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Conserved domains on  [gi|569005301|ref|XP_006526526|]
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CD226 antigen isoform X4 [Mus musculus]

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
V-set super family cl46292
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
21-109 5.49e-07

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


The actual alignment was detected with superfamily member pfam07686:

Pssm-ID: 462230  Cd Length: 109  Bit Score: 46.68  E-value: 5.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005301   21 SDSYLSAEPGQDVTLTCQLPRTW--PVQQVIWEKVQP---HQVDILASCNLSQETRYTSKY-LRQT--RSNCSqgsmksi 92
Cdd:pfam07686   2 TPREVTVALGGSVTLPCTYSSSMseASTSVYWYRQPPgkgPTFLIAYYSNGSEEGVKKGRFsGRGDpsNGDGS------- 74
                          90
                  ....*....|....*..
gi 569005301   93 LIIPNAMAADSGLYRCR 109
Cdd:pfam07686  75 LTIQNLTLSDSGTYTCA 91
 
Name Accession Description Interval E-value
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
21-109 5.49e-07

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: 46.68  E-value: 5.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005301   21 SDSYLSAEPGQDVTLTCQLPRTW--PVQQVIWEKVQP---HQVDILASCNLSQETRYTSKY-LRQT--RSNCSqgsmksi 92
Cdd:pfam07686   2 TPREVTVALGGSVTLPCTYSSSMseASTSVYWYRQPPgkgPTFLIAYYSNGSEEGVKKGRFsGRGDpsNGDGS------- 74
                          90
                  ....*....|....*..
gi 569005301   93 LIIPNAMAADSGLYRCR 109
Cdd:pfam07686  75 LTIQNLTLSDSGTYTCA 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
23-121 5.88e-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: 43.26  E-value: 5.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005301    23 SYLSAEPGQDVTLTCQLPRTwPVQQVIWEKVQPHQvdilascnLSQETRYTSkylrqtrsncSQGSMKSILIIPNAMAAD 102
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGS-PPPEVTWYKQGGKL--------LAESGRFSV----------SRSGSTSTLTISNVTPED 62
                           90
                   ....*....|....*....
gi 569005301   103 SGLYRCRSEAITGKNKSFV 121
Cdd:smart00410  63 SGTYTCAATNSSGSASSGT 81
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
23-108 7.38e-05

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: 40.79  E-value: 7.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005301  23 SYLSAEPGQDVTLTCQLPRTWPVQQVIWEKVQPHQVDILASCNLSQETRYTSKYLRqtRSNCSQ-GSMKSILIIPNAMAA 101
Cdd:cd05846    6 GDTRAVLGGNATLSCNLTLPEEVLQVTWQKIKASSPENIVTYSKKYGVKIQPSYVR--RISFTSsGLNSTSITIWNVTLE 83

                 ....*..
gi 569005301 102 DSGLYRC 108
Cdd:cd05846   84 DEGCYKC 90
 
Name Accession Description Interval E-value
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
21-109 5.49e-07

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: 46.68  E-value: 5.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005301   21 SDSYLSAEPGQDVTLTCQLPRTW--PVQQVIWEKVQP---HQVDILASCNLSQETRYTSKY-LRQT--RSNCSqgsmksi 92
Cdd:pfam07686   2 TPREVTVALGGSVTLPCTYSSSMseASTSVYWYRQPPgkgPTFLIAYYSNGSEEGVKKGRFsGRGDpsNGDGS------- 74
                          90
                  ....*....|....*..
gi 569005301   93 LIIPNAMAADSGLYRCR 109
Cdd:pfam07686  75 LTIQNLTLSDSGTYTCA 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
23-121 5.88e-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: 43.26  E-value: 5.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005301    23 SYLSAEPGQDVTLTCQLPRTwPVQQVIWEKVQPHQvdilascnLSQETRYTSkylrqtrsncSQGSMKSILIIPNAMAAD 102
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGS-PPPEVTWYKQGGKL--------LAESGRFSV----------SRSGSTSTLTISNVTPED 62
                           90
                   ....*....|....*....
gi 569005301   103 SGLYRCRSEAITGKNKSFV 121
Cdd:smart00410  63 SGTYTCAATNSSGSASSGT 81
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
23-108 7.38e-05

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: 40.79  E-value: 7.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005301  23 SYLSAEPGQDVTLTCQLPRTWPVQQVIWEKVQPHQVDILASCNLSQETRYTSKYLRqtRSNCSQ-GSMKSILIIPNAMAA 101
Cdd:cd05846    6 GDTRAVLGGNATLSCNLTLPEEVLQVTWQKIKASSPENIVTYSKKYGVKIQPSYVR--RISFTSsGLNSTSITIWNVTLE 83

                 ....*..
gi 569005301 102 DSGLYRC 108
Cdd:cd05846   84 DEGCYKC 90
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
21-108 1.63e-04

