSSDKALNFMKDHFLMDEVVLPGAGRPLLV 361
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   83 TTDTAYLRVVAHRVTSLSGKEYDVLYLGTEDGHLHRAVRIG-AQLSVLEDLALFPEPQPVENMKLyhswllvgsrtevtq 161
Cdd:cd11256 362 KSNVQYTRIAVDSVQGVSGHNYTVMFLGTDKGFLHKAVLMGgSESHIIEEIELLTPPEPVENLLL--------------- 426
                       170       180
                ....*....|....*....|....*.
gi 8894934  162 vnttncgrlqSCSE-CILAQDPVCAW 186
Cdd:cd11256 427 ----------AANEgVVYIGYSAGVW 442
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
3-167 5.98e-22

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: 97.67  E-value: 5.98e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    3 DIRTVLNGPFRELKHDCNRGLPVvDNDVPQPRPGECITNNMKlRHFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPLLV 82
Cdd:cd11252 304 DIRAVFNGPYAHKESPDHRWVQY-EGRIPYPRPGTCPSKTYD-PLIKSTKDFPDEVISFIKRHPLMYKSVYPLTGGPVFT 381
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   83 TTDTAY--LRVVAHRVTSLSGkEYDVLYLGTEDGHLHRAVRIGAQL-----SVLEDLALFPEPQPVENMKLY--HSWLLV 153
Cdd:cd11252 382 RINVDYrlTQIVVDHVAAEDG-QYDVMFLGTDIGTVLKVVSITKEKwtmeeVVLEELQIFKHPSPILNMELSlkQQQLYI 460
                       170
                ....*....|....
gi 8894934  154 GSRTEVTQVNTTNC 167
Cdd:cd11252 461 GSRDGLVQLSLHRC 474
Sema_3B cd11250
The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is ...
3-167 2.60e-21

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: 95.75  E-value: 2.60e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    3 DIRTVLNGPFRElKHDCNRGLPVVDNDVPQPRPGECITNNMKlrHFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPLLV 82
Cdd:cd11250 301 DVRRAFLGPFAH-KEGPNYQWVSYQGKVPYPRPGMCPSKTFG--SFESTKDFPDDVIQFARNHPLMFNPVLPLGGRPLFL 377
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   83 TT--DTAYLRVVAHRVTSLSGkEYDVLYLGTEDGHLHRAVRI------GAQLSVLEDLALFPEPQPVENMKLY--HSWLL 152
Cdd:cd11250 378 RTgiPYTFTQIAVDRVAAADG-HYDVMFIGTDVGSVLKVISVpkgswpSNEELLLEELHVFKDSSPITSMQISskRQQLY 456
                       170
                ....*....|....*
gi 8894934  153 VGSRTEVTQVNTTNC 167
Cdd:cd11250 457 VGSRSGVSQLPLHRC 471
Sema_6 cd11242
The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 ...
3-147 1.58e-18

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: 87.19  E-value: 1.58e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    3 DIRTVLNGPFRELKHDCNRGLPVVDNDVPQPRPGECITNNMkLRHFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPLLV 82
Cdd:cd11242 287 DIEKVFEGRFKEQKSPDSAWTPVPEDRVPKPRPGCCAGSGS-AEKYKTSNDFPDDTLNFIKTHPLMDEAVPSIINRPWFT 365
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8894934   83 TTDTAYlRVVAHRVTSLSG--KEYDVLYLGTEDGH-LHRAVRIGAqlsvledlALFPEPQPVENMKLY 147
Cdd:cd11242 366 RTMVRY-RLTQIAVDNAAGpyQNYTVVFLGSEAGTvLKFLARIGP--------SGSNGSVFLEEIDVY 424
Sema_2A cd11238
The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted ...
3-163 5.52e-17

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: 82.47  E-value: 5.52e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    3 DIRTVLN-GPFRELKHDCNRGLPVVDNDVPQPRPGECITNnmklrhfgsSLSLPDRVLTFIRDHPLMDRPVfpADGHPLL 81
Cdd:cd11238 297 DINAAFDtGKFKEQASSSSAWLPVLSSEVPEPRPGTCVND---------SATLSDTVLHFARTHPLMDDAV--SHGPPLL 365
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   82 VTTDTAYLRVVAHRVTSlSGKEYDVLYLGTEDGHLHRAV----RIGAQLSVLEDLALFPePQPVENMKLY-HSWLLVGSR 156
Cdd:cd11238 366 YLRDVVFTHLVVDKLRI-DDQEYVVFYAGSNDGKVYKIVhwkdAGESKSNLLDVFELTP-GEPIRAMELLpGEFLYVASD 443

                ....*..
gi 8894934  157 TEVTQVN 163
Cdd:cd11238 444 HRVSQID 450
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
31-162 7.68e-17

