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Conserved domains on  [gi|11386199|ref|NP_056295|]
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nectin-3 isoform 1 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IgV_1_Nectin-3_like cd05887
First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor ...
 58-167 3.84e-73

First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor related protein 3), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 (PVRL3) or cluster of differentiation (CD) 113). Nectin-3 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example, during spermatid development, the nectin-3,-2 trans-interaction is required for the formation of Sertoli cell-spermatid junctions in testis, and during morphogenesis of the ciliary body, the nectin-3,-1 trans-interaction is important for apex-apex adhesion between the pigment and non-pigment layers of the ciliary epithelia. Nectins also heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls); nectin-3 for example, trans-interacts with Necl-5, regulating cell movement and proliferation. Other proteins with which nectin-3 interacts include the actin filament-binding protein, afadin, integrin alpha-beta3, Par-3, and PDGF receptor; its interaction with PDGF receptor regulates the latter's signaling for anti-apoptosis.


:

Pssm-ID: 409470  Cd Length: 110  Bit Score: 228.28  E-value: 3.84e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199  58 GPIIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSSQTVAVHHPQYGFSVQGEYQGRVLFKNYSLNDATITLHN 137
Cdd:cd05887   1 GPIIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSSQTVAVHHPQYGISIQGEYQGRVSFKNYSLNDATITLHN 80

                        90       100       110
                ....*....|....*....|....*....|
gi 11386199 138 IGFSDSGKYICKAVTFPLGNAQSSTTVTVL 167
Cdd:cd05887  81 VGFSDSGKYICKAVTFPLGNAQSSTTVTVL 110
IgC1_2_Nectin-3-4_like cd07704
Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related ...
 170-265 1.56e-56

Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related protein 4), and similar domains; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 or cluster of differentiation (CD) 113) and nectin-4 (poliovirus receptor related protein 4). Nectin-3 and nectin-4 belong to the nectin family comprised of four transmembrane glycoproteins (nectin-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. Nectin-3 has also been shown to form a heterophilic trans-interaction with nectin-1 in ciliary epithelia, establishing the apex-apex adhesion between the pigment and non-pigment cell layers. Nectin-4 has recently been identified in several types of breast carcinoma and can be used as a histological and serological marker for breast cancer.


:

Pssm-ID: 409501  Cd Length: 96  Bit Score: 184.25  E-value: 1.56e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199 170 PTVSLIKGPDSLIDGGNETVAAICIAATGKPVAHIDWEGDLGEMESTTTSFPNETATIISQYKLFPTRFARGRRITCVVK 249
Cdd:cd07704   1 PLVSLNPGPALLIDGGNETLAASCTAETGKPAASVTWETDLGGMESSRTFEHNRTATVTSEYHLVPTRFANGRPLTCVVS 80

                        90
                ....*....|....*.
gi 11386199 250 HPALEKDIRYSFILDI 265
Cdd:cd07704  81 HPALQQDIRITHILDV 96
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 269-355 3.71e-16

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.


The actual alignment was detected with superfamily member cd20930:

Pssm-ID: 472250  Cd Length: 86  Bit Score: 73.75  E-value: 3.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199 269 PEVSVTGYDGNWFVGRKGVNLKCNADANPPPFKSVWSRLDGQWPDGLLASDNTLhFVHPLTFNYSGVYICKVTNSLGQRS 348
Cdd:cd20930   1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQL-LIHSVDRLVNTTFICTVTNAVGTGR 79


                ....*..
gi 11386199 349 DQKVIYI 355
Cdd:cd20930  80 AEQTIFV 86
TM_EGFR-like cd12087
Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine ...
 404-432 5.87e-03

Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane (TM) helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. They are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. The TM domain not only serves as a membrane anchor, but also plays an important role in receptor dimerization and optimal activation. Mutations in the TM domain of EGFR family RTKs have been associated with increased breast cancer risk.


:

Pssm-ID: 213052  Cd Length: 38  Bit Score: 34.81  E-value: 5.87e-03
                        10        20
                ....*....|....*....|....*....
gi 11386199 404 TIIASVVGGALFIVLVSVLaGIFCYRRRR 432
Cdd:cd12087   6 TSIAAGVVGGLLVLVILGL-IVFLFRRRR 33
 
Name Accession Description Interval E-value
IgV_1_Nectin-3_like cd05887
First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor ...
 58-167 3.84e-73

First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor related protein 3), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 (PVRL3) or cluster of differentiation (CD) 113). Nectin-3 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example, during spermatid development, the nectin-3,-2 trans-interaction is required for the formation of Sertoli cell-spermatid junctions in testis, and during morphogenesis of the ciliary body, the nectin-3,-1 trans-interaction is important for apex-apex adhesion between the pigment and non-pigment layers of the ciliary epithelia. Nectins also heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls); nectin-3 for example, trans-interacts with Necl-5, regulating cell movement and proliferation. Other proteins with which nectin-3 interacts include the actin filament-binding protein, afadin, integrin alpha-beta3, Par-3, and PDGF receptor; its interaction with PDGF receptor regulates the latter's signaling for anti-apoptosis.


Pssm-ID: 409470  Cd Length: 110  Bit Score: 228.28  E-value: 3.84e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199  58 GPIIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSSQTVAVHHPQYGFSVQGEYQGRVLFKNYSLNDATITLHN 137
Cdd:cd05887   1 GPIIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSSQTVAVHHPQYGISIQGEYQGRVSFKNYSLNDATITLHN 80

                        90       100       110
                ....*....|....*....|....*....|
gi 11386199 138 IGFSDSGKYICKAVTFPLGNAQSSTTVTVL 167
Cdd:cd05887  81 VGFSDSGKYICKAVTFPLGNAQSSTTVTVL 110
IgC1_2_Nectin-3-4_like cd07704
Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related ...
 170-265 1.56e-56

Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related protein 4), and similar domains; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 or cluster of differentiation (CD) 113) and nectin-4 (poliovirus receptor related protein 4). Nectin-3 and nectin-4 belong to the nectin family comprised of four transmembrane glycoproteins (nectin-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. Nectin-3 has also been shown to form a heterophilic trans-interaction with nectin-1 in ciliary epithelia, establishing the apex-apex adhesion between the pigment and non-pigment cell layers. Nectin-4 has recently been identified in several types of breast carcinoma and can be used as a histological and serological marker for breast cancer.


