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T-cell differentiation antigen CD6 (T12) (TP120) (CD antigen CD6) [Cleaved into: Soluble CD6]

 CD6_HUMAN               Reviewed;         668 AA.
P30203; A4KAD4; A4KAD5; Q9UMF2; Q9Y4K7; Q9Y4K8; Q9Y4K9; Q9Y4L0;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
15-DEC-2009, sequence version 3.
25-OCT-2017, entry version 151.
RecName: Full=T-cell differentiation antigen CD6;
AltName: Full=T12;
AltName: Full=TP120;
AltName: CD_antigen=CD6;
Contains:
RecName: Full=Soluble CD6;
Flags: Precursor;
Name=CD6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING,
VARIANT VAL-257, AND SUBCELLULAR LOCATION.
PubMed=9013954;
Bowen M.A., Whitney G.S., Neubauer M., Starling G.C., Palmer D.,
Zhang J., Nowak N.J., Shows T.B., Aruffo A.;
"Structure and chromosomal location of the human CD6 gene: detection
of five human CD6 isoforms.";
J. Immunol. 158:1149-1156(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-468, AND VARIANT VAL-257.
PubMed=1919444; DOI=10.1084/jem.174.4.949;
Aruffo A., Melnick M.B., Linsley P.S., Seed B.;
"The lymphocyte glycoprotein CD6 contains a repeated domain structure
characteristic of a new family of cell surface and secreted
proteins.";
J. Exp. Med. 174:949-952(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-278 (ISOFORM 6), NUCLEOTIDE SEQUENCE
[MRNA] OF 1-300 (ISOFORM 7), SUBCELLULAR LOCATION, VARIANTS MET-217
AND VAL-257, AND ALTERNATIVE SPLICING.
PubMed=17371992; DOI=10.4049/jimmunol.178.7.4351;
Castro M.A., Oliveira M.I., Nunes R.J., Fabre S., Barbosa R.,
Peixoto A., Brown M.H., Parnes J.R., Bismuth G., Moreira A., Rocha B.,
Carmo A.M.;
"Extracellular isoforms of CD6 generated by alternative splicing
regulate targeting of CD6 to the immunological synapse.";
J. Immunol. 178:4351-4361(2007).
[5]
PHOSPHORYLATION AT SERINE RESIDUES, DISULFIDE BONDS, AND
GLYCOSYLATION.
PubMed=2016320;
Swack J.A., Mier J.W., Romain P.L., Hull S.R., Rudd C.E.;
"Biosynthesis and post-translational modification of CD6, a T cell
signal-transducing molecule.";
J. Biol. Chem. 266:7137-7143(1991).
[6]
PHOSPHORYLATION AT TYROSINE RESIDUES.
PubMed=7678115; DOI=10.1084/jem.177.1.219;
Wee S., Schieven G.L., Kirihara J.M., Tsu T.T., Ledbetter J.A.,
Aruffo A.;
"Tyrosine phosphorylation of CD6 by stimulation of CD3: augmentation
by the CD4 and CD2 coreceptors.";
J. Exp. Med. 177:219-223(1993).
[7]
FUNCTION, INTERACTION WITH ALCAM, TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
PubMed=15048703; DOI=10.1002/eji.200424856;
Hassan N.J., Barclay A.N., Brown M.H.;
"Frontline: Optimal T cell activation requires the engagement of CD6
and CD166.";
Eur. J. Immunol. 34:930-940(2004).
[8]
FUNCTION, INTERACTION WITH CD3E AND THE TCR/CD3 COMPLEX, SUBUNIT,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15294938; DOI=10.4049/jimmunol.173.4.2262;
Gimferrer I., Calvo M., Mittelbrunn M., Farnos M., Sarrias M.R.,
Enrich C., Vives J., Sanchez-Madrid F., Lozano F.;
"Relevance of CD6-mediated interactions in T cell activation and
proliferation.";
J. Immunol. 173:2262-2270(2004).
[9]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ALCAM, AND TISSUE
SPECIFICITY.
PubMed=16352806; DOI=10.1182/blood-2005-09-3881;
Zimmerman A.W., Joosten B., Torensma R., Parnes J.R.,
van Leeuwen F.N., Figdor C.G.;
"Long-term engagement of CD6 and ALCAM is essential for T-cell
proliferation induced by dendritic cells.";
Blood 107:3212-3220(2006).
[10]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ALCAM AND LCP2,
PHOSPHORYLATION AT TYR-662, AND MUTAGENESIS OF TYR-662.
