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Conserved domains on  [gi|157832102|pdb|1NEU|A]
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Chain A, MYELIN P0 PROTEIN

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 ...
 1-117 3.40e-80

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 cd05879:

Pssm-ID: 472250  Cd Length: 117  Bit Score: 230.92  E-value: 3.40e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NEU_A        1 IVVYTDREVYGAVGSQVTLHCSFWSSEWVSDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTFKERIQWVGDPSWKD 80
Cdd:cd05879   1 IVVYTDREVYGTVGSDVTLSCSFWSSEWISDDISFTWHYQPDGSRDAISIFHYGKGQPYIDNVGPFKERIEWVGNPSRKD 80

                        90       100       110
                ....*....|....*....|....*....|....*..
1NEU_A       81 GSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYV 117
Cdd:cd05879  81 GSIVIHNLDYTDNGTFTCDVKNPPDIVGKSSQVTLYV 117
 
Name Accession Description Interval E-value
IgV_P0 cd05879
Immunoglobulin (Ig)-like domain of protein zero (P0); The members here are composed of the ...
 1-117 3.40e-80

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: 230.92  E-value: 3.40e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NEU_A        1 IVVYTDREVYGAVGSQVTLHCSFWSSEWVSDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTFKERIQWVGDPSWKD 80
Cdd:cd05879   1 IVVYTDREVYGTVGSDVTLSCSFWSSEWISDDISFTWHYQPDGSRDAISIFHYGKGQPYIDNVGPFKERIEWVGNPSRKD 80

                        90       100       110
                ....*....|....*....|....*....|....*..
1NEU_A       81 GSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYV 117
Cdd:cd05879  81 GSIVIHNLDYTDNGTFTCDVKNPPDIVGKSSQVTLYV 117
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 4-117 3.40e-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: 86.36  E-value: 3.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NEU_A          4 YTDREVYGAVGSQVTLHCSFWSSeWVSDDISFTWRYQPEGGRDAISIFHYAKGQPyideVGTFKERIQWVGDPSWKDGSI 83
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSS-MSEASTSVYWYRQPPGKGPTFLIAYYSNGSE----EGVKKGRFSGRGDPSNGDGSL 75

                          90       100       110
                  ....*....|....*....|....*....|....
1NEU_A         84 VIHNLDYSDNGTFTCDVkNPPDIVGKTSQVTLYV 117
Cdd:pfam07686  76 TIQNLTLSDSGTYTCAV-IPSGEGVFGKGTRLTV 108
IGv smart00406
Immunoglobulin V-Type;
17-100 1.65e-17

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 71.26  E-value: 1.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NEU_A          17 VTLHCSFWSSEWVsdDISFTWRYQPEGGRDAISIFHYAKGQPYIDEvgTFKERIQWVGDPSWKDGSIVIHNLDYSDNGTF 96
Cdd:smart00406   2 VTLSCKFSGSTFS--SYYVSWVRQPPGKGLEWLGYIGSNGSSYYQE--SYKGRFTISKDTSKNDVSLTISNLRVEDTGTY 77


                   ....
1NEU_A          97 TCDV 100
Cdd:smart00406  78 YCAV 81
 
Name Accession Description Interval E-value
IgV_P0 cd05879
Immunoglobulin (Ig)-like domain of protein zero (P0); The members here are composed of the ...
 1-117 3.40e-80

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: 230.92  E-value: 3.40e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NEU_A        1 IVVYTDREVYGAVGSQVTLHCSFWSSEWVSDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTFKERIQWVGDPSWKD 80
Cdd:cd05879   1 IVVYTDREVYGTVGSDVTLSCSFWSSEWISDDISFTWHYQPDGSRDAISIFHYGKGQPYIDNVGPFKERIEWVGNPSRKD 80

                        90       100       110
                ....*....|....*....|....*....|....*..
1NEU_A       81 GSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYV 117
Cdd:cd05879  81 GSIVIHNLDYTDNGTFTCDVKNPPDIVGKSSQVTLYV 117
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
 1-117 3.96e-68

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: 200.73  E-value: 3.96e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NEU_A        1 IVVYTDREVYGAVGSQVTLHCSFWSSEWVSDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTFKERIQWVGDPSWKD 80
Cdd:cd05715   1 MEVYTPRELNVLNGSDVRLTCTFTSCYTVGDAFSVTWTYQPEGGNTTESMFHYSKGKPYILKVGRFKDRVSWAGNPSKKD 80

                        90       100       110
                ....*....|....*....|....*....|....*..
1NEU_A       81 GSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYV 117
Cdd:cd05715  81 ASIVISNLQFSDNGTYTCDVKNPPDIVGGHGEIRLYV 117
IgV_EVA1 cd05880
Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are ...
 1-117 9.48e-33