Pssm-ID: 409501  Cd Length: 96  Bit Score: 184.25  E-value: 1.56e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199 170 PTVSLIKGPDSLIDGGNETVAAICIAATGKPVAHIDWEGDLGEMESTTTSFPNETATIISQYKLFPTRFARGRRITCVVK 249
Cdd:cd07704   1 PLVSLNPGPALLIDGGNETLAASCTAETGKPAASVTWETDLGGMESSRTFEHNRTATVTSEYHLVPTRFANGRPLTCVVS 80

                        90
                ....*....|....*.
gi 11386199 250 HPALEKDIRYSFILDI 265
Cdd:cd07704  81 HPALQQDIRITHILDV 96
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 175-257 1.05e-22

CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.


Pssm-ID: 400489  Cd Length: 89  Bit Score: 92.10  E-value: 1.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199   175 IKGPDSLIDGGNETVAAICIAATGKPVAHIDWEGDLGEM----ESTTTSFPNETATIISQYKLFPTRFARGRRITCVVKH 250
Cdd:pfam08205   3 IEPPASLLEGEGPEVVATCSSAGGKPAPRITWYLDGKPLeaaeTSSEQDPESGLVTVTSELKLVPSRSDHGQSLTCQVSY 82


                  ....*..
gi 11386199   251 PALEKDI 257
Cdd:pfam08205  83 GALRGSI 89
Ig3_Nectin-5_like cd20930
Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here ...
 269-355 3.71e-16

Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here are composed of the third immunoglobulin domain of Nectin-like Protein-5 (also known as Cluster of Differentiation 155 (CD155)). Nectin-like Protein-5 mediates NK (Natural Killer) cell adhesion and triggers NK cell effector functions. CD155 binds two different NK cell receptors: CD96 and CD226. These interactions accumulate at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytotoxicity of activated NK cells. CD155 may also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Moreover, CD155 plays a role in mediating tumor cell invasion and migration.


Pssm-ID: 409524  Cd Length: 86  Bit Score: 73.75  E-value: 3.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199 269 PEVSVTGYDGNWFVGRKGVNLKCNADANPPPFKSVWSRLDGQWPDGLLASDNTLhFVHPLTFNYSGVYICKVTNSLGQRS 348
Cdd:cd20930   1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQL-LIHSVDRLVNTTFICTVTNAVGTGR 79


                ....*..
gi 11386199 349 DQKVIYI 355
Cdd:cd20930  80 AEQTIFV 86
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 61-167 7.96e-11

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 59.01  E-value: 7.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199    61 IVEPHVTAVWGKNVSLKCLI--EVNETITQISWEKIHGKSSQTVAVHHpQYGFSVQGEYQGRV-LFKNYSLNDATITLHN 137
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYssSMSEASTSVYWYRQPPGKGPTFLIAY-YSNGSEEGVKKGRFsGRGDPSNGDGSLTIQN 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 11386199   138 IGFSDSGKYICKAVTFPLGNAQSSTTVTVL 167
Cdd:pfam07686  80 LTLSDSGTYTCAVIPSGEGVFGKGTRLTVL 109
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 64-166 2.64e-07

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: 48.27  E-value: 2.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199     64 PHVTAVWGKNVSLKCLIEVNETItQISWEKIHGKSSQtvavhhpqygfsvqgeYQGRVLFKNYSlNDATITLHNIGFSDS 143
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPP-EVTWYKQGGKLLA----------------ESGRFSVSRSG-STSTLTISNVTPEDS 63

                           90       100
                   ....*....|....*....|...
gi 11386199    144 GKYICkAVTFPLGNAQSSTTVTV 166
Cdd:smart00410  64 GTYTC-AATNSSGSASSGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 287-348 2.00e-06

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: 45.96  E-value: 2.00e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11386199    287 VNLKCNADANPPPFKSvWSRLDGQW---PDGLLASDNTLHFV---HPLTFNYSGVYICKVTNSLGQRS 348
Cdd:smart00410  12 VTLSCEASGSPPPEVT-WYKQGGKLlaeSGRFSVSRSGSTSTltiSNVTPEDSGTYTCAATNSSGSAS 78
I-set pfam07679
Immunoglobulin I-set domain;
287-348 7.31e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 38.78  E-value: 7.31e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11386199   287 VNLKCNADANPPPfKSVWSRlDGQwpdgLLASDNTLHF----------VHPLTFNYSGVYICKVTNSLGQRS 348
Cdd:pfam07679  18 ARFTCTVTGTPDP-EVSWFK-DGQ----PLRSSDRFKVtyeggtytltISNVQPDDSGKYTCVATNSAGEAE 83
TM_EGFR-like cd12087
Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine ...
 404-432 5.87e-03

Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane (TM) helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. They are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. The TM domain not only serves as a membrane anchor, but also plays an important role in receptor dimerization and optimal activation. Mutations in the TM domain of EGFR family RTKs have been associated with increased breast cancer risk.


Pssm-ID: 213052  Cd Length: 38  Bit Score: 34.81  E-value: 5.87e-03
                        10        20
                ....*....|....*....|....*....
gi 11386199 404 TIIASVVGGALFIVLVSVLaGIFCYRRRR 432
Cdd:cd12087   6 TSIAAGVVGGLLVLVILGL-IVFLFRRRR 33
 
Name Accession Description Interval E-value
IgV_1_Nectin-3_like cd05887
First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor ...
 58-167 3.84e-73

First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor related protein 3), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 (PVRL3) or cluster of differentiation (CD) 113). Nectin-3 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example, during spermatid development, the nectin-3,-2 trans-interaction is required for the formation of Sertoli cell-spermatid junctions in testis, and during morphogenesis of the ciliary body, the nectin-3,-1 trans-interaction is important for apex-apex adhesion between the pigment and non-pigment layers of the ciliary epithelia. Nectins also heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls); nectin-3 for example, trans-interacts with Necl-5, regulating cell movement and proliferation. Other proteins with which nectin-3 interacts include the actin filament-binding protein, afadin, integrin alpha-beta3, Par-3, and PDGF receptor; its interaction with PDGF receptor regulates the latter's signaling for anti-apoptosis.