PubMed=16914752; DOI=10.1128/MCB.00688-06;
Hassan N.J., Simmonds S.J., Clarkson N.G., Hanrahan S., Puklavec M.J.,
Bomb M., Barclay A.N., Brown M.H.;
"CD6 regulates T-cell responses through activation-dependent
recruitment of the positive regulator SLP-76.";
Mol. Cell. Biol. 26:6727-6738(2006).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17601777; DOI=10.1073/pnas.0702815104;
Sarrias M.R., Farnos M., Mota R., Sanchez-Barbero F., Ibanez A.,
Gimferrer I., Vera J., Fenutria R., Casals C., Yelamos J., Lozano F.;
"CD6 binds to pathogen-associated molecular patterns and protects from
LPS-induced septic shock.";
Proc. Natl. Acad. Sci. U.S.A. 104:11724-11729(2007).
[12]
INTERACTION WITH ALCAM; LGALS1 AND LGALS3, GLYCOSYLATION, SUBCELLULAR
LOCATION, AND FUNCTION.
PubMed=24945728; DOI=10.1016/j.febslet.2014.05.064;
Escoda-Ferran C., Carrasco E., Caballero-Banos M., Miro-Julia C.,
Martinez-Florensa M., Consuegra-Fernandez M., Martinez V.G., Liu F.T.,
Lozano F.;
"Modulation of CD6 function through interaction with galectin-1 and
-3.";
FEBS Lett. 588:2805-2813(2014).
[13]
FUNCTION, INTERACTION WITH LCP2, AND PHOSPHORYLATION.
PubMed=24584089; DOI=10.1038/ni.2843;
Roncagalli R., Hauri S., Fiore F., Liang Y., Chen Z., Sansoni A.,
Kanduri K., Joly R., Malzac A., Laehdesmaeki H., Lahesmaa R.,
Yamasaki S., Saito T., Malissen M., Aebersold R., Gstaiger M.,
Malissen B.;
"Quantitative proteomics analysis of signalosome dynamics in primary T
cells identifies the surface receptor CD6 as a Lat adaptor-independent
TCR signaling hub.";
Nat. Immunol. 15:384-392(2014).
[14] {ECO:0000244|PDB:5A2E}
X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 1-364, DISULFIDE BONDS,
GLYCOSYLATION AT ASN-28 ASN-49 AND ASN-229, IDENTIFICATION BY MASS
SPECTROMETRY, INTERACTION WITH ALCAM, CHARACTERIZATION OF VARIANT
ASN-351, AND MUTAGENESIS OF ASP-291; GLU-293; TYR-295; GLU-298;
ARG-314; TYR-327; SER-329; ASN-346; LEU-349; GLN-352 AND SER-353.
PubMed=26146185; DOI=10.1016/j.str.2015.05.019;
Chappell P.E., Garner L.I., Yan J., Metcalfe C., Hatherley D.,
Johnson S., Robinson C.V., Lea S.M., Brown M.H.;
"Structures of CD6 and its ligand CD166 give insight into their
interaction.";
Structure 23:1426-1436(2015).
-!- FUNCTION: Cell adhesion molecule that mediates cell-cell contacts
and regulates T-cell responses via its interaction with
ALCAM/CD166 (PubMed:15048703, PubMed:15294938, PubMed:16352806,
PubMed:16914752, PubMed:24945728, PubMed:24584089). Contributes to
signaling cascades triggered by activation of the TCR/CD3 complex
(PubMed:24584089). Functions as 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 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). {ECO:0000269|PubMed:15048703,
ECO:0000269|PubMed:15294938, ECO:0000269|PubMed:16352806,
ECO:0000269|PubMed:16914752, ECO:0000269|PubMed:17601777,
ECO:0000269|PubMed:24584089, ECO:0000269|PubMed:24945728}.
-!- SUBUNIT: Interacts (via extracellular domain) with ALCAM/CD166
(via extracellular domain) (PubMed:15048703, PubMed:16352806,
PubMed:16914752, PubMed:24945728, PubMed:26146185). 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).
