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Conserved domains on  [gi|1907119219|ref|XP_036015971|]
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nectin-3 isoform X2 [Mus musculus]

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 2.23e-72

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: 220.96  E-value: 2.23e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  58 GSIIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSTQTVAVHHPQYGFSVQGDYQGRVLFKNYSLNDATITLHN 137
Cdd:cd05887     1 GPIIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSSQTVAVHHPQYGISIQGEYQGRVSFKNYSLNDATITLHN 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907119219 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 2.58e-54

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: 174.24  E-value: 2.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219 170 PTVSLIKGPDSLIDGGNETVAAVCVAATGKPVAQIDWEGDLGEMESSTTSFPNETATIVSQYKLFPTRFARGRRITCVVK 249
Cdd:cd07704     1 PLVSLNPGPALLIDGGNETLAASCTAETGKPAASVTWETDLGGMESSRTFEHNRTATVTSEYHLVPTRFANGRPLTCVVS 80

                          90
                  ....*....|....*.
gi 1907119219 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 6.84e-15

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: 69.51  E-value: 6.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219 269 PEVSVTGYDGNWFVGRKGVNLKCNADANPPPFKSVWSRLDGQWPDGLLASDNTLhFVHPLTVNYSGVYVCKVSNSLGQRS 348
Cdd:cd20930     1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQL-LIHSVDRLVNTTFICTVTNAVGTGR 79


                  ....*..
gi 1907119219 349 DQKVIYI 355
Cdd:cd20930    80 AEQTIFV 86
 
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 2.23e-72

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: 220.96  E-value: 2.23e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  58 GSIIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSTQTVAVHHPQYGFSVQGDYQGRVLFKNYSLNDATITLHN 137
Cdd:cd05887     1 GPIIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSSQTVAVHHPQYGISIQGEYQGRVSFKNYSLNDATITLHN 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907119219 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 2.58e-54

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: 174.24  E-value: 2.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219 170 PTVSLIKGPDSLIDGGNETVAAVCVAATGKPVAQIDWEGDLGEMESSTTSFPNETATIVSQYKLFPTRFARGRRITCVVK 249
Cdd:cd07704     1 PLVSLNPGPALLIDGGNETLAASCTAETGKPAASVTWETDLGGMESSRTFEHNRTATVTSEYHLVPTRFANGRPLTCVVS 80

                          90
                  ....*....|....*.
gi 1907119219 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 4.48e-22

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


Pssm-ID: 400489  Cd Length: 89  Bit Score: 89.40  E-value: 4.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219 175 IKGPDSLIDGGNETVAAVCVAATGKPVAQIDWEGDLGEM----ESSTTSFPNETATIVSQYKLFPTRFARGRRITCVVKH 250
Cdd:pfam08205   3 IEPPASLLEGEGPEVVATCSSAGGKPAPRITWYLDGKPLeaaeTSSEQDPESGLVTVTSELKLVPSRSDHGQSLTCQVSY 82


                  ....*..
gi 1907119219 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 6.84e-15

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: 69.51  E-value: 6.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219 269 PEVSVTGYDGNWFVGRKGVNLKCNADANPPPFKSVWSRLDGQWPDGLLASDNTLhFVHPLTVNYSGVYVCKVSNSLGQRS 348
Cdd:cd20930     1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQL-LIHSVDRLVNTTFICTVTNAVGTGR 79


                  ....*..
gi 1907119219 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 3.75e-10

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: 56.70  E-value: 3.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  61 IVEPHVTAVWGKNVSLKCLI--EVNETITQISWEKIHGKSTQTVAVHHpQYGFSVQGDYQGRV-LFKNYSLNDATITLHN 137
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYssSMSEASTSVYWYRQPPGKGPTFLIAY-YSNGSEEGVKKGRFsGRGDPSNGDGSLTIQN 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907119219 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 4.87e-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: 47.11  E-value: 4.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219   64 PHVTAVWGKNVSLKCLIEVNETItQISWEKIHGKstqtvaVHHPQYGFSVQGDYqgrvlfknyslNDATITLHNIGFSDS 143
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPP-EVTWYKQGGK------LLAESGRFSVSRSG-----------STSTLTISNVTPEDS 63

