P30203 · CD6_HUMAN
- ProteinT-cell differentiation antigen CD6
- GeneCD6
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids668 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Contributes to signaling cascades triggered by activation of the TCR/CD3 complex (PubMed:24584089).
Functions as a costimulatory molecule; promotes T-cell activation and proliferation (PubMed:15294938, PubMed:16352806, PubMed:16914752).
Contributes to the formation and maturation of the immunological synapse (PubMed:15294938, PubMed:16352806).
Functions as a calcium-dependent pattern receptor that binds and aggregates both Gram-positive and Gram-negative bacteria. Binds both lipopolysaccharide (LPS) from Gram-negative bacteria and lipoteichoic acid from Gram-positive bacteria (PubMed:17601777).
LPS binding leads to the activation of signaling cascades and down-stream MAP kinases (PubMed:17601777).
Mediates activation of the inflammatory response and the secretion of pro-inflammatory cytokines in response to LPS (PubMed:17601777).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell surface | |
Cellular Component | extracellular region | |
Cellular Component | immunological synapse | |
Cellular Component | plasma membrane | |
Molecular Function | identical protein binding | |
Molecular Function | lipopolysaccharide binding | |
Molecular Function | lipoteichoic acid binding | |
Molecular Function | protein kinase binding | |
Biological Process | acute inflammatory response to antigenic stimulus | |
Biological Process | adaptive immune response | |
Biological Process | heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules | |
Biological Process | immunological synapse formation | |
Biological Process | innate immune response | |
Biological Process | lipopolysaccharide-mediated signaling pathway | |
Biological Process | positive regulation of cytokine production involved in inflammatory response | |
Biological Process | positive regulation of protein phosphorylation | |
Biological Process | positive regulation of T cell proliferation | |
Biological Process | response to lipopolysaccharide |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameT-cell differentiation antigen CD6
- Alternative names
- Cleaved into 1 chains
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP30203
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Soluble CD6
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 18-402 | Extracellular | ||||
Sequence: HPSPAPPDQLNTSSAESELWEPGERLPVRLTNGSSSCSGTVEVRLEASWEPACGALWDSRAAEAVCRALGCGGAEAASQLAPPTPELPPPPAAGNTSVAANATLAGAPALLCSGAEWRLCEVVEHACRSDGRRARVTCAENRALRLVDGGGACAGRVEMLEHGEWGSVCDDTWDLEDAHVVCRQLGCGWAVQALPGLHFTPGRGPIHRDQVNCSGAEAYLWDCPGLPGQHYCGHKEDAGAVCSEHQSWRLTGGADRCEGQVEVHFRGVWNTVCDSEWYPSEAKVLCQSLGCGTAVERPKGLPHSLSGRMYYSCNGEELTLSNCSWRFNNSNLCSQSLAARVLCSASRSLHNLSTPEVPASVQTVTIESSVTVKIENKESRELMLL | ||||||
Transmembrane | 403-423 | Helical | ||||
Sequence: IPSIVLGILLLGSLIFIAFIL | ||||||
Topological domain | 424-668 | Cytoplasmic | ||||
Sequence: LRIKGKYALPVMVNHQHLPTTIPAGSNSYQPVPITIPKEVFMLPIQVQAPPPEDSDSGSDSDYEHYDFSAQPPVALTTFYNSQRHRVTDEEVQQSRFQMPPLEEGLEELHASHIPTANPGHCITDPPSLGPQYHPRSNSESSTSSGEDYCNSPKSKLPPWNPQVFSSERSSFLEQPPNLELAGTQPAFSAGPPADDSSSTSSGEWYQNFQPPPQPPSEEQFGCPGSPSPQPDSTDNDDYDDISAA |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_059809 | 217 | in dbSNP:rs11230562 | |||