{ECO:0000250|UniProtKB:Q61003, ECO:0000269|PubMed:15048703,
ECO:0000269|PubMed:15294938, ECO:0000269|PubMed:16352806,
ECO:0000269|PubMed:16914752, ECO:0000269|PubMed:24945728,
ECO:0000269|PubMed:26146185}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-2873748, EBI-2873748;
Q13740:ALCAM; NbExp=5; IntAct=EBI-2873748, EBI-1188108;
Q13094:LCP2; NbExp=3; IntAct=EBI-2873748, EBI-346946;
P09382:LGALS1; NbExp=2; IntAct=EBI-2873748, EBI-1048875;
P17931:LGALS3; NbExp=2; IntAct=EBI-2873748, EBI-1170392;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15048703,
ECO:0000269|PubMed:15294938, ECO:0000269|PubMed:16352806,
ECO:0000269|PubMed:16914752, ECO:0000269|PubMed:17371992,
ECO:0000269|PubMed:17601777, ECO:0000269|PubMed:24945728,
ECO:0000269|PubMed:9013954}; Single-pass type I membrane protein
{ECO:0000269|PubMed:17371992}. Note=Detected at the immunological
synapse, i.e, at the contact zone between antigen-presenting
dendritic cells and T-cells (PubMed:15294938, PubMed:16352806).
Colocalizes with the TCR/CD3 complex at the immunological synapse
(PubMed:15294938). {ECO:0000269|PubMed:15294938}.
-!- SUBCELLULAR LOCATION: Soluble CD6: Secreted
{ECO:0000269|PubMed:17601777}. Note=The origins of the secreted
form are not clear, but it might be created by proteolytic
shedding of the ectodomain. {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=CD6A;
IsoId=P30203-1; Sequence=Displayed;
Name=CD6B;
IsoId=P30203-2; Sequence=VSP_006221;
Name=CD6C;
IsoId=P30203-3; Sequence=VSP_006221, VSP_006222;
Name=CD6D;
IsoId=P30203-4; Sequence=VSP_006221, VSP_006223;
Name=CD6E;
IsoId=P30203-5; Sequence=VSP_006222, VSP_006223;
Name=6; Synonyms=CD6deltaD3Ex6;
IsoId=P30203-6; Sequence=VSP_054246;
Note=Lacks the third SRCR domain and doesn't bind ALCAM/CD166.
Doesn't localize to the immunological synapse.;
Name=7; Synonyms=CD6deltaD3;
IsoId=P30203-7; Sequence=VSP_054245;
Note=Lacks 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.
{ECO:0000269|PubMed:17371992};
-!- TISSUE SPECIFICITY: Detected on thymocytes (PubMed:15294938).
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. {ECO:0000269|PubMed:15048703, ECO:0000269|PubMed:15294938,
ECO:0000269|PubMed:16352806, ECO:0000269|PubMed:17601777,
ECO:0000269|PubMed:9013954}.
-!- PTM: After T-cell activation, becomes hyperphosphorylated on Ser
and Thr residues and phosphorylated on Tyr residues.
{ECO:0000269|PubMed:16914752, ECO:0000269|PubMed:2016320,
ECO:0000269|PubMed:24584089, ECO:0000269|PubMed:7678115}.
-!- PTM: Glycosylated. {ECO:0000305|PubMed:24945728}.
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EMBL; U66142; AAC51161.1; -; mRNA.
EMBL; U66143; AAC51162.1; -; Genomic_DNA.
EMBL; U66144; AAC51163.1; -; Genomic_DNA.
EMBL; U66145; AAC51164.1; -; mRNA.
EMBL; U66146; AAC51165.1; -; mRNA.
EMBL; AP003721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X60992; CAA43306.1; -; mRNA.
EMBL; DQ786329; ABH04237.1; -; mRNA.
EMBL; DQ786330; ABH04238.1; -; mRNA.
CCDS; CCDS58137.1; -. [P30203-5]
CCDS; CCDS58138.1; -. [P30203-4]
CCDS; CCDS7999.1; -. [P30203-1]
PIR; S26741; S26741.
RefSeq; NP_001241679.1; NM_001254750.1. [P30203-4]
RefSeq; NP_001241680.1; NM_001254751.1. [P30203-5]
RefSeq; NP_006716.3; NM_006725.4. [P30203-1]
RefSeq; XP_006718801.1; XM_006718738.1. [P30203-2]
RefSeq; XP_006718804.1; XM_006718741.1. [P30203-3]
RefSeq; XP_011543664.1; XM_011545362.1. [P30203-7]
UniGene; Hs.744366; -.
PDB; 5A2E; X-ray; 3.15 A; A=1-364.
PDBsum; 5A2E; -.
ProteinModelPortal; P30203; -.
SMR; P30203; -.
BioGrid; 107361; 6.
DIP; DIP-43704N; -.