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: 81.82  E-value: 7.68e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   31 PQPRPGECITnnmklrhfgSSLSLPDRVLTFIRDHPLMDRPVFPADGHPL-LVTTDTAYLRVVAHRVTSLSGKEYDVLYL 109
Cdd:cd11243 286 PNPRPGTCVP---------PEQTHPSETFSFADEHPELDDRIEPDEPRKLpVFQNKDHYQKVVVDEVRASDGVSYDVLYL 356
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 8894934  110 GTEDGHLHRAVRIGAQLSVLEDLALFPEPQPVENMKLYHSW--LLVGSRTEVTQV 162
Cdd:cd11243 357 ATDKGKIHKVVESKGQTHNIMEIQPFKEQEPIQSMILDAERshLYVGTKAEVTRL 411
Sema_6B cd11267
The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as ...
2-114 2.57e-15

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: 77.57  E-value: 2.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    2 QDIRTVLNGPFRELKHDCNRGLPVVDNDVPQPRPGECITNNMKlrhFGSSLSLPDRVLTFIRDHPLMDRPVfPADGH-PL 80
Cdd:cd11267 286 TQVAAVFEGRFREQKSPESIWTPVPEELVPRPRPGCCAAPGMR---YNSSSTLPDEVLNFVKTHPLMDEAV-PSLGHaPW 361
                        90       100       110
                ....*....|....*....|....*....|....*
gi 8894934   81 LVTTDTAY-LRVVAHRVTSLSGKEYDVLYLGTEDG 114
Cdd:cd11267 362 IVRTMTRYqLTHMVVDTEAGPHGNHTVVFLGSTRG 396
Sema_6A cd11266
The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, ...
3-149 7.18e-15

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: 76.22  E-value: 7.18e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    3 DIRTVLNGPFRELKHDCNRGLPVVDNDVPQPRPGeCITNNMKLRHFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPLLV 82
Cdd:cd11266 287 DIASVFTGRFKEQKSPDSTWTPVPDERVPKPRPG-CCAGSSSLEKYATSNEFPDDTLNFIKTHPLMDEAVPSIINRPWFL 365
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   83 TTDTAYlRVVAHRVTSLSG--KEYDVLYLGTEDG-HLHRAVRIGAQlSVLEDlALFpepqpVENMKLYHS 149
Cdd:cd11266 366 RTMVRY-RLTKIAVDNAAGpyQNHTVVFLGSEKGiILKFLARTGNS-GFLND-SLF-----LEEMNVYNS 427
Sema_6E cd11270
The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed ...
3-134 1.03e-13

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: 72.45  E-value: 1.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    3 DIRTVLNGPFRELKHDCNRGLPVVDNDVPQPRPGeCITNNMKLRHFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPLLV 82
Cdd:cd11270 285 DIEKVFNGKFKEQRNSESAWTPVPDEAVPKPRPG-SCAGDGPAAGYKSSTNFPDETLTFIKSYPLMDEAVPSVNNRPCFT 363
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 8894934   83 TTDTAY-LRVVAHRVTSLSGKEYDVLYLGTEDGHLHRAVRIGAQLSVLEDLAL 134
Cdd:cd11270 364 RTTSRFkLTQIAVDTAAGPYKNYTVVFLGSENGHVLKVLASMHPNSSYSTQVL 416
Sema_6C cd11268
The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called ...
3-160 1.19e-13

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: 72.43  E-value: 1.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    3 DIRTVLNGPFRELKHDCNRGLPVVDNDVPQPRPGECI-TNNMKLrhFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPLL 81
Cdd:cd11268 286 EIERGFEGKFKEQRSLDGAWTPVSEDRVPSPRPGSCAgVGGAAL--FSSSRDLPDDVLTFIKAHPLLDPAVPPVTHQPLL 363
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   82 VTTDTAYLRVVAhrVTSLSGKEYD--VLYLGTEDGHLHRAVRIGAQlsvledlALFPEPQPVENMKLYHSWLLVGSRTEV 159
Cdd:cd11268 364 TLTSRALLTQVA--VDGMAGPHSNitVMFLGSNDGTVLKVLPPGGR-------SGGPEPILLEEIDAYSPARCSGKRTAQ 434

                .
gi 8894934  160 T 160
Cdd:cd11268 435 T 435
Sema_6D cd11269
The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed ...
3-114 4.86e-13

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: 70.44  E-value: 4.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    3 DIRTVLNGPFRELKHDCNRGLPVVDNDVPQPRPGECITNNMKlRHFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPLLV 82
Cdd:cd11269 287 DIEKVFKGRFKEQKTPDSVWTAVPEDKVPKPRPGCCAKHGLA-EAYKTSIDFPDETLSFIKSHPLMDSAVPSIIEEPWFT 365
                        90       100       110
                ....*....|....*....|....*....|....
gi 8894934   83 TTDTAYlRVVAHRVTSLSG--KEYDVLYLGTEDG 114
Cdd:cd11269 366 KTRVRY-RLTAIAVDHAAGphQNYTVIFVGSEAG 398
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
26-225 3.28e-08