Pssm-ID: 409470  Cd Length: 110  Bit Score: 228.28  E-value: 3.84e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199  58 GPIIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSSQTVAVHHPQYGFSVQGEYQGRVLFKNYSLNDATITLHN 137
Cdd:cd05887   1 GPIIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSSQTVAVHHPQYGISIQGEYQGRVSFKNYSLNDATITLHN 80

                        90       100       110
                ....*....|....*....|....*....|
gi 11386199 138 IGFSDSGKYICKAVTFPLGNAQSSTTVTVL 167
Cdd:cd05887  81 VGFSDSGKYICKAVTFPLGNAQSSTTVTVL 110
IgC1_2_Nectin-3-4_like cd07704
Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related ...
 170-265 1.56e-56

Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related protein 4), and similar domains; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 or cluster of differentiation (CD) 113) and nectin-4 (poliovirus receptor related protein 4). Nectin-3 and nectin-4 belong to the nectin family comprised of four transmembrane glycoproteins (nectin-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. Nectin-3 has also been shown to form a heterophilic trans-interaction with nectin-1 in ciliary epithelia, establishing the apex-apex adhesion between the pigment and non-pigment cell layers. Nectin-4 has recently been identified in several types of breast carcinoma and can be used as a histological and serological marker for breast cancer.


Pssm-ID: 409501  Cd Length: 96  Bit Score: 184.25  E-value: 1.56e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199 170 PTVSLIKGPDSLIDGGNETVAAICIAATGKPVAHIDWEGDLGEMESTTTSFPNETATIISQYKLFPTRFARGRRITCVVK 249
Cdd:cd07704   1 PLVSLNPGPALLIDGGNETLAASCTAETGKPAASVTWETDLGGMESSRTFEHNRTATVTSEYHLVPTRFANGRPLTCVVS 80

                        90
                ....*....|....*.
gi 11386199 250 HPALEKDIRYSFILDI 265
Cdd:cd07704  81 HPALQQDIRITHILDV 96
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 58-166 9.70e-51

First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 and necl-5), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (necl-5)). Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), that result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted; CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" with a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the first Ig-like domain of nectin-1 (also known as poliovirus receptor related protein(PVRL)1; CD111), nectin-3 (also known as PVRL 3), nectin-4 (also known as PVRL4; LNIR receptor)and DNAX accessory molecule 1 (DNAM-1; CD226).


Pssm-ID: 409383  Cd Length: 113  Bit Score: 169.55  E-value: 9.70e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199  58 GPIIVEPHVTAVWGKNVSLKCLIEVNET--ITQISWEKIHGKSSQTVAVHHPQYGFSVQGEYQGRVLFKNYS--LNDATI 133
Cdd:cd05718   1 QRVQVPTEVTGFLGGSVTLPCSLTSPGTtkITQVTWMKIGAGSSQNVAVFHPQYGPSVPNPYAERVEFLAARlgLRNATL 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 11386199 134 TLHNIGFSDSGKYICKAVTFPLGNAQSSTTVTV 166
Cdd:cd05718  81 RIRNLRVEDEGNYICEFATFPQGNRQGTTWLRV 113
IgC1_2_PVR_like cd05719
Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), ...
 170-265 3.46e-45

Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), and similar domains; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (Necl-5)) and similar proteins. Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), these result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted, while CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" and has a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the second Ig-like domain of nectin-1, also known as poliovirus receptor related protein(PVRL)1 or CD111.


Pssm-ID: 409384  Cd Length: 96  Bit Score: 154.19  E-value: 3.46e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199 170 PTVSLIKGPDSLIdGGNETVAAICIAATGKPVAHIDWEGDLGEMESTTTSFP-NETATIISQYKLFPTRFARGRRITCVV 248
Cdd:cd05719   1 PTNSLEGGPALLI-GGEPTLVATCISANGKPPASVTWETDLKGEASTTQVRGsNGTVTVTSRYRLVPSREADGQPLTCVV 79

                        90
                ....*....|....*..
gi 11386199 249 KHPALEKDIRYSFILDI 265
Cdd:cd05719  80 EHPSLEKDQRISVTLNV 96
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 175-257 1.05e-22

CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.


Pssm-ID: 400489  Cd Length: 89  Bit Score: 92.10  E-value: 1.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199   175 IKGPDSLIDGGNETVAAICIAATGKPVAHIDWEGDLGEM----ESTTTSFPNETATIISQYKLFPTRFARGRRITCVVKH 250
Cdd:pfam08205   3 IEPPASLLEGEGPEVVATCSSAGGKPAPRITWYLDGKPLeaaeTSSEQDPESGLVTVTSELKLVPSRSDHGQSLTCQVSY 82


                  ....*..
gi 11386199   251 PALEKDI 257
Cdd:pfam08205  83 GALRGSI 89
IgV_1_Nectin-1_like cd05886
First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here ...
 71-167 5.60e-20

First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-1 (also known as poliovirus receptor related protein 1 (PVRL1) or cluster of differentiation (CD) 111). Nectin-1 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. In addition nectins heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls), nectin-1 for example, has been shown to trans-interact with Necl-1. Nectins also interact with various other proteins, including the actin filament (F-actin)-binding protein, afadin. Mutation in the human nectin-1 gene is associated with cleft lip/palate ectodermal dysplasia syndrome (CLPED1). Nectin-1 is a major receptor for herpes simplex virus through interaction with the viral envelope glycoprotein D.


Pssm-ID: 409469  Cd Length: 113  Bit Score: 85.40  E-value: 5.60e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199  71 GKNVSLKCLI---EVNETITQISWEKIHGKSSQTVAVHHPQYGFSVQGEYQGRVLFKNYSLNDATITLHNIGFSDSGKYI 147
Cdd:cd05886  14 GTDVVLHCSFanpLPSVKITQVTWQKSTNGSKQNVAIYNPSMGVSVLPPYRERVTFLNPSFTDGTIRLSRLELEDEGVYI 93

                        90       100
                ....*....|....*....|
gi 11386199 148 CKAVTFPLGNAQSSTTVTVL 167
Cdd:cd05886  94 CEFATFPTGNRESQLNLTVM 113
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 60-166 3.60e-19

First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of rat MRC OX-2 antigen (also known as CD200) and similar proteins. MRC OX-2 is a membrane glycoprotein expressed in a variety of lymphoid and non-lymphoid cells in rats. It has a similar broad distribution pattern in humans. MRC OX-2 may regulate myeloid cell activity. The protein has an extracellular portion containing two Ig-like domains, a transmembrane portion, and a cytoplasmic portion.