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: 39.62  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005301  21 SDSYLSAEPGQDVTLTCQLPRTWPVQQVIWEKVQPHQ--------VDILASCNLSQETRYTSKylrqtrsncSQGSMKSI 92
Cdd:cd00099    4 SPRSLSVQEGESVTLSCEVSSSFSSTYIYWYRQKPGQgpefliylSSSKGKTKGGVPGRFSGS---------RDGTSSFS 74
                         90
                 ....*....|....*.
gi 569005301  93 LIIPNAMAADSGLYRC 108
Cdd:cd00099   75 LTISNLQPEDSGTYYC 90
IgV_pIgR_like cd05716
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The ...
25-108 3.22e-04

Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins. pIgR delivers dimeric IgA and pentameric IgM to mucosal secretions. Polymeric immunoglobulin (pIgs) are the first defense against pathogens and toxins. IgA and IgM can form polymers via an 18-residue extension at their C-termini referred to as the tailpiece. pIgR transports pIgs across mucosal epithelia into mucosal secretions. Human pIgR is a glycosylated type I transmembrane protein, comprised of a 620-residue extracellular region, a 23-residue transmembrane region, and a 103-residue cytoplasmic tail. The extracellular region contains five domains that share sequence similarity with Ig variable (v) regions. This group also contains the Ig-like extracellular domains of other receptors such as NK cell receptor Nkp44 and myeloid receptors, among others.


Pssm-ID: 409381  Cd Length: 100  Bit Score: 38.53  E-value: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005301  25 LSAEPGQDVTLTCQLPRTWPVQQVIWEKVQPHqvdilaSCNLSQETRYTSKYLRQT-RSNCSQGSMKSILIipNAMAADS 103
Cdd:cd05716    7 VTGVEGGSVTIQCPYPPKYASSRKYWCKWGSE------GCQTLVSSEGVVPGGRISlTDDPDNGVFTVTLN--QLRKEDA 78

                 ....*
gi 569005301 104 GLYRC 108
Cdd:cd05716   79 GWYWC 83
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
14-118 5.76e-04

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third 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. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 37.91  E-value: 5.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005301  14 SFEIAAPSDSYlsAEPGQDVTLTCqLPRTWPVQQVIWEKVQPHQVdilascnlSQETRYTSKylrqtrsncsqgsmkSIL 93
Cdd:cd04968    2 SIKVRFPADTY--ALKGQTVTLEC-FALGNPVPQIKWRKVDGSPS--------SQWEITTSE---------------PVL 55
                         90       100
                 ....*....|....*....|....*
gi 569005301  94 IIPNAMAADSGLYRCRSEAITGKNK 118
Cdd:cd04968   56 EIPNVQFEDEGTYECEAENSRGKDT 80
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
27-108 3.13e-03

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig 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: 409551  Cd Length: 94  Bit Score: 35.93  E-value: 3.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005301  27 AEPGQDVTLTCQLPRTWPVQQVIWEKV-QPHQVDILAScnLSQETRYTSkylrqtrsncsqgsmksILIIPNAMAADSGL 105
Cdd:cd20959   14 AQVGMRAQLHCGVPGGDLPLNIRWTLDgQPISDDLGIT--VSRLGRRSS-----------------ILSIDSLEASHAGN 74

                 ...
gi 569005301 106 YRC 108
Cdd:cd20959   75 YTC 77
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
26-109 4.16e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 35.23  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005301   26 SAEPGQDVTLTCQLpRTWPVQQVIWEKVQPHQVDilascnlsqetrytskylrQTRSNCSQGSMKSILIIPNAMAADSGL 105
Cdd:pfam13927  12 TVREGETVTLTCEA-TGSPPPTITWYKNGEPISS-------------------GSTRSRSLSGSNSTLTISNVTRSDAGT 71

                  ....
gi 569005301  106 YRCR 109
Cdd:pfam13927  72 YTCV 75
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
30-126 5.48e-03

Second 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 second 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 the 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, and 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, 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 Slit-2 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: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 35.07  E-value: 5.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005301  30 GQDVTLTCQLPRTWPVQQVIWEKV-QPhqvdilasCNLSQETRYTskylrqtrsnCSQGSmksiLIIPNAMAADSGLYRC 108
Cdd:cd05724   12 GEMAVLECSPPRGHPEPTVSWRKDgQP--------LNLDNERVRI----------VDDGN----LLIAEARKSDEGTYKC 69
                         90
                 ....*....|....*...
gi 569005301 109 RSEAITGKNKSFVIRLII 126
Cdd:cd05724   70 VATNMVGERESRAARLSV 87
IGv smart00406
Immunoglobulin V-Type;
32-108 8.91e-03

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 34.28  E-value: 8.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005301    32 DVTLTCQL-PRTWPVQQVIWEKVQP-HQVDILASCNLSQETRYTSKYlrQTRSNCSQGSMKSI--LIIPNAMAADSGLYR 107
Cdd:smart00406   1 SVTLSCKFsGSTFSSYYVSWVRQPPgKGLEWLGYIGSNGSSYYQESY--KGRFTISKDTSKNDvsLTISNLRVEDTGTYY 78

                   .
gi 569005301   108 C 108
Cdd:smart00406  79 C 79
 
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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