                           90       100
                   ....*....|....*....|...
gi 1907119219  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 3.95e-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: 44.42  E-value: 3.95e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907119219  287 VNLKCNADANPPPFKSvWSRLDGQW---PDGLLASDNTLHFV---HPLTVNYSGVYVCKVSNSLGQRS 348
Cdd:smart00410  12 VTLSCEASGSPPPEVT-WYKQGGKLlaeSGRFSVSRSGSTSTltiSNVTPEDSGTYTCAATNSSGSAS 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 287-342 9.90e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 37.55  E-value: 9.90e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907119219 287 VNLKCNADANPPPfkSVWSRLDGQWPDGLLASDNTLHF------VHPLTVNYSGVYVCKVSN 342
Cdd:pfam13927  19 VTLTCEATGSPPP--TITWYKNGEPISSGSTRSRSLSGsnstltISNVTRSDAGTYTCVASN 78
 
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 2.23e-72

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: 220.96  E-value: 2.23e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  58 GSIIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSTQTVAVHHPQYGFSVQGDYQGRVLFKNYSLNDATITLHN 137
Cdd:cd05887     1 GPIIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSSQTVAVHHPQYGISIQGEYQGRVSFKNYSLNDATITLHN 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907119219 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 2.58e-54

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: 174.24  E-value: 2.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219 170 PTVSLIKGPDSLIDGGNETVAAVCVAATGKPVAQIDWEGDLGEMESSTTSFPNETATIVSQYKLFPTRFARGRRITCVVK 249
Cdd:cd07704     1 PLVSLNPGPALLIDGGNETLAASCTAETGKPAASVTWETDLGGMESSRTFEHNRTATVTSEYHLVPTRFANGRPLTCVVS 80

                          90
                  ....*....|....*.
gi 1907119219 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 ...
 60-166 1.32e-49

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: 162.62  E-value: 1.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  60 IIVEPHVTAVWGKNVSLKCLIEVNET--ITQISWEKIHGKSTQTVAVHHPQYGFSVQGDYQGRVLFKNYS--LNDATITL 135
Cdd:cd05718     3 VQVPTEVTGFLGGSVTLPCSLTSPGTtkITQVTWMKIGAGSSQNVAVFHPQYGPSVPNPYAERVEFLAARlgLRNATLRI 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907119219 136 HNIGFSDSGKYICKAVTFPLGNAQSSTTVTV 166
Cdd:cd05718    83 RNLRVEDEGNYICEFATFPQGNRQGTTWLRV 113
IgC1_2_PVR_like cd05719
Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), ...
 170-265 2.87e-43

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: 145.71  E-value: 2.87e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219 170 PTVSLIKGPDSLIdGGNETVAAVCVAATGKPVAQIDWEGDLGEMESSTTSFP-NETATIVSQYKLFPTRFARGRRITCVV 248
Cdd:cd05719     1 PTNSLEGGPALLI-GGEPTLVATCISANGKPPASVTWETDLKGEASTTQVRGsNGTVTVTSRYRLVPSREADGQPLTCVV 79

                          90
                  ....*....|....*..
gi 1907119219 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 4.48e-22

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


Pssm-ID: 400489  Cd Length: 89  Bit Score: 89.40  E-value: 4.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219 175 IKGPDSLIDGGNETVAAVCVAATGKPVAQIDWEGDLGEM----ESSTTSFPNETATIVSQYKLFPTRFARGRRITCVVKH 250
Cdd:pfam08205   3 IEPPASLLEGEGPEVVATCSSAGGKPAPRITWYLDGKPLeaaeTSSEQDPESGLVTVTSELKLVPSRSDHGQSLTCQVSY 82