Pssm-ID: 409433  Cd Length: 108  Bit Score: 82.78  E-value: 3.60e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199  60 IIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSSQTVAVHHPQYGFSVQGEYQGRVLFKNYSLNDATITLHNIG 139
Cdd:cd05846   2 VVHTGDTRAVLGGNATLSCNLTLPEEVLQVTWQKIKASSPENIVTYSKKYGVKIQPSYVRRISFTSSGLNSTSITIWNVT 81

                        90       100
                ....*....|....*....|....*..
gi 11386199 140 FSDSGKYICKAVTFPLGNAQSSTTVTV 166
Cdd:cd05846  82 LEDEGCYKCLFNTFPDGIKSGTACLTV 108
Ig3_Nectin-5_like cd20930
Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here ...
 269-355 3.71e-16

Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here are composed of the third immunoglobulin domain of Nectin-like Protein-5 (also known as Cluster of Differentiation 155 (CD155)). Nectin-like Protein-5 mediates NK (Natural Killer) cell adhesion and triggers NK cell effector functions. CD155 binds two different NK cell receptors: CD96 and CD226. These interactions accumulate at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytotoxicity of activated NK cells. CD155 may also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Moreover, CD155 plays a role in mediating tumor cell invasion and migration.


Pssm-ID: 409524  Cd Length: 86  Bit Score: 73.75  E-value: 3.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199 269 PEVSVTGYDGNWFVGRKGVNLKCNADANPPPFKSVWSRLDGQWPDGLLASDNTLhFVHPLTFNYSGVYICKVTNSLGQRS 348
Cdd:cd20930   1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQL-LIHSVDRLVNTTFICTVTNAVGTGR 79


                ....*..
gi 11386199 349 DQKVIYI 355
Cdd:cd20930  80 AEQTIFV 86
IgV_1_DNAM-1_like cd05889
First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; ...
 64-170 9.75e-16

First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of DNAX accessory molecule 1 (DNAM-1, also known as CD226). DNAM-1 is a transmembrane protein having two Ig-like domains. It is an adhesion molecule which plays a part in tumor-directed cytotoxicity and adhesion in natural killer (NK) cells and T lymphocytes. It has been shown to regulate the NK cell killing of several tumor types, including myeloma cells and ovarian carcinoma cells. DNAM-1 interacts specifically with poliovirus receptor (PVR; CD155) and nectin -2 (CD211), other members of the Ig superfamily. DNAM-1 is expressed in most peripheral T cells, NK cells, monocytes and a subset of B lymphocytes.


Pssm-ID: 409472  Cd Length: 111  Bit Score: 73.36  E-value: 9.75e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199  64 PHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSsQTVAVHHPQYGFSVQGEYQGRVLFKNYSL--NDATITLHNIGFS 141
Cdd:cd05889   7 WDTSVPLSENMSLECVYPSTGILTQVEWTKIGGQK-DNIAVYHPTHGMHIRKPYAGRVYFLNSTMasNNMSLSFRNASED 85

                        90       100
                ....*....|....*....|....*....
gi 11386199 142 DSGKYICKAVTFPLGnaqSSTTVTVLVEP 170
Cdd:cd05889  86 DVGYYSCSLYTYPQG---SWEKVIQVVQS 111
IgC1_2_Nectin-2_Necl-5_like cd07703
Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; ...
 184-256 2.08e-15

Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; member of the C1-set of the Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'.


Pssm-ID: 409500  Cd Length: 97  Bit Score: 71.66  E-value: 2.08e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11386199 184 GGNETVAAICIAATGKPVAHIDWEGDLGEMESTT--TSFPNETATIISQYKLFPTRFARGRRITCVVKHPALEKD 256
Cdd:cd07703  13 GGIPVPVARCVSANGRPPARISWSSTLNGNANTTqvPGPDSGTVTVTSEYSLVPTPEANGKEVTCKVEHETLEEP 87
IgV_1_Nectin-4_like cd05888
First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are ...
 66-167 1.03e-14

First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-4 (also known as poliovirus receptor related protein 4 or LNIR receptor). Nectin-4 belongs to the nectin family, which is comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example nectin-4 trans-interacts with nectin-1. Nectin-4 has also been shown to interact with the actin filament-binding protein, afadin. Unlike the other nectins, which are widely expressed in adult tissues, nectin-4 is mainly expressed during embryogenesis, and is not detected in normal adult tissue or in serum. Nectin-4 is re-expressed in breast carcinoma, and patients having metastatic breast cancer have a circulating form of nectin-4 formed from the ectodomain


Pssm-ID: 409471  Cd Length: 108  Bit Score: 70.31  E-value: 1.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199  66 VTAVWGKNVSLKCLIEVN--ETITQISWEKIH-GKSSQTVAVHHPQYGFSVQGEYQGRVLFK-NYSLNDATITLHNIGFS 141
Cdd:cd05888   3 VTVVLGQDAKLPCFYRGDsgEQVGQVAWARVDaGEGAQEIALLHSKYGLHVFPAYEGRVEQPpPPRPADGSVLLRNAVQA 82

                        90       100
                ....*....|....*....|....*.
gi 11386199 142 DSGKYICKAVTFPLGNAQSSTTVTVL 167
Cdd:cd05888  83 DEGEYECRVSTFPAGNFQAELRLRVL 108
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 60-166 9.40e-13

First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'.