IntAct; P30203; 8.
MINT; MINT-1351620; -.
STRING; 9606.ENSP00000323280; -.
ChEMBL; CHEMBL3712853; -.
GuidetoPHARMACOLOGY; 2917; -.
iPTMnet; P30203; -.
PhosphoSitePlus; P30203; -.
BioMuta; CD6; -.
DMDM; 281185506; -.
PaxDb; P30203; -.
PeptideAtlas; P30203; -.
PRIDE; P30203; -.
DNASU; 923; -.
Ensembl; ENST00000313421; ENSP00000323280; ENSG00000013725. [P30203-1]
Ensembl; ENST00000352009; ENSP00000340628; ENSG00000013725. [P30203-4]
Ensembl; ENST00000452451; ENSP00000390676; ENSG00000013725. [P30203-5]
GeneID; 923; -.
KEGG; hsa:923; -.
UCSC; uc001nqq.4; human. [P30203-1]
CTD; 923; -.
DisGeNET; 923; -.
EuPathDB; HostDB:ENSG00000013725.14; -.
GeneCards; CD6; -.
H-InvDB; HIX0009678; -.
HGNC; HGNC:1691; CD6.
HPA; CAB002489; -.
HPA; CAB016252; -.
MIM; 186720; gene.
neXtProt; NX_P30203; -.
OpenTargets; ENSG00000013725; -.
PharmGKB; PA26230; -.
eggNOG; ENOG410IK9E; Eukaryota.
eggNOG; ENOG410YC2B; LUCA.
GeneTree; ENSGT00900000140803; -.
HOGENOM; HOG000137917; -.
HOVERGEN; HBG005289; -.
InParanoid; P30203; -.
KO; K06456; -.
OMA; RFQMPPL; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; P30203; -.
TreeFam; TF329295; -.
GeneWiki; CD6; -.
GenomeRNAi; 923; -.
PRO; PR:P30203; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000013725; -.
CleanEx; HS_CD6; -.
ExpressionAtlas; P30203; baseline and differential.
Genevisible; P30203; HS.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
GO; GO:0070891; F:lipoteichoic acid binding; IMP:UniProtKB.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IDA:UniProtKB.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:UniProtKB.
GO; GO:0001771; P:immunological synapse formation; IMP:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IDA:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; IDA:UniProtKB.
Gene3D; 3.10.250.10; -; 2.
InterPro; IPR001190; SRCR.
InterPro; IPR017448; SRCR-like_dom.
InterPro; IPR036772; SRCR-like_dom_sf.
Pfam; PF00530; SRCR; 3.
PRINTS; PR00258; SPERACTRCPTR.
SMART; SM00202; SR; 3.
SUPFAM; SSF56487; SSF56487; 3.
PROSITE; PS00420; SRCR_1; 1.
PROSITE; PS50287; SRCR_2; 3.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing; Cell adhesion;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Immunity; Innate immunity; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 668 T-cell differentiation antigen CD6.
/FTId=PRO_0000033227.
CHAIN 18 ? Soluble CD6.
/FTId=PRO_0000435133.
TOPO_DOM 18 402 Extracellular. {ECO:0000255}.
TRANSMEM 403 423 Helical. {ECO:0000255}.
TOPO_DOM 424 668 Cytoplasmic. {ECO:0000255}.
DOMAIN 45 156 SRCR 1. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 161 260 SRCR 2. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 265 361 SRCR 3. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
MOD_RES 662 662 Phosphotyrosine.
{ECO:0000269|PubMed:16914752}.
CARBOHYD 28 28 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000269|PubMed:26146185}.
CARBOHYD 49 49 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000269|PubMed:26146185}.
CARBOHYD 112 112 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 118 118 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 229 229 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000269|PubMed:26146185}.
CARBOHYD 339 339 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 345 345 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 368 368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 54 88 {ECO:0000244|PDB:5A2E,
ECO:0000269|PubMed:26146185}.
DISULFID 70 144 {ECO:0000244|PDB:5A2E,
ECO:0000255|PROSITE-ProRule:PRU00196,
ECO:0000269|PubMed:26146185}.
DISULFID 83 155 {ECO:0000244|PDB:5A2E,
ECO:0000255|PROSITE-ProRule:PRU00196,
ECO:0000269|PubMed:26146185}.
DISULFID 129 137 {ECO:0000244|PDB:5A2E,
ECO:0000255|PROSITE-ProRule:PRU00196,
ECO:0000269|PubMed:26146185}.