                  ....*..
gi 1907119219 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 3.25e-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: 85.02  E-value: 3.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  71 GKNVSLKCLI---EVNETITQISWEKIHGKSTQTVAVHHPQYGFSVQGDYQGRVLFKNYSLNDATITLHNIGFSDSGKYI 147
Cdd:cd05886    14 GTDVVLHCSFanpLPSVKITQVTWQKSTNGSKQNVAIYNPSMGVSVLPPYRERVTFLNPSFTDGTIRLSRLELEDEGVYI 93

                          90       100
                  ....*....|....*....|
gi 1907119219 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; ...
 59-166 8.97e-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: 80.85  E-value: 8.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  59 SIIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSTQTVAVHHPQYGFSVQGDYQGRVLFKNYSLNDATITLHNI 138
Cdd:cd05846     1 VVVHTGDTRAVLGGNATLSCNLTLPEEVLQVTWQKIKASSPENIVTYSKKYGVKIQPSYVRRISFTSSGLNSTSITIWNV 80

                          90       100
                  ....*....|....*....|....*...
gi 1907119219 139 GFSDSGKYICKAVTFPLGNAQSSTTVTV 166
Cdd:cd05846    81 TLEDEGCYKCLFNTFPDGIKSGTACLTV 108
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 1.32e-16

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: 74.36  E-value: 1.32e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907119219 184 GGNETVAAVCVAATGKPVAQIDWEGDLGEM--ESSTTSFPNETATIVSQYKLFPTRFARGRRITCVVKHPALEKD 256
Cdd:cd07703    13 GGIPVPVARCVSANGRPPARISWSSTLNGNanTTQVPGPDSGTVTVTSEYSLVPTPEANGKEVTCKVEHETLEEP 87
IgV_1_DNAM-1_like cd05889
First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; ...
 64-170 4.25e-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: 73.74  E-value: 4.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  64 PHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKStQTVAVHHPQYGFSVQGDYQGRVLFKNYSL--NDATITLHNIGFS 141
Cdd:cd05889     7 WDTSVPLSENMSLECVYPSTGILTQVEWTKIGGQK-DNIAVYHPTHGMHIRKPYAGRVYFLNSTMasNNMSLSFRNASED 85

                          90       100
                  ....*....|....*....|....*....
gi 1907119219 142 DSGKYICKAVTFPLGnaqSSTTVTVLVEP 170
Cdd:cd05889    86 DVGYYSCSLYTYPQG---SWEKVIQVVQS 111
Ig3_Nectin-5_like cd20930
Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here ...
 269-355 6.84e-15

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: 69.51  E-value: 6.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219 269 PEVSVTGYDGNWFVGRKGVNLKCNADANPPPFKSVWSRLDGQWPDGLLASDNTLhFVHPLTVNYSGVYVCKVSNSLGQRS 348
Cdd:cd20930     1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQL-LIHSVDRLVNTTFICTVTNAVGTGR 79


                  ....*..
gi 1907119219 349 DQKVIYI 355
Cdd:cd20930    80 AEQTIFV 86
IgV_1_Nectin-4_like cd05888
First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are ...
 66-167 9.79e-15

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: 69.54  E-value: 9.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  66 VTAVWGKNVSLKCLIEVN--ETITQISWEKIH-GKSTQTVAVHHPQYGFSVQGDYQGRVLFK-NYSLNDATITLHNIGFS 141
Cdd:cd05888     3 VTVVLGQDAKLPCFYRGDsgEQVGQVAWARVDaGEGAQEIALLHSKYGLHVFPAYEGRVEQPpPPRPADGSVLLRNAVQA 82

                          90       100
                  ....*....|....*....|....*.
gi 1907119219 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 2.80e-12

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: 62.98  E-value: 2.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  60 IIVEPHVTAVWGKNVSLKCLIEVNE---TITQISWEKiHGKStQTVAVHHPQYGFSVQGdyQGRVLF----KNYSLNDAT 132
Cdd:cd20989     3 VQVPPEVRGFLGGSVTLPCHLLPPNmvtHVSQVTWQR-HDEH-GSVAVFHPKQGPSFPE--SERLSFvaarLGAELRNAS 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907119219 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 3.75e-10