Sequence: T → M | ||||||
Natural variant | VAR_057202 | 225 | in dbSNP:rs11230563 | |||
Sequence: R → W | ||||||
Natural variant | VAR_060790 | 257 | in dbSNP:rs2074225 | |||
Sequence: A → V | ||||||
Natural variant | VAR_057203 | 271 | in dbSNP:rs12360861 | |||
Sequence: A → T | ||||||
Mutagenesis | 291 | Strongly reduces interaction with ALCAM. | ||||
Sequence: D → A | ||||||
Mutagenesis | 293 | Reduces interaction with ALCAM. | ||||
Sequence: E → A | ||||||
Mutagenesis | 295 | Abolishes interaction with ALCAM. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 298 | Nearly abolishes interaction with ALCAM. | ||||
Sequence: E → A | ||||||
Mutagenesis | 314 | Reduces interaction with ALCAM. | ||||
Sequence: R → A | ||||||
Mutagenesis | 327 | Nearly abolishes interaction with ALCAM. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 329 | Reduces interaction with ALCAM. | ||||
Sequence: S → A | ||||||
Mutagenesis | 346 | Strongly reduces interaction with ALCAM. | ||||
Sequence: N → A | ||||||
Mutagenesis | 349 | Reduces interaction with ALCAM. | ||||
Sequence: L → A | ||||||
Natural variant | VAR_057204 | 351 | adds an additional glycosylation site and impairs interaction with ALCAM; dbSNP:rs34974368 | |||
Sequence: S → N | ||||||
Mutagenesis | 352 | Reduces interaction with ALCAM. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 353 | Reduces interaction with ALCAM. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_057205 | 606 | in dbSNP:rs2074233 | |||
Sequence: G → S | ||||||
Mutagenesis | 662 | Reduces tyrosine phosphorylation. Reduces affinity for LCP2. Impairs activation of T-cells. | ||||
Sequence: Y → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 747 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MWLFFGITGLLTAALSG | ||||||
Chain | PRO_0000435133 | 18-? | Soluble CD6 | |||
Sequence: MWLFFGITGLLTAALSG | ||||||
Chain | PRO_0000033227 | 18-668 | T-cell differentiation antigen CD6 | |||
Sequence: HPSPAPPDQLNTSSAESELWEPGERLPVRLTNGSSSCSGTVEVRLEASWEPACGALWDSRAAEAVCRALGCGGAEAASQLAPPTPELPPPPAAGNTSVAANATLAGAPALLCSGAEWRLCEVVEHACRSDGRRARVTCAENRALRLVDGGGACAGRVEMLEHGEWGSVCDDTWDLEDAHVVCRQLGCGWAVQALPGLHFTPGRGPIHRDQVNCSGAEAYLWDCPGLPGQHYCGHKEDAGAVCSEHQSWRLTGGADRCEGQVEVHFRGVWNTVCDSEWYPSEAKVLCQSLGCGTAVERPKGLPHSLSGRMYYSCNGEELTLSNCSWRFNNSNLCSQSLAARVLCSASRSLHNLSTPEVPASVQTVTIESSVTVKIENKESRELMLLIPSIVLGILLLGSLIFIAFILLRIKGKYALPVMVNHQHLPTTIPAGSNSYQPVPITIPKEVFMLPIQVQAPPPEDSDSGSDSDYEHYDFSAQPPVALTTFYNSQRHRVTDEEVQQSRFQMPPLEEGLEELHASHIPTANPGHCITDPPSLGPQYHPRSNSESSTSSGEDYCNSPKSKLPPWNPQVFSSERSSFLEQPPNLELAGTQPAFSAGPPADDSSSTSSGEWYQNFQPPPQPPSEEQFGCPGSPSPQPDSTDNDDYDDISAA | ||||||
Glycosylation | 28 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 49 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 54↔88 | |||||
Sequence: CSGTVEVRLEASWEPACGALWDSRAAEAVCRALGC | ||||||
Disulfide bond | 70↔144 | |||||
Sequence: CGALWDSRAAEAVCRALGCGGAEAASQLAPPTPELPPPPAAGNTSVAANATLAGAPALLCSGAEWRLCEVVEHAC | ||||||
Disulfide bond | 83↔155 | |||||
Sequence: CRALGCGGAEAASQLAPPTPELPPPPAAGNTSVAANATLAGAPALLCSGAEWRLCEVVEHACRSDGRRARVTC | ||||||
Glycosylation | 112 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 118 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 129↔137 | |||||
Sequence: CSGAEWRLC | ||||||
Disulfide bond | 170↔204 | |||||