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: 111.07  E-value: 9.48e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NEU_A        1 IVVYTDREVYGAVGSQVTLHCSFWSSEWVSDDISFTWRYQPEGGRDAISIFHYAKgQPYIDEVGTFKERIQWVGDPSWKD 80
Cdd:cd05880   1 IEVYTSKEVEAVNGTDVRLKCTFSSSAPIGDTLVITWNFRPLDGGREESVFYYHK-RPYPPPDGRFKGRVVWDGNIMRRD 79

                        90       100       110
                ....*....|....*....|....*....|....*..
1NEU_A       81 GSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYV 117
Cdd:cd05880  80 ASILIWQLQPTDNGTYTCQVKNPPDVHGPIGEIRLRV 116
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 4-117 3.40e-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: 86.36  E-value: 3.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NEU_A          4 YTDREVYGAVGSQVTLHCSFWSSeWVSDDISFTWRYQPEGGRDAISIFHYAKGQPyideVGTFKERIQWVGDPSWKDGSI 83
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSS-MSEASTSVYWYRQPPGKGPTFLIAYYSNGSE----EGVKKGRFSGRGDPSNGDGSL 75

                          90       100       110
                  ....*....|....*....|....*....|....
1NEU_A         84 VIHNLDYSDNGTFTCDVkNPPDIVGKTSQVTLYV 117
Cdd:pfam07686  76 TIQNLTLSDSGTYTCAV-IPSGEGVFGKGTRLTV 108
IGv smart00406
Immunoglobulin V-Type;
17-100 1.65e-17

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 71.26  E-value: 1.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NEU_A          17 VTLHCSFWSSEWVsdDISFTWRYQPEGGRDAISIFHYAKGQPYIDEvgTFKERIQWVGDPSWKDGSIVIHNLDYSDNGTF 96
Cdd:smart00406   2 VTLSCKFSGSTFS--SYYVSWVRQPPGKGLEWLGYIGSNGSSYYQE--SYKGRFTISKDTSKNDVSLTISNLRVEDTGTY 77


                   ....
1NEU_A          97 TCDV 100
Cdd:smart00406  78 YCAV 81
IgV_1_Nectin-1_like cd05886
First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here ...
 2-118 4.33e-11

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: 55.74  E-value: 4.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NEU_A        2 VVYTDREVYGAVGSQVTLHCSFWSSEWVSDDISFTWRYQPEGGRDAISIFHYAKG----QPYIDEVgTFKeriqwvgDPS 77
Cdd:cd05886   2 TVQVNDSMSGFIGTDVVLHCSFANPLPSVKITQVTWQKSTNGSKQNVAIYNPSMGvsvlPPYRERV-TFL-------NPS 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
1NEU_A       78 WKDGSIVIHNLDYSDNGTFTCDVKNPPdIVGKTSQVTLYVF 118
Cdd:cd05886  74 FTDGTIRLSRLELEDEGVYICEFATFP-TGNRESQLNLTVM 113
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 1-117 2.28e-09

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: 51.29  E-value: 2.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NEU_A        1 IVVYTDREVYGAVGSQVTLHCSFWSSEWVSddIS-FTWRYQPEGGRDAISIFHYAKGqpyIDEVGTFKERIQWVGDP-SW 78
Cdd:cd05718   1 QRVQVPTEVTGFLGGSVTLPCSLTSPGTTK--ITqVTWMKIGAGSSQNVAVFHPQYG---PSVPNPYAERVEFLAARlGL 75

                        90       100       110
                ....*....|....*....|....*....|....*....
1NEU_A       79 KDGSIVIHNLDYSDNGTFTCDVKNPPdivGKTSQVTLYV 117
Cdd:cd05718  76 RNATLRIRNLRVEDEGNYICEFATFP---QGNRQGTTWL 111
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 12-114 3.09e-09

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: 50.91  E-value: 3.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NEU_A       12 AVGSQVTLHC--SFWSSEWVSDDISftWRYQPEGGRDAISIFhYAKGQPYIDEVGTFKERIQWVGDPSWKDGSIVIHNLD 89
Cdd:cd20960  13 VAGENVTLPChhQLGLEDQGTLDIE--WLLLPSDKVEKVVIT-YSGDRVYNHYYPALKGRVAFTSNDLSGDASLNISNLK 89

                        90       100
                ....*....|....*....|....*
1NEU_A       90 YSDNGTFTCDVKNPPDIVGKTSQVT 114
Cdd:cd20960  90 LSDTGTYQCKVKKAPGYAWSKITLI 114
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 7-117 4.55e-08

