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Conserved domains on  [gi|4759066|ref|NP_004579|]
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sodium channel subunit beta-2 precursor [Homo sapiens]

Protein Classification

Ig_P0-like domain-containing protein( domain architecture ID 10146023)

Ig_P0-like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
 30-146 1.29e-69

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: 208.05  E-value: 1.29e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759066   30 MEVTVPATLNVLNGSDARLPCTFNSCYTVnHKQFSLNWTYQECN-NCSEEMFLQFRMKIINLKLERFQDRVEFSGNPSKY 108
Cdd:cd05715   1 MEVYTPRELNVLNGSDVRLTCTFTSCYTV-GDAFSVTWTYQPEGgNTTESMFHYSKGKPYILKVGRFKDRVSWAGNPSKK 79

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 4759066  109 DVSVMLRNVQPEDEGIYNCYIMNPPDRHRGHGKIHLQV 146
Cdd:cd05715  80 DASIVISNLQFSDNGTYTCDVKNPPDIVGGHGEIRLYV 117
 
Name Accession Description Interval E-value
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
 30-146 1.29e-69

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: 208.05  E-value: 1.29e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759066   30 MEVTVPATLNVLNGSDARLPCTFNSCYTVnHKQFSLNWTYQECN-NCSEEMFLQFRMKIINLKLERFQDRVEFSGNPSKY 108
Cdd:cd05715   1 MEVYTPRELNVLNGSDVRLTCTFTSCYTV-GDAFSVTWTYQPEGgNTTESMFHYSKGKPYILKVGRFKDRVSWAGNPSKK 79

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 4759066  109 DVSVMLRNVQPEDEGIYNCYIMNPPDRHRGHGKIHLQV 146
Cdd:cd05715  80 DASIVISNLQFSDNGTYTCDVKNPPDIVGGHGEIRLYV 117
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 33-147 2.07e-23

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: 90.21  E-value: 2.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759066     33 TVPATLNVLNGSDARLPCTFNScyTVNHKQFSLNWTYQECNNCSEEMFLQFRmkiINLKLERFQDRVEFSGNPSKYDVSV 112
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSS--SMSEASTSVYWYRQPPGKGPTFLIAYYS---NGSEEGVKKGRFSGRGDPSNGDGSL 75

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 4759066    113 MLRNVQPEDEGIYNCYiMNPPDRHRGHGKIHLQVL 147
Cdd:pfam07686  76 TIQNLTLSDSGTYTCA-VIPSGEGVFGKGTRLTVL 109
IGv smart00406
Immunoglobulin V-Type;
45-127 6.59e-08

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 48.53  E-value: 6.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759066      45 DARLPCTF----NSCYTVNhkqfslnWTYQECNNcSEEMFLQFRMKIINLKLERFQDRVEFSGNPSKYDVSVMLRNVQPE 120
Cdd:smart00406   1 SVTLSCKFsgstFSSYYVS-------WVRQPPGK-GLEWLGYIGSNGSSYYQESYKGRFTISKDTSKNDVSLTISNLRVE 72


                   ....*..
gi 4759066     121 DEGIYNC 127
Cdd:smart00406  73 DTGTYYC 79
 
Name Accession Description Interval E-value
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
 30-146 1.29e-69

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: 208.05  E-value: 1.29e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759066   30 MEVTVPATLNVLNGSDARLPCTFNSCYTVnHKQFSLNWTYQECN-NCSEEMFLQFRMKIINLKLERFQDRVEFSGNPSKY 108
Cdd:cd05715   1 MEVYTPRELNVLNGSDVRLTCTFTSCYTV-GDAFSVTWTYQPEGgNTTESMFHYSKGKPYILKVGRFKDRVSWAGNPSKK 79

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 4759066  109 DVSVMLRNVQPEDEGIYNCYIMNPPDRHRGHGKIHLQV 146
Cdd:cd05715  80 DASIVISNLQFSDNGTYTCDVKNPPDIVGGHGEIRLYV 117
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 33-147 2.07e-23