DISULFID 170 204 {ECO:0000244|PDB:5A2E,
ECO:0000269|PubMed:26146185}.
DISULFID 186 249 {ECO:0000244|PDB:5A2E,
ECO:0000255|PROSITE-ProRule:PRU00196,
ECO:0000269|PubMed:26146185}.
DISULFID 199 259 {ECO:0000244|PDB:5A2E,
ECO:0000255|PROSITE-ProRule:PRU00196,
ECO:0000269|PubMed:26146185}.
DISULFID 230 240 {ECO:0000244|PDB:5A2E,
ECO:0000255|PROSITE-ProRule:PRU00196,
ECO:0000269|PubMed:26146185}.
DISULFID 290 350 {ECO:0000244|PDB:5A2E,
ECO:0000255|PROSITE-ProRule:PRU00196,
ECO:0000269|PubMed:26146185}.
DISULFID 303 360 {ECO:0000244|PDB:5A2E,
ECO:0000255|PROSITE-ProRule:PRU00196,
ECO:0000269|PubMed:26146185}.
DISULFID 330 340 {ECO:0000244|PDB:5A2E,
ECO:0000255|PROSITE-ProRule:PRU00196,
ECO:0000269|PubMed:26146185}.
VAR_SEQ 259 359 Missing (in isoform 7).
{ECO:0000303|PubMed:17371992}.
/FTId=VSP_054245.
VAR_SEQ 261 383 Missing (in isoform 6).
{ECO:0000303|PubMed:17371992}.
/FTId=VSP_054246.
VAR_SEQ 431 462 Missing (in isoform CD6B, isoform CD6C
and isoform CD6D). {ECO:0000305}.
/FTId=VSP_006221.
VAR_SEQ 463 504 VFMLPIQVQAPPPEDSDSGSDSDYEHYDFSAQPPVALTTFY
N -> D (in isoform CD6C and isoform
CD6E). {ECO:0000305}.
/FTId=VSP_006222.
VAR_SEQ 613 647 Missing (in isoform CD6D and isoform
CD6E). {ECO:0000305}.
/FTId=VSP_006223.
VARIANT 217 217 T -> M (in dbSNP:rs11230562).
{ECO:0000269|PubMed:17371992}.
/FTId=VAR_059809.
VARIANT 225 225 R -> W (in dbSNP:rs11230563).
/FTId=VAR_057202.
VARIANT 257 257 A -> V (in dbSNP:rs2074225).
{ECO:0000269|PubMed:17371992,
ECO:0000269|PubMed:1919444,
ECO:0000269|PubMed:9013954}.
/FTId=VAR_060790.
VARIANT 271 271 A -> T (in dbSNP:rs12360861).
/FTId=VAR_057203.
VARIANT 351 351 S -> N (adds an additional glycosylation
site and impairs interaction with ALCAM;
dbSNP:rs34974368).
{ECO:0000269|PubMed:26146185}.
/FTId=VAR_057204.
VARIANT 606 606 G -> S (in dbSNP:rs2074233).
/FTId=VAR_057205.
MUTAGEN 291 291 D->A: Strongly reduces interaction with
ALCAM. {ECO:0000269|PubMed:26146185}.
MUTAGEN 293 293 E->A: Reduces interaction with ALCAM.
{ECO:0000269|PubMed:26146185}.
MUTAGEN 295 295 Y->A: Abolishes interaction with ALCAM.
{ECO:0000269|PubMed:26146185}.
MUTAGEN 298 298 E->A: Nearly abolishes interaction with
ALCAM. {ECO:0000269|PubMed:26146185}.
MUTAGEN 314 314 R->A: Reduces interaction with ALCAM.
{ECO:0000269|PubMed:26146185}.
MUTAGEN 327 327 Y->A: Nearly abolishes interaction with
ALCAM. {ECO:0000269|PubMed:26146185}.
MUTAGEN 329 329 S->A: Reduces interaction with ALCAM.
{ECO:0000269|PubMed:26146185}.
MUTAGEN 346 346 N->A: Strongly reduces interaction with
ALCAM. {ECO:0000269|PubMed:26146185}.
MUTAGEN 349 349 L->A: Reduces interaction with ALCAM.
{ECO:0000269|PubMed:26146185}.
MUTAGEN 352 352 Q->A: Reduces interaction with ALCAM.
{ECO:0000269|PubMed:26146185}.
MUTAGEN 353 353 S->A: Reduces interaction with ALCAM.