Sequence: CAGRVEMLEHGEWGSVCDDTWDLEDAHVVCRQLGC | ||||||
Disulfide bond | 186↔249 | |||||
Sequence: CDDTWDLEDAHVVCRQLGCGWAVQALPGLHFTPGRGPIHRDQVNCSGAEAYLWDCPGLPGQHYC | ||||||
Disulfide bond | 199↔259 | |||||
Sequence: CRQLGCGWAVQALPGLHFTPGRGPIHRDQVNCSGAEAYLWDCPGLPGQHYCGHKEDAGAVC | ||||||
Glycosylation | 229 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 230↔240 | |||||
Sequence: CSGAEAYLWDC | ||||||
Disulfide bond | 290↔350 | |||||
Sequence: CDSEWYPSEAKVLCQSLGCGTAVERPKGLPHSLSGRMYYSCNGEELTLSNCSWRFNNSNLC | ||||||
Disulfide bond | 303↔360 | |||||
Sequence: CQSLGCGTAVERPKGLPHSLSGRMYYSCNGEELTLSNCSWRFNNSNLCSQSLAARVLC | ||||||
Disulfide bond | 330↔340 | |||||
Sequence: CNGEELTLSNC | ||||||
Glycosylation | 339 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 345 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 368 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 662 | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected on peripheral blood T-cells (PubMed:15048703, PubMed:16352806).
Detected on natural killer (NK) cells (PubMed:16352806).
Soluble CD6 is detected in blood serum (at protein level) (PubMed:17601777).
Detected in spleen, thymus, appendix, lymph node and peripheral blood leukocytes (PubMed:9013954).
Expressed by thymocytes, mature T-cells, a subset of B-cells known as B-1 cells, and by some cells in the brain
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with the TCR/CD3 complex subunit CD3E (PubMed:15294938).
Interacts (via tyrosine phosphorylated C-terminus) with LCP2 (via SH2 domain) (PubMed:16914752).
Interacts with VAV1 (By similarity).
Interacts (via glycosylated extracellular domain) with LGALS1 and LGALS3 (PubMed:24945728).
Interaction with LGALS1 or LGALS3 inhibits interaction with ALCAM (PubMed:24945728).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P30203 | ALCAM Q13740 | 6 | EBI-2873748, EBI-1188108 | |
BINARY | P30203 | CD6 P30203 | 3 | EBI-2873748, EBI-2873748 | |
BINARY | P30203 | LCP2 Q13094 | 3 | EBI-2873748, EBI-346946 | |
BINARY | P30203 | LGALS1 P09382 | 2 | EBI-2873748, EBI-1048875 | |
BINARY | P30203 | LGALS3 P17931 | 2 | EBI-2873748, EBI-1170392 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 18-37 | Disordered | ||||
Sequence: HPSPAPPDQLNTSSAESELW | ||||||
Domain | 45-156 | SRCR 1 | ||||
Sequence: VRLTNGSSSCSGTVEVRLEASWEPACGALWDSRAAEAVCRALGCGGAEAASQLAPPTPELPPPPAAGNTSVAANATLAGAPALLCSGAEWRLCEVVEHACRSDGRRARVTCA | ||||||
Domain | 161-260 | SRCR 2 | ||||
Sequence: LRLVDGGGACAGRVEMLEHGEWGSVCDDTWDLEDAHVVCRQLGCGWAVQALPGLHFTPGRGPIHRDQVNCSGAEAYLWDCPGLPGQHYCGHKEDAGAVCS | ||||||
Domain | 265-361 | SRCR 3 | ||||
Sequence: WRLTGGADRCEGQVEVHFRGVWNTVCDSEWYPSEAKVLCQSLGCGTAVERPKGLPHSLSGRMYYSCNGEELTLSNCSWRFNNSNLCSQSLAARVLCS | ||||||
Region | 471-490 | Disordered | ||||
Sequence: QAPPPEDSDSGSDSDYEHYD | ||||||
Region | 537-668 | Disordered | ||||
Sequence: IPTANPGHCITDPPSLGPQYHPRSNSESSTSSGEDYCNSPKSKLPPWNPQVFSSERSSFLEQPPNLELAGTQPAFSAGPPADDSSSTSSGEWYQNFQPPPQPPSEEQFGCPGSPSPQPDSTDNDDYDDISAA | ||||||
Compositional bias | 554-601 | Polar residues | ||||
Sequence: PQYHPRSNSESSTSSGEDYCNSPKSKLPPWNPQVFSSERSSFLEQPPN | ||||||
Compositional bias | 614-631 | Polar residues | ||||
Sequence: GPPADDSSSTSSGEWYQN |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 7 isoforms produced by Alternative splicing.