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: 56.70  E-value: 3.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  61 IVEPHVTAVWGKNVSLKCLI--EVNETITQISWEKIHGKSTQTVAVHHpQYGFSVQGDYQGRV-LFKNYSLNDATITLHN 137
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYssSMSEASTSVYWYRQPPGKGPTFLIAY-YSNGSEEGVKKGRFsGRGDPSNGDGSLTIQN 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907119219 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 4.73e-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: 56.15  E-value: 4.73e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907119219 191 AVCVAATGKPVAQIDWEGDL-GEMESSTTSFPNETATIVSQYKLFPTRFARGRRITCVVKH 250
Cdd:cd05890    25 ATCTSANGKPPSVVSWDTRLkGEAEFQEIRNPNGTVTVISRYRLVPSREAHQQSLACIVNY 85
IgV_1_JAM1-like cd20946
First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of ...
 63-168 8.09e-08

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: 49.84  E-value: 8.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  63 EPHVTAVWGKNVSLKCLIEVNETITQISWEKIhGKSTQTVAVhhpqYGFSVQGDYQGRVlfknySLNDATITLHNIGFSD 142
Cdd:cd20946     6 QQVVTVVENQEVILSCKTPKKTSSPRVEWKKL-QRDVTFVVF----QNNKIQGDYKGRA-----EILGTNITIKNVTRSD 75

                          90       100
                  ....*....|....*....|....*.
gi 1907119219 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.
 64-166 4.87e-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: 47.11  E-value: 4.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219   64 PHVTAVWGKNVSLKCLIEVNETItQISWEKIHGKstqtvaVHHPQYGFSVQGDYqgrvlfknyslNDATITLHNIGFSDS 143
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPP-EVTWYKQGGK------LLAESGRFSVSRSG-----------STSTLTISNVTPEDS 63

                           90       100
                   ....*....|....*....|...
gi 1907119219  144 GKYICkAVTFPLGNAQSSTTVTV 166
Cdd:smart00410  64 GTYTC-AATNSSGSASSGTTLTV 85
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 66-148 3.51e-06

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: 45.78  E-value: 3.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  66 VTAVWGKNVSLKCLIEVNETI-----TQISWEKIHGKSTQTVAV------HHPQYGfsvqgDYQGRVLFKNYSLNDATIT 134
Cdd:cd05877     7 VFSHRGGNVTLPCRYHYEPELsaprkIRVKWTKLEVDYAKEEDVlvaigtRHKSYG-----SYQGRVFLRRADDLDASLV 81

                          90
                  ....*....|....
gi 1907119219 135 LHNIGFSDSGKYIC 148
Cdd:cd05877    82 ITDLRLEDYGRYRC 95
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 287-348 3.95e-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: 44.42  E-value: 3.95e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907119219  287 VNLKCNADANPPPFKSvWSRLDGQW---PDGLLASDNTLHFV---HPLTVNYSGVYVCKVSNSLGQRS 348
Cdd:smart00410  12 VTLSCEASGSPPPEVT-WYKQGGKLlaeSGRFSVSRSGSTSTltiSNVTPEDSGTYTCAATNSSGSAS 78
IgV_CD2_like_N cd05775
N-terminal immunoglobulin (Ig)-like domain of T-cell surface antigen CD2, and similar domains; ...
 62-167 3.54e-05

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: 42.33  E-value: 3.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  62 VEPHVTAVWGKNVSLKCLiEVNETITQISWEKihgkSTQTVAVHHPQYGFSVQGDYQGRVLFKNyslNDATITLHNIGFS 141
Cdd:cd05775     1 SSGEVYGALGGNVTLTIS-SLQDDIDEIKWKK----TKDKIVEWENNIGPTYFGSFKDRVLLDK---ESGSLTIKNLTKE 72