{ECO:0000269|PubMed:26146185}.
MUTAGEN 662 662 Y->F: Reduces tyrosine phosphorylation.
Reduces affinity for LCP2. Impairs
activation of T-cells.
{ECO:0000269|PubMed:16914752}.
CONFLICT 47 47 L -> R (in Ref. 4; ABH04237).
{ECO:0000305}.
CONFLICT 463 468 VFMLPI -> GPGPAP (in Ref. 3; CAA43306).
{ECO:0000305}.
CONFLICT 613 613 Missing (in Ref. 1; AAC51162).
{ECO:0000305}.
STRAND 45 52 {ECO:0000244|PDB:5A2E}.
STRAND 55 60 {ECO:0000244|PDB:5A2E}.
HELIX 76 86 {ECO:0000244|PDB:5A2E}.
STRAND 90 97 {ECO:0000244|PDB:5A2E}.
STRAND 126 134 {ECO:0000244|PDB:5A2E}.
STRAND 137 142 {ECO:0000244|PDB:5A2E}.
STRAND 146 148 {ECO:0000244|PDB:5A2E}.
STRAND 150 155 {ECO:0000244|PDB:5A2E}.
STRAND 159 168 {ECO:0000244|PDB:5A2E}.
STRAND 171 180 {ECO:0000244|PDB:5A2E}.
STRAND 182 187 {ECO:0000244|PDB:5A2E}.
HELIX 192 202 {ECO:0000244|PDB:5A2E}.
STRAND 206 209 {ECO:0000244|PDB:5A2E}.
STRAND 223 228 {ECO:0000244|PDB:5A2E}.
STRAND 235 237 {ECO:0000244|PDB:5A2E}.
STRAND 247 249 {ECO:0000244|PDB:5A2E}.
HELIX 251 253 {ECO:0000244|PDB:5A2E}.
STRAND 256 259 {ECO:0000244|PDB:5A2E}.
STRAND 264 272 {ECO:0000244|PDB:5A2E}.
STRAND 275 282 {ECO:0000244|PDB:5A2E}.
STRAND 285 291 {ECO:0000244|PDB:5A2E}.
HELIX 296 306 {ECO:0000244|PDB:5A2E}.
STRAND 310 313 {ECO:0000244|PDB:5A2E}.
STRAND 325 329 {ECO:0000244|PDB:5A2E}.
HELIX 337 339 {ECO:0000244|PDB:5A2E}.
STRAND 340 345 {ECO:0000244|PDB:5A2E}.
TURN 347 349 {ECO:0000244|PDB:5A2E}.
STRAND 350 352 {ECO:0000244|PDB:5A2E}.
STRAND 357 363 {ECO:0000244|PDB:5A2E}.
SEQUENCE 668 AA; 71801 MW; 59E6790E77FFBC42 CRC64;
MWLFFGITGL LTAALSGHPS PAPPDQLNTS SAESELWEPG ERLPVRLTNG SSSCSGTVEV
RLEASWEPAC GALWDSRAAE AVCRALGCGG AEAASQLAPP TPELPPPPAA GNTSVAANAT
LAGAPALLCS GAEWRLCEVV EHACRSDGRR ARVTCAENRA LRLVDGGGAC AGRVEMLEHG
EWGSVCDDTW DLEDAHVVCR QLGCGWAVQA LPGLHFTPGR GPIHRDQVNC SGAEAYLWDC
PGLPGQHYCG HKEDAGAVCS EHQSWRLTGG ADRCEGQVEV HFRGVWNTVC DSEWYPSEAK
VLCQSLGCGT AVERPKGLPH SLSGRMYYSC NGEELTLSNC SWRFNNSNLC SQSLAARVLC
SASRSLHNLS TPEVPASVQT VTIESSVTVK IENKESRELM LLIPSIVLGI LLLGSLIFIA
FILLRIKGKY ALPVMVNHQH LPTTIPAGSN SYQPVPITIP KEVFMLPIQV QAPPPEDSDS
GSDSDYEHYD FSAQPPVALT TFYNSQRHRV TDEEVQQSRF QMPPLEEGLE ELHASHIPTA
NPGHCITDPP SLGPQYHPRS NSESSTSSGE DYCNSPKSKL PPWNPQVFSS ERSSFLEQPP
NLELAGTQPA FSAGPPADDS SSTSSGEWYQ NFQPPPQPPS EEQFGCPGSP SPQPDSTDND
DYDDISAA


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