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: 90.21  E-value: 2.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759066     33 TVPATLNVLNGSDARLPCTFNScyTVNHKQFSLNWTYQECNNCSEEMFLQFRmkiINLKLERFQDRVEFSGNPSKYDVSV 112
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSS--SMSEASTSVYWYRQPPGKGPTFLIAYYS---NGSEEGVKKGRFSGRGDPSNGDGSL 75

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 4759066    113 MLRNVQPEDEGIYNCYiMNPPDRHRGHGKIHLQVL 147
Cdd:pfam07686  76 TIQNLTLSDSGTYTCA-VIPSGEGVFGKGTRLTVL 109
IgV_EVA1 cd05880
Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are ...
 30-146 7.55e-23

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: 88.73  E-value: 7.55e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759066   30 MEVTVPATLNVLNGSDARLPCTFNSCYTVNhKQFSLNWTYQECNNCSEEMFLQFRMKIINLKLERFQDRVEFSGNPSKYD 109
Cdd:cd05880   1 IEVYTSKEVEAVNGTDVRLKCTFSSSAPIG-DTLVITWNFRPLDGGREESVFYYHKRPYPPPDGRFKGRVVWDGNIMRRD 79

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 4759066  110 VSVMLRNVQPEDEGIYNCYIMNPPDRHRGHGKIHLQV 146
Cdd:cd05880  80 ASILIWQLQPTDNGTYTCQVKNPPDVHGPIGEIRLRV 116
IgV_P0 cd05879
Immunoglobulin (Ig)-like domain of protein zero (P0); The members here are composed of the ...
 30-146 3.55e-11

Immunoglobulin (Ig)-like domain of protein zero (P0); 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 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.


Pssm-ID: 409463  Cd Length: 117  Bit Score: 58.35  E-value: 3.55e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759066   30 MEVTVPATLNVLNGSDARLPCTFNSCYTVNhKQFSLNWTYQEcnNCSEEMFLQFRMK-----IINLKLerFQDRVEFSGN 104
Cdd:cd05879   1 IVVYTDREVYGTVGSDVTLSCSFWSSEWIS-DDISFTWHYQP--DGSRDAISIFHYGkgqpyIDNVGP--FKERIEWVGN 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 4759066  105 PSKYDVSVMLRNVQPEDEGIYNCYIMNPPDRHRGHGKIHLQV 146
Cdd:cd05879  76 PSRKDGSIVIHNLDYTDNGTFTCDVKNPPDIVGKSSQVTLYV 117
IGv smart00406
Immunoglobulin V-Type;
45-127 6.59e-08

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 48.53  E-value: 6.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759066      45 DARLPCTF----NSCYTVNhkqfslnWTYQECNNcSEEMFLQFRMKIINLKLERFQDRVEFSGNPSKYDVSVMLRNVQPE 120
Cdd:smart00406   1 SVTLSCKFsgstFSSYYVS-------WVRQPPGK-GLEWLGYIGSNGSSYYQESYKGRFTISKDTSKNDVSLTISNLRVE 72


                   ....*..
gi 4759066     121 DEGIYNC 127
Cdd:smart00406  73 DTGTYYC 79
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 35-146 1.14e-05

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 42.49  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759066      35 PATLNVLNGSDARLPCTFNSCYTVNhkqfsLNWTYQecnncseemflqfrmkiiNLKLERFQDRveFSGNPSKYDVSVML 114
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPE-----VTWYKQ------------------GGKLLAESGR--FSVSRSGSTSTLTI 55

                           90       100       110
                   ....*....|....*....|....*....|..
gi 4759066     115 RNVQPEDEGIYNCYIMNppDRHRGHGKIHLQV 146
Cdd:smart00410  56 SNVTPEDSGTYTCAATN--SSGSASSGTTLTV 85
IgV_B7-H3 cd20934
Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint ...
 40-129 1.87e-05

Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint molecules; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H3 also known as CD276), a member of the B7 family of immune checkpoint molecules. B7-H3 is an important immune checkpoint member of the B7 family and shares homology with other B7 ligands such as programmed death ligand 1 (PD-L1). The B7 family molecules interact with CD28 on T-cells to provide co-stimulatory signals that regulate T-cell activation and T-helper cell differentiation. Although B7-H3 has been shown to have both co-stimulatory and co-inhibitory effects on T-cell responses, the most current studies describe B7-H3 as a T cell inhibitor that promotes tumor aggressiveness and proliferation. Moreover, B7-H3 is highly overexpressed on a wide range of human solid cancers and promotes tumor growth, metastasis, and drug resistance. Thus, B7-H3 expression in tumors often correlates with both negative prognosis and poor clinical outcome in cancer patients. B7-H3 protein contains a predicted signal peptide, V- and C-like Ig domains (IgV and IgC), a transmembrane region, and an intracellular tail.


Pssm-ID: 409528  Cd Length: 115  Bit Score: 42.59  E-value: 1.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759066   40 VLNGSDARLPCTFNSCYTVNHKQFSLNW----TYQECNNCSEEMFLQFRMKiinlklERFQDRVE-FSGNPSKYDVSVML 114
Cdd:cd20934   9 ALVGTDATLRCSFSPEPGFSLAQLSVFWqltdTKQLVHSFTESQDQGRDQG------SAYANRTAlFPDLLAQGNASLRL 82

                        90
                ....*....|....*
gi 4759066  115 RNVQPEDEGIYNCYI 129
Cdd:cd20934  83 QRVRVADEGSYTCFV 97
IgV_1_Nectin-4_like cd05888
First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are ...
 43-133 1.96e-05

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: 42.19  E-value: 1.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759066   43 GSDARLPCTFNSCYTVNHKQFSlnWTyQECNNCSEEMFLQFRMKIINLKLERFQDRVEFSGNPSKYDVSVMLRNVQPEDE 122
Cdd:cd05888   8 GQDAKLPCFYRGDSGEQVGQVA--WA-RVDAGEGAQEIALLHSKYGLHVFPAYEGRVEQPPPPRPADGSVLLRNAVQADE 84

                        90
                ....*....|.
gi 4759066  123 GIYNCYIMNPP 133
Cdd:cd05888  85 GEYECRVSTFP 95
IgV_CD33 cd05712
Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic ...
 93-126 3.16e-05

Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic acid-binding Ig-like lectins); The members here are composed of the immunoglobulin (Ig) domain at the N-terminus of Cluster of Differentiation (CD) 33 and related Siglecs (sialic acid-binding Ig-like lectins). Siglec refers to a structurally related protein family that specifically recognizes sialic acid in oligosaccharide chains of glycoproteins and glycolipids. Siglecs are type I transmembrane proteins, organized as an extracellular module composed of Ig-like domains, an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains, followed by transmembrane and short cytoplasmic domains. Human Siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG, the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11.


Pssm-ID: 409377  Cd Length: 119  Bit Score: 41.99  E-value: 3.16e-05
                        10        20        30
                ....*....|....*....|....*....|....
gi 4759066   93 ERFQDRVEFSGNPSKYDVSVMLRNVQPEDEGIYN 126
Cdd:cd05712  63 ESTQGRFRLLGDPGKKNCSLSISDARPEDSGKYF 96
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
 43-129 8.06e-04

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.