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: 4.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NEU_A           7 REVYGAVGSQVTLHCSFWSSEwvsdDISFTWRYQPeggrdaisifhyakgqpyiDEVGTFKERIQWVGDPSwkDGSIVIH 86
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSP----PPEVTWYKQG-------------------GKLLAESGRFSVSRSGS--TSTLTIS 56

                           90       100       110
                   ....*....|....*....|....*....|.
1NEU_A          87 NLDYSDNGTFTCDVKNppDIVGKTSQVTLYV 117
Cdd:smart00410  57 NVTPEDSGTYTCAATN--SSGSASSGTTLTV 85
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 1-104 1.92e-07

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: 46.03  E-value: 1.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NEU_A        1 IVVYTDREVYGAVGSQVTLHCSFWSSEWVSDDISFTWRYQPEGGrdAISIFHYAKGqPYIDEvgtfKERIQWVG---DPS 77
Cdd:cd20989   1 VRVQVPPEVRGFLGGSVTLPCHLLPPNMVTHVSQVTWQRHDEHG--SVAVFHPKQG-PSFPE----SERLSFVAarlGAE 73

                        90       100
                ....*....|....*....|....*..
1NEU_A       78 WKDGSIVIHNLDYSDNGTFTCDVKNPP 104
Cdd:cd20989  74 LRNASLAMFGLRVEDEGNYTCEFATFP 100
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 1-115 3.52e-04

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: 37.32  E-value: 3.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NEU_A        1 IVVYTDREVygAVGSQVTLHCSFWSSEWVsddISFTWRYQPEGGRDAISIFHYAKGQPYIdevGTFKERIQwVGDPSWKD 80
Cdd:cd05846   2 VVHTGDTRA--VLGGNATLSCNLTLPEEV---LQVTWQKIKASSPENIVTYSKKYGVKIQ---PSYVRRIS-FTSSGLNS 72

                        90       100       110
                ....*....|....*....|....*....|....*.
1NEU_A       81 GSIVIHNLDYSDNGTFTCDVKNPPD-IVGKTSQVTL 115
Cdd:cd05846  73 TSITIWNVTLEDEGCYKCLFNTFPDgIKSGTACLTV 108
IgV_1_CD4 cd07690
First immunoglobulin (Ig) domain of Cluster of Differentiation (CD) 4; member of the V-set of ...
 9-117 3.19e-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: 34.45  E-value: 3.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NEU_A        9 VYGAVGSQVTLHCSfwSSEWVSddISFTWRYQpeggrDAISIFHYakgQPYIDEVGTFKERIQWVGDPS-WKDGS--IVI 85
Cdd:cd07690   4 VLGKKGDTAELPCT--ASQKKS--IQFHWKNS-----NQIKILGN---QGSFLTKGPSKLNDRADSRRNlWDQGSfpLII 71

                        90       100       110
                ....*....|....*....|....*....|..
1NEU_A       86 HNLDYSDNGTFTCDVKNppdivgKTSQVTLYV 117
Cdd:cd07690  72 KNLKIEDSDTYICEVED------KKEEVELLV 97
IgV_CEACAM_like cd05741
Immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion ...
 5-117 5.53e-03

Immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain in carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) and related 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. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions: it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two (D1, D4) or four (D1-D4) Ig-like domains on the cell surface. This family corresponds to the D1 Ig-like domain. Also belonging to this group is the N-terminal immunoglobulin (Ig)-like domain of the signaling lymphocyte activation molecule (SLAM) family, CD84-like family. The SLAM family is a group of immune-cell specific receptors that can regulate both adaptive and innate immune responses. SLAM family proteins are organized as an extracellular domain with having two or four Ig-like domains, a single transmembrane segment, and a cytoplasmic region having Tyr-based motifs. The extracellular domain is organized as a membrane-distal Ig variable (IgV) domain that is responsible for ligand recognition and a membrane-proximal truncated Ig constant-2 (IgC2) domain.


Pssm-ID: 409403  Cd Length: 102  Bit Score: 34.03  E-value: 5.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NEU_A        5 TDREVYGAVGSQVTLHcsfwssewVSD----DISFTWRYQPEGGRDaISIFHYAKGQPYIDEVGTFKERIQWvgdpsWKD 80
Cdd:cd05741   1 SSEQFYGAEGKNVLLL--------VPNlqtpLKSVSWYKGKQVSRN-DEIAEYENSSDEFRAGSAFSGREYI-----YTN 66

                        90       100       110
                ....*....|....*....|....*....|....*....
1NEU_A       81 GSIVIHNLDYSDNGTFTCDVknpPDIVGKTSQVT--LYV 117
Cdd:cd05741  67 GSLLIQNITLSDTGFYTLES---TNIGGKTESATfqLHV 102
 
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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