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Conserved domains on  [gi|28372555|ref|NP_777594|]
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sodium channel subunit beta-4 isoform 1 precursor [Homo sapiens]

Protein Classification

immunoglobulin domain-containing family protein( domain architecture ID 34076)

immunoglobulin (Ig) domain-containing family protein is a member of a large superfamily containing cell surface antigen receptors, co-receptors and co-stimulatory molecules of the immune system, molecules involved in antigen presentation to lymphocytes, cell adhesion molecules, certain cytokine receptors and intracellular muscle proteins; immunoglobulin domains are typically divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 31-151 1.27e-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 cd05715:

Pssm-ID: 472250  Cd Length: 117  Bit Score: 70.15  E-value: 1.27e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28372555  31 LEVSVGKatDIYAVNGTEILLPCTFSSCFGFED-LHFRWTY-----NSSDAFKILIEGTVKNEKSDPKvtlkdDDRITLV 104
Cdd:cd05715   1 MEVYTPR--ELNVLNGSDVRLTCTFTSCYTVGDaFSVTWTYqpeggNTTESMFHYSKGKPYILKVGRF-----KDRVSWA 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 28372555 105 GSTKEKmnNISIVLRDLEFSDTGKYTCHVKNPKEnNLQHHATIFLQV 151
Cdd:cd05715  74 GNPSKK--DASIVISNLQFSDNGTYTCDVKNPPD-IVGGHGEIRLYV 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 ...
 31-151 1.27e-15

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: 70.15  E-value: 1.27e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28372555  31 LEVSVGKatDIYAVNGTEILLPCTFSSCFGFED-LHFRWTY-----NSSDAFKILIEGTVKNEKSDPKvtlkdDDRITLV 104
Cdd:cd05715   1 MEVYTPR--ELNVLNGSDVRLTCTFTSCYTVGDaFSVTWTYqpeggNTTESMFHYSKGKPYILKVGRF-----KDRVSWA 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 28372555 105 GSTKEKmnNISIVLRDLEFSDTGKYTCHVKNPKEnNLQHHATIFLQV 151
Cdd:cd05715  74 GNPSKK--DASIVISNLQFSDNGTYTCDVKNPPD-IVGGHGEIRLYV 117
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 43-144 6.50e-09

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: 52.08  E-value: 6.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28372555    43 AVNGTEILLPCTFSSCFGFEDLHFRWTYNSSDA---FKILIEgtvknekSDPKVTLKDDDRITLVGSTKEkmNNISIVLR 119
Cdd:pfam07686   8 VALGGSVTLPCTYSSSMSEASTSVYWYRQPPGKgptFLIAYY-------SNGSEEGVKKGRFSGRGDPSN--GDGSLTIQ 78

                          90       100
                  ....*....|....*....|....*
gi 28372555   120 DLEFSDTGKYTCHVKNPKENNLQHH 144
Cdd:pfam07686  79 NLTLSDSGTYTCAVIPSGEGVFGKG 103
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 40-151 4.02e-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: 43.65  E-value: 4.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28372555     40 DIYAVNGTEILLPCTFSscfGFEDLHFRWTYNssdafkiliegtvkneksdPKVTLKDDDRITLVGSTkekmNNISIVLR 119
Cdd:smart00410   3 SVTVKEGESVTLSCEAS---GSPPPEVTWYKQ-------------------GGKLLAESGRFSVSRSG----STSTLTIS 56

                           90       100       110
                   ....*....|....*....|....*....|..
gi 28372555    120 DLEFSDTGKYTCHVKNpkeNNLQHHATIFLQV 151
Cdd:smart00410  57 NVTPEDSGTYTCAATN---SSGSASSGTTLTV 85
 
Name Accession Description Interval E-value
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
 31-151 1.27e-15