                          90       100
                  ....*....|....*....|....*..
gi 1907119219 142 DSGKYICKaVTFPLGNAQSST-TVTVL 167
Cdd:cd05775    73 DSGTYELE-ITSTNGKVLSSKfTLEVL 98
IgC1 cd00098
Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, ...
 171-261 8.97e-05

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: 40.91  E-value: 8.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219 171 TVSLIKGPDSLIDGGNETVaaVCVAaTG--KPVAQIDWEGDLGEMESSTTSFP-----NETATIVSQYKLFPTRFARGRR 243
Cdd:cd00098     1 TVTLLPPSPEEKGGGKVTL--VCLV-SGfyPKDITVTWLKNGVPLTSGVSTSSpvepnDGTYSVTSSLTVPPSDWDEGAT 77

                          90
                  ....*....|....*...
gi 1907119219 244 ITCVVKHPALEKDIRYSF 261
Cdd:cd00098    78 YTCVVTHESLKSPLSKTW 95
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 287-345 1.21e-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: 1.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907119219 287 VNLKCNADANPPPfKSVWSR------LDGQWPDGLLASDNTLHFvHPLTVNYSGVYVCKVSNSLG 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 1.24e-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: 40.46  E-value: 1.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907119219 287 VNLKCNADANPPPfKSVWSRLDGQWPDGL--LASDNTLHFVHpLTVNYSGVYVCKVSNSLGQ 346
Cdd:cd05725    15 AEFQCEVGGDPVP-TVRWRKEDGELPKGRyeILDDHSLKIRK-VTAGDMGSYTCVAENMVGK 74
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 59-150 2.08e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 39.47  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  59 SIIVEP-HVTAVWGKNVSLKCLIEVNETITqISWEKiHGKSTQTvavhhpqygfsvqgdyqGRVLFKNYSLNDATITLHN 137
Cdd:pfam13927   3 VITVSPsSVTVREGETVTLTCEATGSPPPT-ITWYK-NGEPISS-----------------GSTRSRSLSGSNSTLTISN 63

                          90
                  ....*....|...
gi 1907119219 138 IGFSDSGKYICKA 150
Cdd:pfam13927  64 VTRSDAGTYTCVA 76
IgV_EVA1 cd05880
Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are ...
 66-149 2.15e-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: 40.58  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  66 VTAVWGKNVSLKCLIE----VNETITqISW--EKIHGKSTQTVAVHHPQYGFSVQGDYQGRVLFK-NYSLNDATITLHNI 138
Cdd:cd05880     9 VEAVNGTDVRLKCTFSssapIGDTLV-ITWnfRPLDGGREESVFYYHKRPYPPPDGRFKGRVVWDgNIMRRDASILIWQL 87

                          90
                  ....*....|.
gi 1907119219 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 3.35e-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: 39.26  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  66 VTAVWGKNVSLKCLIEVNETiTQISWEKihgKSTQTVavhhpqYGFSVQGDYQGRVLFKNYSLNDATITLHNIGFSDSGK 145
Cdd:cd05882     7 ETVAVGGTVTLKCGVKEHDN-SSLQWSN---TAQQTL------YFGEKRALRDNRIQLVKSTPTELIISISNVQLSDEGE 76

                          90
                  ....*....|....*....
gi 1907119219 146 YICKAVTFPLGNAQSSTTV 164
Cdd:cd05882    77 YTCSIFTMPVRTAKATVTV 95
IgI_2_KIRREL3-like cd05759
Second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, and similar ...
 179-265 3.46e-04

Second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (Neph1), Kirrel2 (Neph3), and Drosophila RST (irregular chiasm C-roughest) protein. These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development.