Pssm-ID: 409581  Cd Length: 112  Bit Score: 64.91  E-value: 9.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199  60 IIVEPHVTAVWGKNVSLKCLIEVNE---TITQISWEKiHGkSSQTVAVHHPQYGFSVQGEyqGRVLF----KNYSLNDAT 132
Cdd:cd20989   3 VQVPPEVRGFLGGSVTLPCHLLPPNmvtHVSQVTWQR-HD-EHGSVAVFHPKQGPSFPES--ERLSFvaarLGAELRNAS 78

                        90       100       110
                ....*....|....*....|....*....|....
gi 11386199 133 ITLHNIGFSDSGKYICKAVTFPLGNAQSSTTVTV 166
Cdd:cd20989  79 LAMFGLRVEDEGNYTCEFATFPQGSRSGDTWLRV 112
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 61-167 7.96e-11

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 59.01  E-value: 7.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199    61 IVEPHVTAVWGKNVSLKCLI--EVNETITQISWEKIHGKSSQTVAVHHpQYGFSVQGEYQGRV-LFKNYSLNDATITLHN 137
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYssSMSEASTSVYWYRQPPGKGPTFLIAY-YSNGSEEGVKKGRFsGRGDPSNGDGSLTIQN 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 11386199   138 IGFSDSGKYICKAVTFPLGNAQSSTTVTVL 167
Cdd:pfam07686  80 LTLSDSGTYTCAVIPSGEGVFGKGTRLTVL 109
IgC1_2_Nectin-1_like cd05890
Second immunoglobulin (Ig) domain of nectin-1, and similar domains; member of the C1-set of Ig ...
 191-250 4.56e-10

Second immunoglobulin (Ig) domain of nectin-1, and similar domains; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-1 (also known as poliovirus receptor related protein 1, or cluster of differentiation (CD) 111). Nectin-1 belongs to the nectin family comprised of four transmembrane glycoproteins (nectin-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectins also heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls); nectin-1 for example, has been shown to trans-interact with Necl-1. Nectins also interact with various other proteins, including the actin filament (F-actin)-binding protein, afadin. Mutation in the human nectin-1 gene is associated with cleft lip/palate ectodermal dysplasia syndrome (CLPED1). Nectin-1 is a major receptor for herpes simplex virus through interaction with the viral envelope glycoprotein D.


Pssm-ID: 143298  Cd Length: 98  Bit Score: 56.54  E-value: 4.56e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 11386199 191 AICIAATGKPVAHIDWEGDL-GEMESTTTSFPNETATIISQYKLFPTRFARGRRITCVVKH 250
Cdd:cd05890  25 ATCTSANGKPPSVVSWDTRLkGEAEFQEIRNPNGTVTVISRYRLVPSREAHQQSLACIVNY 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 64-166 2.64e-07

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: 48.27  E-value: 2.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199     64 PHVTAVWGKNVSLKCLIEVNETItQISWEKIHGKSSQtvavhhpqygfsvqgeYQGRVLFKNYSlNDATITLHNIGFSDS 143
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPP-EVTWYKQGGKLLA----------------ESGRFSVSRSG-STSTLTISNVTPEDS 63

                           90       100
                   ....*....|....*....|...
gi 11386199    144 GKYICkAVTFPLGNAQSSTTVTV 166
Cdd:smart00410  64 GTYTC-AATNSSGSASSGTTLTV 85
IgV_1_JAM1-like cd20946
First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of ...
 63-168 1.66e-06

First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of the V-set of IgSF domains; The members here are composed of the first Ig-like domain of Junctional Adhesion Molecule-1 (JAM1)and similar domains. JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The IgSF is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. 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 first Ig-like domain of JAM1 is a member of the V-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C'-C" in the other.


Pssm-ID: 409538  Cd Length: 102  Bit Score: 46.76  E-value: 1.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199  63 EPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGksSQTVAVHHPQygfSVQGEYQGRVlfknySLNDATITLHNIGFSD 142
Cdd:cd20946   6 QQVVTVVENQEVILSCKTPKKTSSPRVEWKKLQR--DVTFVVFQNN---KIQGDYKGRA-----EILGTNITIKNVTRSD 75

                        90       100
                ....*....|....*....|....*.
gi 11386199 143 SGKYICKAVTFPLGNAQSSTTVTVLV 168
Cdd:cd20946  76 SGKYRCEVSARSDGQNLGEVTVTLEV 101
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 287-348 2.00e-06

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: 45.96  E-value: 2.00e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11386199    287 VNLKCNADANPPPFKSvWSRLDGQW---PDGLLASDNTLHFV---HPLTFNYSGVYICKVTNSLGQRS 348
Cdd:smart00410  12 VTLSCEASGSPPPEVT-WYKQGGKLlaeSGRFSVSRSGSTSTltiSNVTPEDSGTYTCAATNSSGSAS 78
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 66-148 2.29e-05

Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in human cartilage link protein (LP; also called hyaluronan and proteoglycan link protein). In cartilage, chondroitin-keratan sulfate proteoglycan (CSPG), aggrecan, forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409461  Cd Length: 117  Bit Score: 43.85  E-value: 2.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199  66 VTAVWGKNVSLKCLIEVNETI-----TQISWEKIHGKSSQTVAV------HHPQYGfsvqgEYQGRVLFKNYSLNDATIT 134
Cdd:cd05877   7 VFSHRGGNVTLPCRYHYEPELsaprkIRVKWTKLEVDYAKEEDVlvaigtRHKSYG-----SYQGRVFLRRADDLDASLV 81

                        90
                ....*....|....
gi 11386199 135 LHNIGFSDSGKYIC 148
Cdd:cd05877  82 ITDLRLEDYGRYRC 95
IgV_CRIg cd16089
Immunoglobulin variable (IgV)-like domain in complement receptor of the immunoglobulin ...
 59-153 9.93e-05

Immunoglobulin variable (IgV)-like domain in complement receptor of the immunoglobulin superfamily (CRIg); The members here are composed of the immunoglobulin variable (IgV) region of the complement receptor of the immunoglobulin superfamily (CRIg). The N-terminal domain of CRIg (also known as Z39Ig and V-set and Ig domain-containing 4 (VSIG4) belongs to the IgV family of immunoglobulin-like domains while the C-terminal domain of CRIg belongs to the IgC family of immunoglobulin-like domains. Like all members of this family, the CRIg domain contains two beta-sheets: one composed of strands A', G, F, C, C' and C", and the other of strands B, E and D. The complement system is an important part of the innate immune system and is required for removal of pathogens from the bloodstream. After exposure to pathogens, the third component of the complement system, C3, is cleaved to C3b which, after recruitment of factor B, initiates formation of the alternative pathway convertases. CRIg, a complement receptor expressed on macrophages, binds to C3b and iC3b mediating phagocytosis of the particles. It is also a potent inhibitor of the alternative pathway convertases and a negative regulator of T cell activation. 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, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, 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.