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: 70.15  E-value: 1.27e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28372555  31 LEVSVGKatDIYAVNGTEILLPCTFSSCFGFED-LHFRWTY-----NSSDAFKILIEGTVKNEKSDPKvtlkdDDRITLV 104
Cdd:cd05715   1 MEVYTPR--ELNVLNGSDVRLTCTFTSCYTVGDaFSVTWTYqpeggNTTESMFHYSKGKPYILKVGRF-----KDRVSWA 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 28372555 105 GSTKEKmnNISIVLRDLEFSDTGKYTCHVKNPKEnNLQHHATIFLQV 151
Cdd:cd05715  74 GNPSKK--DASIVISNLQFSDNGTYTCDVKNPPD-IVGGHGEIRLYV 117
IgV_EVA1 cd05880
Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are ...
 40-138 8.42e-11

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: 57.53  E-value: 8.42e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28372555  40 DIYAVNGTEILLPCTFSSCFGFED-LHFRWTYNSSDAFKiliEGTVKNEKSDPKVTLKD--DDRITLVGSTKEkmNNISI 116
Cdd:cd05880   8 EVEAVNGTDVRLKCTFSSSAPIGDtLVITWNFRPLDGGR---EESVFYYHKRPYPPPDGrfKGRVVWDGNIMR--RDASI 82

                        90       100
                ....*....|....*....|..
gi 28372555 117 VLRDLEFSDTGKYTCHVKNPKE 138
Cdd:cd05880  83 LIWQLQPTDNGTYTCQVKNPPD 104
IgV_P0 cd05879
Immunoglobulin (Ig)-like domain of protein zero (P0); The members here are composed of the ...
 40-151 1.20e-10

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: 57.19  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28372555  40 DIYAVNGTEILLPCTF-SSCFGFEDLHFRWTYN---SSDAFKILIEGtvKNEKS-DPKVTLKDddRITLVGSTKEKmnNI 114
Cdd:cd05879   8 EVYGTVGSDVTLSCSFwSSEWISDDISFTWHYQpdgSRDAISIFHYG--KGQPYiDNVGPFKE--RIEWVGNPSRK--DG 81

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 28372555 115 SIVLRDLEFSDTGKYTCHVKNPKEnNLQHHATIFLQV 151
Cdd:cd05879  82 SIVIHNLDYTDNGTFTCDVKNPPD-IVGKSSQVTLYV 117
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 43-144 6.50e-09

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: 52.08  E-value: 6.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28372555    43 AVNGTEILLPCTFSSCFGFEDLHFRWTYNSSDA---FKILIEgtvknekSDPKVTLKDDDRITLVGSTKEkmNNISIVLR 119
Cdd:pfam07686   8 VALGGSVTLPCTYSSSMSEASTSVYWYRQPPGKgptFLIAYY-------SNGSEEGVKKGRFSGRGDPSN--GDGSLTIQ 78

                          90       100
                  ....*....|....*....|....*
gi 28372555   120 DLEFSDTGKYTCHVKNPKENNLQHH 144
Cdd:pfam07686  79 NLTLSDSGTYTCAVIPSGEGVFGKG 103
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 40-151 4.02e-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: 43.65  E-value: 4.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28372555     40 DIYAVNGTEILLPCTFSscfGFEDLHFRWTYNssdafkiliegtvkneksdPKVTLKDDDRITLVGSTkekmNNISIVLR 119
Cdd:smart00410   3 SVTVKEGESVTLSCEAS---GSPPPEVTWYKQ-------------------GGKLLAESGRFSVSRSG----STSTLTIS 56

                           90       100       110
                   ....*....|....*....|....*....|..
gi 28372555    120 DLEFSDTGKYTCHVKNpkeNNLQHHATIFLQV 151
Cdd:smart00410  57 NVTPEDSGTYTCAATN---SSGSASSGTTLTV 85
IGv smart00406
Immunoglobulin V-Type;
51-131 1.60e-05