Pssm-ID: 409416  Cd Length: 98  Bit Score: 39.36  E-value: 3.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219 179 DSLIDGGNET--VAAV-----CVAATGKPVAQIDWEGDLGEME---SSTTSFPNET-ATIVSQYKLFPTRFARGRRITCV 247
Cdd:cd05759     1 DPVIEGGPVIslQAGVpynltCRARGAKPAAEIIWFRDGEQLEgavYSKELLKDGKrETTVSTLLITPSDLDTGRTFTCR 80

                          90
                  ....*....|....*...
gi 1907119219 248 VKHPALEKDIRYSFILDI 265
Cdd:cd05759    81 ARNEAIPNGKETSITLDV 98
I-set pfam07679
Immunoglobulin I-set domain;
59-166 3.96e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 39.16  E-value: 3.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  59 SIIVEPH-VTAVWGKNVSLKCLIEVNETItQISWEKihGKSTQTVAVHHpqygfsvqgdyqgRVLFKNyslNDATITLHN 137
Cdd:pfam07679   2 KFTQKPKdVEVQEGESARFTCTVTGTPDP-EVSWFK--DGQPLRSSDRF-------------KVTYEG---GTYTLTISN 62

                          90       100
                  ....*....|....*....|....*....
gi 1907119219 138 IGFSDSGKYICKAvTFPLGNAQSSTTVTV 166
Cdd:pfam07679  63 VQPDDSGKYTCVA-TNSAGEAEASAELTV 90
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 62-164 5.31e-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: 38.72  E-value: 5.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  62 VEPHVTAVW-GKNVSLKCLIEVNETITQISWEKIHGKSTQTVAVHHpqygfsvqgdyqgrvlfKNYSLNDATITLHNIGF 140
Cdd:pfam00047   1 SAPPTVTVLeGDSATLTCSASTGSPGPDVTWSKEGGTLIESLKVKH-----------------DNGRTTQSSLLISNVTK 63

                          90       100
                  ....*....|....*....|....
gi 1907119219 141 SDSGKYICKaVTFPLGNAQSSTTV 164
Cdd:pfam00047  64 EDAGTYTCV-VNNPGGSATLSTSL 86
IgV_1_Necl_like cd05717
First (N-terminal) immunoglobulin (Ig)-like domain of the nectin-like molecules; member of the ...
 65-166 6.19e-04

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: 38.65  E-value: 6.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  65 HVTAVWGKNVSLKCLIEVNETiTQISWEKIHGkstQTVAVhhpqygfsvqGDYQG----RVLFKNYSLNDATITLHNIGF 140
Cdd:cd05717     5 DVTVVEGETLTLKCQVSLRDD-SSLQWLNPNG---QTIYF----------NDKRAlrdsRYQLLNHSASELSISVSNVTL 70

                          90       100
                  ....*....|....*....|....*.
gi 1907119219 141 SDSGKYICKAVTFPLgnAQSSTTVTV 166
Cdd:cd05717    71 SDEGVYTCLHYTDPV--STKKVTVTV 94
IGv smart00406
Immunoglobulin V-Type;
73-149 8.54e-04

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 37.75  E-value: 8.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219   73 NVSLKCLIEVNE-TITQISW-EKIHGKSTQTVAVHHPQYGFSVQGDYQGRVLF-KNYSLNDATITLHNIGFSDSGKYICK 149
Cdd:smart00406   1 SVTLSCKFSGSTfSSYYVSWvRQPPGKGLEWLGYIGSNGSSYYQESYKGRFTIsKDTSKNDVSLTISNLRVEDTGTYYCA 80
IgI_2_Necl-2 cd05883
Second immunoglobulin (Ig)-like domain of nectin-like molecule 2 (Necl-2); member of the I-set ...
 167-257 9.49e-04

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: 38.36  E-value: 9.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219 167 LVEPTVSLIKGPDSLIDGGNEtVAAVCVAATGKPVAQIDWEGDLGEM--ESSTTSFPNETATIVSQYKLFPTRFARGRRI 244
Cdd:cd05883     1 LVPPRNLVIDIQKDTAVEGEE-IELNCTAMASKPAATIRWFKGNKELtgKSEVEEWYSRMFTVTSQLMLKVTKEDDGVPV 79