Pssm-ID: 409512  Cd Length: 107  Bit Score: 37.75  E-value: 8.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759066   43 GSDARLPCTFNSCYTVnhkqfSLNWTYQECNNCSEEMFLQfrMKIINLKLERFQDRVE-FSGNPSKYDVSVMLRNVQPED 121
Cdd:cd16091  12 SEDCILPCSFTPGSEV-----VIHWYKQDSDIKVHSYYYG--KDQLESQDQRYRNRTSlFKDQISNGNASLLLRRVQLQD 84


                ....*...
gi 4759066  122 EGIYNCYI 129
Cdd:cd16091  85 EGRYKCYT 92
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 43-144 1.19e-03

Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins; The members here are composed of the Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins. CAR, which is encoded by human CXADR gene, is a cell adhesion molecule of the Immunoglobulin (Ig) superfamily. The CAR acts as a type I membrane receptor for group B1-B6 coxsackie viruses and subgroup C adenoviruses. For instance, adenovirus interacts with the coxsackievirus and adenovirus receptor to enter epithelial airway cells. The CAR is also shown to be involved in physiological processes such as neuronal and heart development, epithelial tight junction integrity, and tumor suppression. The CAR is a component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. The CAR is also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. The CAR is composed of one V-set and one C2-set Ig module, a single transmembrane helix, and an intracellular domain. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other


Pssm-ID: 409552  Cd Length: 114  Bit Score: 37.43  E-value: 1.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759066   43 GSDARLPCTFnSCYTVNHKQFSLNWTYQECNNCSEEMFLQFRMKIINLKLERFQDRVEFSGNPSKYDVSVMLRNVQPEDE 122
Cdd:cd20960  15 GENVTLPCHH-QLGLEDQGTLDIEWLLLPSDKVEKVVITYSGDRVYNHYYPALKGRVAFTSNDLSGDASLNISNLKLSDT 93

                        90       100
                ....*....|....*....|..
gi 4759066  123 GIYNCYIMNPPDRHRGHgkIHL 144
Cdd:cd20960  94 GTYQCKVKKAPGYAWSK--ITL 113
IgV_1_Nectin-1_like cd05886
First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here ...
 43-147 1.88e-03

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: 36.87  E-value: 1.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759066   43 GSDARLPCTF-NSCYTVNHKQFslnwTYQECNNCSEEMFLQFRMKIINLKLERFQDRVEFSgNPSKYDVSVMLRNVQPED 121
Cdd:cd05886  14 GTDVVLHCSFaNPLPSVKITQV----TWQKSTNGSKQNVAIYNPSMGVSVLPPYRERVTFL-NPSFTDGTIRLSRLELED 88

                        90       100
                ....*....|....*....|....*.
gi 4759066  122 EGIYNCYIMNPPDRHRgHGKIHLQVL 147
Cdd:cd05886  89 EGVYICEFATFPTGNR-ESQLNLTVM 113
IgV_L_kappa cd04980
Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are ...
 101-127 7.60e-03

Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, kappa type, variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains.


Pssm-ID: 409369  Cd Length: 106  Bit Score: 35.06  E-value: 7.60e-03
                        10        20
                ....*....|....*....|....*..
gi 4759066  101 FSGNPSKYDVSVMLRNVQPEDEGIYNC 127
Cdd:cd04980  62 FSGSGSGTDFTLTISSVEPEDAAVYYC 88
IgV_CD86 cd16087
Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86; The members here ...
 114-143 9.70e-03

Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86; The members here are composed of the immunoglobulin variable region (IgV) in the Cluster of Differentiation (CD) 86). Glycoproteins B7-1 (also known as cluster of differentiation (CD) 80) and B7-2 (also known as CD86) are expressed on antigen-presenting cells and deliver the co-stimulatory signal through CD28 and CTLA-4 (also known as CD152) on T cells. signaling through CD28 augments the T-cell response, whereas CTLA-4 signaling attenuates it. The CTLA-4 and B7-2 monomers are both two-layer beta-sandwiches that display the chain topology characteristic of the immunoglobulin variable (V-type) domains present in antigen receptors. The front and back sheets of B7-2 are composed of AGFCC'C" and BED strands, respectively. Members of the IgV family 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.


Pssm-ID: 409508  Cd Length: 108  Bit Score: 34.61  E-value: 9.70e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 4759066  114 LRNVQPEDEGIYNCYIMNppDRHRGHGKIH 143
Cdd:cd16087  72 LHNVQIKDQGTYQCFIHH--KSPKGLVLIH 99
 
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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