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 41.98  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28372555     51 LPCTFSScFGFEDLHFRWTYNSSD-AFKILIEGTVKNEKSDPKvtlKDDDRITLVGSTKEkmNNISIVLRDLEFSDTGKY 129
Cdd:smart00406   4 LSCKFSG-STFSSYYVSWVRQPPGkGLEWLGYIGSNGSSYYQE---SYKGRFTISKDTSK--NDVSLTISNLRVEDTGTY 77


                   ..
gi 28372555    130 TC 131
Cdd:smart00406  78 YC 79
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 39-135 2.31e-04

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: 39.36  E-value: 2.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28372555  39 TDIYAVNGTEILLPCTFSscFGFED---LHFRWTYNSSDAF-KILIE---GTVKNEKSDPkvtLKDddRITLVGSTKEkm 111
Cdd:cd20960   8 TEIKKVAGENVTLPCHHQ--LGLEDqgtLDIEWLLLPSDKVeKVVITysgDRVYNHYYPA---LKG--RVAFTSNDLS-- 78

                        90       100
                ....*....|....*....|....
gi 28372555 112 NNISIVLRDLEFSDTGKYTCHVKN 135
Cdd:cd20960  79 GDASLNISNLKLSDTGTYQCKVKK 102
IgV_CRIg cd16089
Immunoglobulin variable (IgV)-like domain in complement receptor of the immunoglobulin ...
 51-152 8.79e-04

Immunoglobulin variable (IgV)-like domain in complement receptor of the immunoglobulin superfamily (CRIg); The members here are composed of the immunoglobulin variable (IgV) region of the complement receptor of the immunoglobulin superfamily (CRIg). The N-terminal domain of CRIg (also known as Z39Ig and V-set and Ig domain-containing 4 (VSIG4) belongs to the IgV family of immunoglobulin-like domains while the C-terminal domain of CRIg belongs to the IgC family of immunoglobulin-like domains. Like all members of this family, the CRIg domain contains two beta-sheets: one composed of strands A', G, F, C, C' and C", and the other of strands B, E and D. The complement system is an important part of the innate immune system and is required for removal of pathogens from the bloodstream. After exposure to pathogens, the third component of the complement system, C3, is cleaved to C3b which, after recruitment of factor B, initiates formation of the alternative pathway convertases. CRIg, a complement receptor expressed on macrophages, binds to C3b and iC3b mediating phagocytosis of the particles. It is also a potent inhibitor of the alternative pathway convertases and a negative regulator of T cell activation. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 409510  Cd Length: 117  Bit Score: 37.89  E-value: 8.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28372555  51 LPCTFSSCFGFEDLHFRWT----YNSSDAFkiliegtVKNEKSDPKVTLKDDDRITLvgsTKEKMNNISIVLRDLEFSDT 126
Cdd:cd16089  19 LPCTYVPEEGYTQVLVKWLvqrdSDPVTIF-------LRDSSGDHIQQAKYRGRLEV---SKDTPGDVSLQLDTLEMDDR 88

                        90       100
                ....*....|....*....|....*...
gi 28372555 127 GKYTCHV--KNPKENNLQHHATIFLQVV 152
Cdd:cd16089  89 GHYTCQVtwQTPDGNLIVREKTTELRVQ 116
IgV_1_CD4 cd07690
First immunoglobulin (Ig) domain of Cluster of Differentiation (CD) 4; member of the V-set of ...
 32-138 2.28e-03

First immunoglobulin (Ig) domain of Cluster of Differentiation (CD) 4; member of the V-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig) domain of Cluster of Differentiation (CD) 4. CD4 and CD8 are the two primary co-receptor proteins found on the surface of T cells, and the presence of either CD4 or CD8 determines the function of the T cell. CD4 is found on helper T cells, where it is required for the binding of MHC (major histocompatibility complex) class II molecules, while CD8 is found on cytotoxic T cells, where it is required for the binding of MHC class I molecules. CD4 contains four immunoglobulin domains, with the first three included in this hierarchy. The fourth domain has a general Ig architecture, but has slight topological changes in the arrangement of beta strands relative to the other structures in this family and is not specifically included in the hierarchy.