                          90
                  ....*....|...
gi 1907119219 245 TCVVKHPALeKDI 257
Cdd:cd05883    80 ICLVDHPAV-KDL 91
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 287-342 9.90e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 37.55  E-value: 9.90e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907119219 287 VNLKCNADANPPPfkSVWSRLDGQWPDGLLASDNTLHF------VHPLTVNYSGVYVCKVSN 342
Cdd:pfam13927  19 VTLTCEATGSPPP--TITWYKNGEPISSGSTRSRSLSGsnstltISNVTRSDAGTYTCVASN 78
Ig_Aggrecan_like cd05878
Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core ...
 64-172 1.63e-03

Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core protein (CSPG); The members here are composed of the immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core proteins (CSPGs). Included in this group are the Ig domains of other CSPGs: versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. 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: 409462  Cd Length: 125  Bit Score: 37.98  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  64 PHVTAVWGKNVSLKCLIEVNETIT---------QISWEKIH--GKSTQTVAVHHPQYG-FSVQGDYQGRVLFKNY--SLN 129
Cdd:cd05878     5 SPVRVLLGTSVTLPCYFIDPPHPVtpstaplapRIKWSKVSvdGKKEKEVVLLVATEGrVRVNSAYQGRVSLPNYpaIPS 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1907119219 130 DATITLHNIGFSDSGKYICKAVTfplGNAQSSTTVTVLVEPTV 172
Cdd:cd05878    85 DATLEVQSLRASDSGLYRCEVMH---GIEDSQDTVELVVKGVV 124
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 287-346 2.20e-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: 36.79  E-value: 2.20e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907119219 287 VNLKCNADANPPPFKSVWSRLDGQWPDGLLA-------SDNTLHFVhPLTVNYSGVYVCKVSNSLGQ 346
Cdd:pfam00047  14 ATLTCSASTGSPGPDVTWSKEGGTLIESLKVkhdngrtTQSSLLIS-NVTKEDAGTYTCVVNNPGGS 79
I-set pfam07679
Immunoglobulin I-set domain;
287-348 2.23e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 36.85  E-value: 2.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907119219 287 VNLKCNADANPPPfKSVWSRlDGQwpdgLLASDNTLHF----------VHPLTVNYSGVYVCKVSNSLGQRS 348
Cdd:pfam07679  18 ARFTCTVTGTPDP-EVSWFK-DGQ----PLRSSDRFKVtyeggtytltISNVQPDDSGKYTCVATNSAGEAE 83
IgC1_Tapasin_R cd05771
Tapasin-R immunoglobulin-like domain; member of the C1-set of Ig superfamily (IgSF) domains; ...
 224-260 2.36e-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: 37.09  E-value: 2.36e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907119219 224 TATIVSQYKLFPTRFARGRRITCVVKHPALEKDIRYS 260
Cdd:cd05771    64 TYSISSYLTLEPGTENRGATYTCRVTHVSLEEPLSVS 100
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 71-166 3.46e-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: 36.93  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  71 GKNVSLKCLIEVNETITQISWEKIHGKSTQTVAVHHPQYGFSVQGDYQGRVLFKNYSLNDATITLHNIGFSDSGKYICKA 150
Cdd:cd00099    13 GESVTLSCEVSSSFSSTYIYWYRQKPGQGPEFLIYLSSSKGKTKGGVPGRFSGSRDGTSSFSLTISNLQPEDSGTYYCAV 92

                          90
                  ....*....|....*....
gi 1907119219 151 VTFPLGNAQ---SSTTVTV 166
Cdd:cd00099    93 SESGGTDKLtfgSGTRLTV 111
IgV_1_Necl-2 cd05881
First (N-terminal) immunoglobulin (Ig)-like domain of nectin-like molecule 2; member of the ...
 120-166 3.93e-03

First (N-terminal) immunoglobulin (Ig)-like domain of nectin-like molecule 2; 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-2, Necl-2 (also known as cell adhesion molecule 1 (CADM1), SynCAM1, IGSF4A, Tslc1, sgIGSF, and RA175). 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-2 has Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-2 is expressed in a wide variety of tissues and is a putative tumour suppressor gene, which is downregulated in aggressive neuroblastoma.