P30203-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameCD6A
- Length668
- Mass (Da)71,801
- Last updated2009-12-15 v3
- Checksum59E6790E77FFBC42
P30203-2
- NameCD6B
P30203-3
- NameCD6C
P30203-4
- NameCD6D
P30203-5
- NameCD6E
P30203-6
- Name6
- SynonymsCD6deltaD3Ex6
- NoteLacks the third SRCR domain and doesn't bind ALCAM/CD166. Doesn't localize to the immunological synapse.
- Differences from canonical
- 261-383: Missing
P30203-7
- Name7
- SynonymsCD6deltaD3
- NoteLacks the third SRCR domain and doesn't bind ALCAM/CD166. Doesn't localize to the immunological synapse. Constitutes the only expressed species in a small percentage of T-cells.
- Differences from canonical
- 259-359: Missing
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 47 | in Ref. 4; ABH04237 | ||||
Sequence: L → R | ||||||
Alternative sequence | VSP_054245 | 259-359 | in isoform 7 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_054246 | 261-383 | in isoform 6 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_006221 | 431-462 | in isoform CD6B, isoform CD6C and isoform CD6D | |||
Sequence: Missing | ||||||
Sequence conflict | 463-468 | in Ref. 3; CAA43306 | ||||
Sequence: VFMLPI → GPGPAP | ||||||
Alternative sequence | VSP_006222 | 463-504 | in isoform CD6C and isoform CD6E | |||
Sequence: VFMLPIQVQAPPPEDSDSGSDSDYEHYDFSAQPPVALTTFYN → D | ||||||
Compositional bias | 554-601 | Polar residues | ||||
Sequence: PQYHPRSNSESSTSSGEDYCNSPKSKLPPWNPQVFSSERSSFLEQPPN | ||||||
Alternative sequence | VSP_061447 | 613 | in isoform CD6B | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_006223 | 613-647 | in isoform CD6D and isoform CD6E | |||
Sequence: Missing | ||||||
Compositional bias | 614-631 | Polar residues | ||||
Sequence: GPPADDSSSTSSGEWYQN |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AH011243 EMBL· GenBank· DDBJ | AAL40085.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L78837 EMBL· GenBank· DDBJ | AAL40085.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AH011243 EMBL· GenBank· DDBJ | AAL40086.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AH011243 EMBL· GenBank· DDBJ | AAL40087.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AH011243 EMBL· GenBank· DDBJ | AAL40088.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L78837 EMBL· GenBank· DDBJ | AAL40088.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AH011243 EMBL· GenBank· DDBJ | AAL40089.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U66142 EMBL· GenBank· DDBJ | AAC51161.1 EMBL· GenBank· DDBJ | mRNA | ||
U66143 EMBL· GenBank· DDBJ | AAC51162.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U66144 EMBL· GenBank· DDBJ | AAC51163.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U66145 EMBL· GenBank· DDBJ | AAC51164.1 EMBL· GenBank· DDBJ | mRNA | ||
U66146 EMBL· GenBank· DDBJ | AAC51165.1 EMBL· GenBank· DDBJ | mRNA | ||
AP003721 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
X60992 EMBL· GenBank· DDBJ | CAA43306.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ786329 EMBL· GenBank· DDBJ | ABH04237.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ786330 EMBL· GenBank· DDBJ | ABH04238.1 EMBL· GenBank· DDBJ | mRNA |