Pssm-ID: 409487  Cd Length: 97  Bit Score: 36.37  E-value: 2.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28372555  32 EVSVGKAtdiyavnGTEILLPCTFSScfgFEDLHFRWTYnsSDAFKIL-------IEGTVK-NEKSDPKVTLKDDdritl 103
Cdd:cd07690   2 KVVLGKK-------GDTAELPCTASQ---KKSIQFHWKN--SNQIKILgnqgsflTKGPSKlNDRADSRRNLWDQ----- 64

                        90       100       110
                ....*....|....*....|....*....|....*
gi 28372555 104 vgstkekmNNISIVLRDLEFSDTGKYTCHVKNPKE 138
Cdd:cd07690  65 --------GSFPLIIKNLKIEDSDTYICEVEDKKE 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 90-145 2.46e-03

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: 35.77  E-value: 2.46e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 28372555  90 DPKVT-LKDDDRITL--VGSTKEKMNNISIVLRDLEFSDTGKYTCHVKNPKENNLQHHA 145
Cdd:cd00096  12 PPTITwYKNGKPLPPssRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
IgV_B7-H3 cd20934
Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint ...
 46-151 2.72e-03

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: 36.43  E-value: 2.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28372555  46 GTEILLPCTFSSCFGF--EDLHFRWTYNSSdafKILIEGTVKNEKSDPKVTLKDDDRITLVgSTKEKMNNISIVLRDLEF 123
Cdd:cd20934  12 GTDATLRCSFSPEPGFslAQLSVFWQLTDT---KQLVHSFTESQDQGRDQGSAYANRTALF-PDLLAQGNASLRLQRVRV 87

                        90       100       110
                ....*....|....*....|....*....|
gi 28372555 124 SDTGKYTCHVknpkenNLQHH--ATIFLQV 151
Cdd:cd20934  88 ADEGSYTCFV------SVQDFgsAAVSLQV 111
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 91-135 4.81e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 35.22  E-value: 4.81e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 28372555  91 PKVT-LKDDDRITLVGSTKEKMNNISIVLRDLEFSDTGKYTCHVKN 135
Cdd:cd05856  34 PDITwLKDNKPLTPPEIGENKKKKWTLSLKNLKPEDSGKYTCHVSN 79
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 39-133 5.27e-03

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: 35.76  E-value: 5.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28372555  39 TDIYAVNGTEILLPCTFSSCFGFEDLH---FRWTYNSSDAFK---ILIE-GTVKNEKSDPKvtlkddDRITLVGSTKekm 111
Cdd:cd05877   5 AKVFSHRGGNVTLPCRYHYEPELSAPRkirVKWTKLEVDYAKeedVLVAiGTRHKSYGSYQ------GRVFLRRADD--- 75

                        90       100
                ....*....|....*....|..
gi 28372555 112 NNISIVLRDLEFSDTGKYTCHV 133
Cdd:cd05877  76 LDASLVITDLRLEDYGRYRCEV 97
IgV_MOG_like cd05713
Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here ...
 41-151 6.90e-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: 35.24  E-value: 6.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28372555  41 IYAVNGTEILLPCTFSSCFGFEDLHFRWtYNSSDAFKILI--EGTVKNEKSDPKVTlkddDRITLVgstKEKMNNISIVL 118
Cdd:cd05713  10 ILALVGEDAELPCHLSPKMSAEHMEVRW-FRSQFSPVVHLyrDGQDQEEEQMPEYR----GRTELL---KDAIAEGSVAL 81

                        90       100       110
                ....*....|....*....|....*....|....*
gi 28372555 119 R--DLEFSDTGKYTCHVknpKENNLQHHATIFLQV 151
Cdd:cd05713  82 RihNVRPSDEGQYTCFF---RSGSFYEEATLELKV 113
 
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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