Pssm-ID: 409465  Cd Length: 94  Bit Score: 36.52  E-value: 3.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907119219 120 RVLFKNYSLNDATITLHNIGFSDSGKYICKAVTFPlgNAQSSTTVTV 166
Cdd:cd05881    50 RFQLVNFSSSELRVSLTNVSISDEGRYFCQLYTDP--PQEAYTTITV 94
IgC2_CEACAM5-like cd20948
Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell ...
 288-352 5.11e-03

Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell adhesion molecule 5 (CEACAM5) and similar domains; member of the C2-set IgSF domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell adhesion molecule 5 (CEACAM5) and similar domains. The CEA family is a group of anchored or secreted glycoproteins, expressed by epithelial cells, leukocytes, endothelial cells and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. Carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), also known as CD66e (Cluster of Differentiation 66e), is a cell surface glycoprotein that plays a role in cell adhesion, intracellular signaling and tumor progression. Diseases associated with CEACAM5 include lung cancer and rectum cancer. 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. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409540  Cd Length: 76  Bit Score: 35.55  E-value: 5.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907119219 288 NLKCNADANPPPFKSvWSrldgqWPDGLLASDNTLhFVHPLTVNYSGVYVCKVSNSLGQRSDQKV 352
Cdd:cd20948    14 NLSCHAASNPPAQYS-WT-----INGTFQTSSQEL-FLPAITENNEGTYTCSAHNSLTGKNISLV 71
Ig_CSPGs_LP_like cd05714
Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage ...
 63-151 5.65e-03

Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in chondroitin sulfate proteoglycans (CSPGs) and human cartilage link protein (LP). Included in this group are the CSPGs aggrecan, versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. There is considerable evidence that HA-binding CSPGs are involved in developmental processes in the central nervous system. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409379  Cd Length: 123  Bit Score: 36.42  E-value: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  63 EPHVTAVWGKNVSLKCLIEVNETIT-------QISWEKIHGKSTQT------VAVHHPQYgfsVQGDYQGRVLFKNY--S 127
Cdd:cd05714     4 SAKVFSHLGGNVTLPCKFYRDPTAFgsgihkiRIKWTKLTSDSGYLkevdvlVAMGNVVY---HKKTYGGRVSVPLKpgS 80

                          90       100
                  ....*....|....*....|....
gi 1907119219 128 LNDATITLHNIGFSDSGKYICKAV 151
Cdd:cd05714    81 DSDASLVITDLTASDYGLYRCEVI 104
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 128-166 6.03e-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: 35.51  E-value: 6.03e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907119219 128 LNDATITLHNIGFSDSGKYICKAVTFpLGNAQSSTTVTV 166
Cdd:cd04969    52 LPDGSLKIKNVTKSDEGKYTCFAVNF-FGKANSTGSLSV 89
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
 115-148 8.04e-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: 35.87  E-value: 8.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1907119219 115 GDYQGRVLFK-NYSLNDATITLHNIGFSDSGKYIC 148
Cdd:cd05715    64 GRFKDRVSWAgNPSKKDASIVISNLQFSDNGTYTC 98
IgV_MOG_like cd05713
Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here ...
 64-148 9.90e-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: 35.63  E-value: 9.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119219  64 PHVTAVWGKNVSLKCLI--EVNETITQISWekIHGKSTQtvAVHHPQYG---FSVQ-GDYQGRVLFKNYSLNDATITL-- 135
Cdd:cd05713     8 EPILALVGEDAELPCHLspKMSAEHMEVRW--FRSQFSP--VVHLYRDGqdqEEEQmPEYRGRTELLKDAIAEGSVALri 83

                          90
                  ....*....|...
gi 1907119219 136 HNIGFSDSGKYIC 148
Cdd:cd05713    84 HNVRPSDEGQYTC 96
 
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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