Pssm-ID: 409510  Cd Length: 117  Bit Score: 42.13  E-value: 9.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199  59 PIIVEPH-VTAVWGKNVSLKCLIEVNETITQI--SWEKIHGKSSQTVAVHHPQYGFSVQGEYQGRVLFKNYSLNDATITL 135
Cdd:cd16089   1 PILEGPEsITGPWKGSVNLPCTYVPEEGYTQVlvKWLVQRDSDPVTIFLRDSSGDHIQQAKYRGRLEVSKDTPGDVSLQL 80

                        90
                ....*....|....*...
gi 11386199 136 HNIGFSDSGKYICkAVTF 153
Cdd:cd16089  81 DTLEMDDRGHYTC-QVTW 97
IgC1 cd00098
Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, ...
 171-261 1.04e-04

Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, classical Ig-like domains resembling the antibody constant domain. Members of the IgC1 family are components of immunoglobulin, T-cell receptors, CD1 cell surface glycoproteins, secretory glycoproteins A/C, and major histocompatibility complex (MHC) class I/II molecules. In immunoglobulins, each chain is composed of one variable domain (IgV) and one or more IgC domains. These names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. The IgV domain is responsible for antigen binding, while the IgC domain is involved in oligomerization and molecular interactions. 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 strands by G, F, C, and C'.


Pssm-ID: 409354  Cd Length: 95  Bit Score: 41.29  E-value: 1.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199 171 TVSLIKGPDSLIDGGNETVaaICIAaTG--KPVAHIDWEGDLGEMESTTTSFP-----NETATIISQYKLFPTRFARGRR 243
Cdd:cd00098   1 TVTLLPPSPEEKGGGKVTL--VCLV-SGfyPKDITVTWLKNGVPLTSGVSTSSpvepnDGTYSVTSSLTVPPSDWDEGAT 77

                        90
                ....*....|....*...
gi 11386199 244 ITCVVKHPALEKDIRYSF 261
Cdd:cd00098  78 YTCVVTHESLKSPLSKTW 95
IgV_CD2_like_N cd05775
N-terminal immunoglobulin (Ig)-like domain of T-cell surface antigen CD2, and similar domains; ...
 62-167 1.87e-04

N-terminal immunoglobulin (Ig)-like domain of T-cell surface antigen CD2, and similar domains; The members here are composed of the N-terminal immunoglobulin (Ig)-like domain (or domain 1) of T-cell surface antigen Clusters of Differentiation (CD) 2 and similar proteins. CD2 is a T-cell specific surface glycoprotein and is critically important for mediating adhesion between T cells and antigen-presenting cells or between cytolytic T cells and target cells. CD2 is located on chromosome 1 at 1p13 in humans and on chromosome 3 in mice. CD2 contains an extracellular domain with two or Ig-like domains, a single transmembrane segment, and a cytoplasmic region rich in proline and basic residues.


Pssm-ID: 409431  Cd Length: 98  Bit Score: 40.79  E-value: 1.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199  62 VEPHVTAVWGKNVSLKCLiEVNETITQISWEKihgkSSQTVAVHHPQYGFSVQGEYQGRVLFKNyslNDATITLHNIGFS 141
Cdd:cd05775   1 SSGEVYGALGGNVTLTIS-SLQDDIDEIKWKK----TKDKIVEWENNIGPTYFGSFKDRVLLDK---ESGSLTIKNLTKE 72

                        90       100
                ....*....|....*....|....*..
gi 11386199 142 DSGKYICKaVTFPLGNAQSST-TVTVL 167
Cdd:cd05775  73 DSGTYELE-ITSTNGKVLSSKfTLEVL 98
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 287-345 1.91e-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: 40.01  E-value: 1.91e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11386199 287 VNLKCNADANPPPfKSVWSR------LDGQWPDGLLASDNTLHFvHPLTFNYSGVYICKVTNSLG 345
Cdd:cd00096   1 VTLTCSASGNPPP-TITWYKngkplpPSSRDSRRSELGNGTLTI-SNVTLEDSGTYTCVASNSAG 63
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 287-346 2.06e-04

Third 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 third 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 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, 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, and 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 Slit2 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: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 40.07  E-value: 2.06e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11386199 287 VNLKCNADANPPPfKSVWSRLDGQWPDGL--LASDNTLHFVHpLTFNYSGVYICKVTNSLGQ 346
Cdd:cd05725  15 AEFQCEVGGDPVP-TVRWRKEDGELPKGRyeILDDHSLKIRK-VTAGDMGSYTCVAENMVGK 74
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 62-164 2.39e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 40.26  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199    62 VEPHVTAVW-GKNVSLKCLIEVNETITQISWEKiHGKSSQTVAVHHPQygfsvqgeyqgrvlfkNYSLNDATITLHNIGF 140
Cdd:pfam00047   1 SAPPTVTVLeGDSATLTCSASTGSPGPDVTWSK-EGGTLIESLKVKHD----------------NGRTTQSSLLISNVTK 63

                          90       100
                  ....*....|....*....|....
gi 11386199   141 SDSGKYICKaVTFPLGNAQSSTTV 164
Cdd:pfam00047  64 EDAGTYTCV-VNNPGGSATLSTSL 86
IgV_EVA1 cd05880
Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are ...
 66-149 2.52e-04

Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are composed of the immunoglobulin (Ig) domain of epithelial V-like antigen 1 (EVA 1). EVA is also known as myelin protein zero-like 2. EVA is an adhesion molecule and may play a role in the structural organization of the thymus and early lymphocyte development.


Pssm-ID: 409464  Cd Length: 116  Bit Score: 40.97  E-value: 2.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199  66 VTAVWGKNVSLKCLIE----VNETITqISW--EKIHGKSSQTVAVHHPQYGFSVQGEYQGRVLFK-NYSLNDATITLHNI 138
Cdd:cd05880   9 VEAVNGTDVRLKCTFSssapIGDTLV-ITWnfRPLDGGREESVFYYHKRPYPPPDGRFKGRVVWDgNIMRRDASILIWQL 87

                        90
                ....*....|.
gi 11386199 139 GFSDSGKYICK 149
Cdd:cd05880  88 QPTDNGTYTCQ 98
IgV_1_Necl-1 cd05882
First (N-terminal) immunoglobulin (Ig)-like domain of nectin-like molecule-1 (Necl-1); member ...
 66-164 2.63e-04

First (N-terminal) immunoglobulin (Ig)-like domain of nectin-like molecule-1 (Necl-1); member of the V-set of Ig superfamily (IgSF) domains; The members here are composed of the N-terminal immunoglobulin (Ig)-like domain of nectin-like molecule-1, Necl-1 (also known as celll adhesion molecule 3 (CADM3), SynCAM2, or IGSF4). Nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 - Necl-5). They all have an extracellular region containing three Ig-like domains, a transmembrane region, and a cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1 has Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue and is important to the formation of synapses, axon bundles, and myelinated axons.