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: 55.29  E-value: 3.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   26 VDNDVPQPRPGECITNnmklrhFGSSLSL-PDRVLTFIRDHPLMD--RPVFpadghpLLVTTDTAYLRVVAHRVTSLSGK 102
Cdd:cd09295 103 GKVRWPSGRPRCPIDN------KHSNMGVnVDSKLYSATDHDFKDgdRPAL------SRRSSNVHYLRIVVDSSTGLDEI 170
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934  103 EYDVLYLGTEDghlhravrigaqlsvLEDLALFPEPQPVENMKLYHswLLVGSRTEVTQVNTTNCGRLQSCSECILAQDP 182
Cdd:cd09295 171 TFVYAFVSGDD---------------DDEVYFFFRQEPVEYLKKGM--VYVPRIARVCKLDVGGCHRLKKKLTSFLKADL 233
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 8894934  183 VCAWSFRLDECV---AHAGEHRGLVQDIESADVSSlCPKEPGERPV 225
Cdd:cd09295 234 NCSRPQSGFAFNllqDATGDTKNLIQDVKFAIFSS-CLNKSVESAV 278
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
166-217 2.63e-07

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 some members show 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: 46.93  E-value: 2.63e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 8894934    166 NCGRLQSCSECILAQDPVCAWSFRLDECVAHA--GEHRGLVQDIESAdvSSLCP 217
Cdd:pfam01437   1 RCSQYTSCSSCLAARDPYCGWCSSEGRCVRRSacGAPEGNCEEWEQA--SSKCP 52
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
166-195 1.92e-06

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 44.46  E-value: 1.92e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 8894934     166 NCGRLQSCSECILAQDPVCAWSFRLDECVA 195
Cdd:smart00423   1 RCSKYTSCSECLLARDPYCAWCSSQGRCTS 30
Sema_5B cd11264
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed ...
4-162 2.06e-06

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: 49.60  E-value: 2.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    4 IRTVLNGPFRELKHDCNRGLPVvdndvPQPRPG-ECITnnmkLRHFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPLLV 82
Cdd:cd11264 278 ITQAFNGPFRYQENPRSAWLPT-----ANPIPNfQCGT----LSDDSPNENLTERSLQDAQRLFLMNDVVQPVTVDPLVT 348
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   83 TTDTAYLRVVahrVTSLSGKE--YDVLYLGTEDGHLHRAVRIGA---QLSVLEDLALFP--EPQPVENMKLYHS--WLLV 153
Cdd:cd11264 349 QDSVRFSKLV---VDIVQGKDtlYHVMYIGTEYGTILKALSTTNrslRSCYLEEMQILPpgQREPIRSLQILHSdrSLFV 425

                ....*....
gi 8894934  154 GSRTEVTQV 162
Cdd:cd11264 426 GLNNGVLKI 434
Sema_5 cd11241
The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins ...
4-162 4.67e-06

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 [Multi-domain]  Cd Length: 438  Bit Score: 48.70  E-value: 4.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934    4 IRTVLNGPFRELKHDCNRGLPVvdndvPQPRPGECITNNMKLrhfGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPLLVT 83
Cdd:cd11241 279 INQAFNGPFKYQENNGSAWLPT-----PNPHPNFQCTTSIDR---GQPANTTERDLQDAQKYQLMAEVVQPVTKIPLVTM 350
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   84 TDTAYLRVVAHRVTSLSGKEYDVLYLGTEDGHLHRA-VRIGAQ-LSVLEDLALFPEPQ--PVENMKLYHS--WLLVGSRT 157
Cdd:cd11241 351 DDVRFSKLAVDVVQGRGTQLVHIFYVGTDYGTILKMyQPHRSQkSCTLEEIKILPAMKgePITSLQFLKSekSLFVGLET 430

                ....*
gi 8894934  158 EVTQV 162
Cdd:cd11241 431 GVLRI 435
Sema_plexin_A2 cd11272
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
95-196 1.35e-05

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: 47.23  E-value: 1.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8894934   95 RVTSLSG---KEYDVLYLGTEDGHLHRaVRIGAQLS---VLEDLALFPEPQPV-ENM--KLYHSWLLVGSRTEVTQVNTT 165
Cdd:cd11272 394 RLTSVASyvyNGYSVVFVGTKSGKLKK-IRADGPPHggvQYEMVSVFKDGSPIlRDMafSIDHKYLYVMSERQVSRVPVE 472
                        90       100       110
                ....*....|....*....|....*....|.
gi 8894934  166 NCGRLQSCSECILAQDPVCAWsfrldeCVAH 196
Cdd:cd11272 473 SCEQYTTCGECLSSGDPHCGW------CALH 497
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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