Pssm-ID: 143290  Cd Length: 95  Bit Score: 40.42  E-value: 2.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199  66 VTAVWGKNVSLKCLIEVNETiTQISWEKihgKSSQTVavhhpqYGFSVQGEYQGRVLFKNYSLNDATITLHNIGFSDSGK 145
Cdd:cd05882   7 ETVAVGGTVTLKCGVKEHDN-SSLQWSN---TAQQTL------YFGEKRALRDNRIQLVKSTPTELIISISNVQLSDEGE 76

                        90
                ....*....|....*....
gi 11386199 146 YICKAVTFPLGNAQSSTTV 164
Cdd:cd05882  77 YTCSIFTMPVRTAKATVTV 95
I-set pfam07679
Immunoglobulin I-set domain;
65-166 3.22e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 39.93  E-value: 3.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199    65 HVTAVWGKNVSLKCLIEVNETItQISWEKihGKSSQTVAVHHpqygfsvqgeyqgRVLFKNyslNDATITLHNIGFSDSG 144
Cdd:pfam07679   9 DVEVQEGESARFTCTVTGTPDP-EVSWFK--DGQPLRSSDRF-------------KVTYEG---GTYTLTISNVQPDDSG 69

                          90       100
                  ....*....|....*....|..
gi 11386199   145 KYICKAvTFPLGNAQSSTTVTV 166
Cdd:pfam07679  70 KYTCVA-TNSAGEAEASAELTV 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 60-150 5.07e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 39.09  E-value: 5.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199    60 IIVEP-HVTAVWGKNVSLKCLIEVNETITqISWEKiHGKSSQTvavhhpqygfsvqgeyqGRVLFKNYSLNDATITLHNI 138
Cdd:pfam13927   4 ITVSPsSVTVREGETVTLTCEATGSPPPT-ITWYK-NGEPISS-----------------GSTRSRSLSGSNSTLTISNV 64

                          90
                  ....*....|..
gi 11386199   139 GFSDSGKYICKA 150
Cdd:pfam13927  65 TRSDAGTYTCVA 76
I-set pfam07679
Immunoglobulin I-set domain;
287-348 7.31e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 38.78  E-value: 7.31e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11386199   287 VNLKCNADANPPPfKSVWSRlDGQwpdgLLASDNTLHF----------VHPLTFNYSGVYICKVTNSLGQRS 348
Cdd:pfam07679  18 ARFTCTVTGTPDP-EVSWFK-DGQ----PLRSSDRFKVtyeggtytltISNVQPDDSGKYTCVATNSAGEAE 83
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 71-166 1.39e-03

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 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" strands in the other.


Pssm-ID: 409355 [Multi-domain]  Cd Length: 111  Bit Score: 38.47  E-value: 1.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199  71 GKNVSLKCLIEVNETITQISWekIHGKSSQtvavhHPQY-------GFSVQGEYQGRVLFKNYSLNDATITLHNIGFSDS 143
Cdd:cd00099  13 GESVTLSCEVSSSFSSTYIYW--YRQKPGQ-----GPEFliylsssKGKTKGGVPGRFSGSRDGTSSFSLTISNLQPEDS 85

                        90       100
                ....*....|....*....|....*.
gi 11386199 144 GKYICKAVTFPLGNAQ---SSTTVTV 166
Cdd:cd00099  86 GTYYCAVSESGGTDKLtfgSGTRLTV 111
IgV_MOG_like cd05713
Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here ...
 58-148 1.40e-03

Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here are composed of the immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG). MOG, a minor component of the myelin sheath, is an important CNS-specific autoantigen, linked to the pathogenesis of multiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE). It is a transmembrane protein having an extracellular Ig domain. MOG is expressed in the CNS on the outermost lamellae of the myelin sheath, and on the surface of oligodendrocytes, and may participate in the completion, compaction, and/or maintenance of myelin. This group also includes butyrophilin (BTN). BTN is the most abundant protein in bovine milk-fat globule membrane (MFGM).


Pssm-ID: 409378  Cd Length: 114  Bit Score: 38.71  E-value: 1.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199  58 GPiivEPHVTAVWGKNVSLKCLI--EVNETITQISWekIHGKSSQtvAVHHPQYG---FSVQ-GEYQGRVLFKNYSLNDA 131
Cdd:cd05713   5 GP---TEPILALVGEDAELPCHLspKMSAEHMEVRW--FRSQFSP--VVHLYRDGqdqEEEQmPEYRGRTELLKDAIAEG 77

                        90
                ....*....|....*....
gi 11386199 132 TITL--HNIGFSDSGKYIC 148
Cdd:cd05713  78 SVALriHNVRPSDEGQYTC 96
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 287-342 1.48e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 37.55  E-value: 1.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11386199   287 VNLKCNADANPPPfkSVWSRLDGQWPDGLLASDNTLHF------VHPLTFNYSGVYICKVTN 342
Cdd:pfam13927  19 VTLTCEATGSPPP--TITWYKNGEPISSGSTRSRSLSGsnstltISNVTRSDAGTYTCVASN 78
IGv smart00406
Immunoglobulin V-Type;
73-149 1.58e-03

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 37.75  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199     73 NVSLKCLIEVNE-TITQISW-EKIHGKSSQTVAVHHPQYGFSVQGEYQGRVLF-KNYSLNDATITLHNIGFSDSGKYICK 149
Cdd:smart00406   1 SVTLSCKFSGSTfSSYYVSWvRQPPGKGLEWLGYIGSNGSSYYQESYKGRFTIsKDTSKNDVSLTISNLRVEDTGTYYCA 80
IgV_1_Necl_like cd05717
First (N-terminal) immunoglobulin (Ig)-like domain of the nectin-like molecules; member of the ...
 65-166 1.88e-03

First (N-terminal) immunoglobulin (Ig)-like domain of the nectin-like molecules; member of the V-set of Ig superfamily (IgSF) domains; The members here are composed of the N-terminal immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 (also known as cell adhesion molecule 3 (CADM3)), Necl-2 (CADM1), Necl-3 (CADM2), and similar proteins. At least five nectin-like molecules have been identified (Necl-1 to Necl-5). They all have an extracellular region containing three Ig-like domains, a transmembrane region, and a cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1, Necl-2, and Necl-3 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue, and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues and is a putative tumour suppressor gene which is downregulated in aggressive neuroblastoma. Necl-3 accumulates in central and peripheral nervous system tissue and has been shown to selectively interact with oligodendrocytes. This group also contains Class-I MHC-restricted T-cell-associated molecule (CRTAM), whose expression pattern is consistent with its expression in Class-I MHC-restricted T-cells.


Pssm-ID: 409382  Cd Length: 94  Bit Score: 37.88  E-value: 1.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199  65 HVTAVWGKNVSLKCLIEVNETiTQISWEKihgKSSQTVAVhhpqygfsvqGEYQG----RVLFKNYSLNDATITLHNIGF 140
Cdd:cd05717   5 DVTVVEGETLTLKCQVSLRDD-SSLQWLN---PNGQTIYF----------NDKRAlrdsRYQLLNHSASELSISVSNVTL 70

                        90       100
                ....*....|....*....|....*.
gi 11386199 141 SDSGKYICKAVTFPLgnAQSSTTVTV 166
Cdd:cd05717  71 SDEGVYTCLHYTDPV--STKKVTVTV 94
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 287-346 1.90e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 37.56  E-value: 1.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11386199   287 VNLKCNADANPPPFKSVWSRLDGQWPDGLLA-------SDNTLHFVhPLTFNYSGVYICKVTNSLGQ 346
Cdd:pfam00047  14 ATLTCSASTGSPGPDVTWSKEGGTLIESLKVkhdngrtTQSSLLIS-NVTKEDAGTYTCVVNNPGGS 79
IgI_2_Necl-2 cd05883
Second immunoglobulin (Ig)-like domain of nectin-like molecule 2 (Necl-2); member of the I-set ...
 167-257 2.31e-03

Second immunoglobulin (Ig)-like domain of nectin-like molecule 2 (Necl-2); member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin (Ig)-like domain of nectin-like molecule 2 (Necl-2; also known as cell adhesion molecule 1 (CADM1)). Nectin-like molecules (Necls) have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. Necl-2 has Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is expressed in a wide variety of tissues and is a putative tumour suppressor gene which is downregulated in aggressive neuroblastoma. Ig domains are likely to participate in ligand binding and recognition.


Pssm-ID: 409466  Cd Length: 99  Bit Score: 37.59  E-value: 2.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199 167 LVEPTVSLIKGPDSLIDGGNEtVAAICIAATGKPVAHIDWEGDLGEM--ESTTTSFPNETATIISQYKLFPTRFARGRRI 244
Cdd:cd05883   1 LVPPRNLVIDIQKDTAVEGEE-IELNCTAMASKPAATIRWFKGNKELtgKSEVEEWYSRMFTVTSQLMLKVTKEDDGVPV 79

                        90
                ....*....|...
gi 11386199 245 TCVVKHPALeKDI 257
Cdd:cd05883  80 ICLVDHPAV-KDL 91
IgC1_Tapasin_R cd05771
Tapasin-R immunoglobulin-like domain; member of the C1-set of Ig superfamily (IgSF) domains; ...
 224-260 2.91e-03

Tapasin-R immunoglobulin-like domain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin-like domain on Tapasin-R. Tapasin is a V-C1 (variable-constant) immunoglobulin superfamily molecule present in the endoplasmic reticulum (ER), where it links MHC class I molecules to the transporter associated with antigen processing (TAP). Tapasin-R is a tapasin-related protein that contains similar structural motifs to Tapasin, with some marked differences, especially in the V domain, transmembrane and cytoplasmic regions. The majority of Tapasin-R is located within the ER; however, there may be some expression of Tapasin-R at the cell surface. Tapasin-R lacks an obvious ER retention signal.


Pssm-ID: 409428  Cd Length: 100  Bit Score: 37.47  E-value: 2.91e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 11386199 224 TATIISQYKLFPTRFARGRRITCVVKHPALEKDIRYS 260
Cdd:cd05771  64 TYSISSYLTLEPGTENRGATYTCRVTHVSLEEPLSVS 100
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 128-166 5.34e-03

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: 36.28  E-value: 5.34e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 11386199 128 LNDATITLHNIGFSDSGKYICKAVTFpLGNAQSSTTVTV 166
Cdd:cd04969  52 LPDGSLKIKNVTKSDEGKYTCFAVNF-FGKANSTGSLSV 89
TM_EGFR-like cd12087
Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine ...
 404-432 5.87e-03

Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane (TM) helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. They are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. The TM domain not only serves as a membrane anchor, but also plays an important role in receptor dimerization and optimal activation. Mutations in the TM domain of EGFR family RTKs have been associated with increased breast cancer risk.


Pssm-ID: 213052  Cd Length: 38  Bit Score: 34.81  E-value: 5.87e-03
                        10        20
                ....*....|....*....|....*....
gi 11386199 404 TIIASVVGGALFIVLVSVLaGIFCYRRRR 432
Cdd:cd12087   6 TSIAAGVVGGLLVLVILGL-IVFLFRRRR 33
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
 66-148 8.70e-03

Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an extracellular Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin. This group also contains the Ig domain of sodium channel subunit beta-2 (SCN2B), and of epithelial V-like antigen 1 (EVA). EVA, also known as myelin protein zero-like 2, is an adhesion molecule, which may play a role in structural organization of the thymus and early lymphocyte development. SCN2B subunits play a role in determining sodium channel density and function in neurons,and in control of electrical excitability in the brain.


Pssm-ID: 409380  Cd Length: 117  Bit Score: 36.25  E-value: 8.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386199  66 VTAVWGKNVSLKCLIEVNETI---TQISWEKIHGKSSQTVAVHHPQYGFSVQGEY---QGRVLFK-NYSLNDATITLHNI 138
Cdd:cd05715   9 LNVLNGSDVRLTCTFTSCYTVgdaFSVTWTYQPEGGNTTESMFHYSKGKPYILKVgrfKDRVSWAgNPSKKDASIVISNL 88

                        90
                ....*....|
gi 11386199 139 GFSDSGKYIC 148
Cdd:cd05715  89 QFSDNGTYTC 98
 
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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