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T-cell surface glycoprotein CD8 alpha chain (CD8 antigen 32 kDa chain) (OX-8 membrane antigen) (CD antigen CD8a)

 CD8A_RAT                Reviewed;         236 AA.
P07725;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
20-JUN-2018, entry version 147.
RecName: Full=T-cell surface glycoprotein CD8 alpha chain;
AltName: Full=CD8 antigen 32 kDa chain;
AltName: Full=OX-8 membrane antigen;
AltName: CD_antigen=CD8a;
Flags: Precursor;
Name=Cd8a;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3932064;
Johnson P., Gagnon J., Barclay A.N., Williams A.F.;
"Purification, chain separation and sequence of the MRC OX-8 antigen,
a marker of rat cytotoxic T lymphocytes.";
EMBO J. 4:2539-2545(1985).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
GLYCOSYLATION AT ASN-63; THR-144; THR-148; THR-152; THR-158 AND
THR-160.
PubMed=1908233; DOI=10.1016/0006-291X(91)91019-9;
Gooley A.A., Classon B.J., Marschalek R., Williams K.L.;
"Glycosylation sites identified by detection of glycosylated amino
acids released from Edman degradation: the identification of Xaa-Pro-
Xaa-Xaa as a motif for Thr-O-glycosylation.";
Biochem. Biophys. Res. Commun. 178:1194-1200(1991).
-!- FUNCTION: Integral membrane glycoprotein that plays an essential
role in the immune response and serves multiple functions in
responses against both external and internal offenses. In T-cells,
functions primarily as a coreceptor for MHC class I
molecule:peptide complex. The antigens presented by class I
peptides are derived from cytosolic proteins while class II
derived from extracellular proteins. Interacts simultaneously with
the T-cell receptor (TCR) and the MHC class I proteins presented
by antigen presenting cells (APCs). In turn, recruits the Src
kinase LCK to the vicinity of the TCR-CD3 complex. LCK then
initiates different intracellular signaling pathways by
phosphorylating various substrates ultimately leading to
lymphokine production, motility, adhesion and activation of
cytotoxic T-lymphocytes (CTLs). This mechanism enables CTLs to
recognize and eliminate infected cells and tumor cells. In NK-
cells, the presence of CD8A homodimers at the cell surface
provides a survival mechanism allowing conjugation and lysis of
multiple target cells. CD8A homodimer molecules also promote the
survival and differentiation of activated lymphocytes into memory
CD8 T-cells. {ECO:0000250|UniProtKB:P01732}.
-!- SUBUNIT: Forms disulfide-linked heterodimers with CD8B at the cell
surface. Forms also homodimers in several cell types including NK-
cells or peripheral blood T-lymphocytes. Interacts with the MHC
class I HLA-A/B2M dimer. Interacts with LCK in a zinc-dependent
manner. {ECO:0000250|UniProtKB:P01732}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P01732}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P01732}. Note=CD8A localizes to
lipid rafts only when associated with its partner CD8B.
{ECO:0000250|UniProtKB:P01732}.
-!- PTM: Palmitoylated, but association with CD8B seems to be more
important for the enrichment of CD8A in lipid rafts.
{ECO:0000250|UniProtKB:P01732}.
-!- PTM: O-glycosylated. {ECO:0000250|UniProtKB:P01732}.
-!- PTM: Phosphorylated in cytotoxic T-lymphocytes (CTLs) following
activation. {ECO:0000250|UniProtKB:P01732}.
-----------------------------------------------------------------------
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EMBL; X03015; CAA26798.1; -; mRNA.
EMBL; BC088126; AAH88126.1; -; mRNA.
PIR; A24637; A24637.
RefSeq; NP_113726.1; NM_031538.2.
RefSeq; XP_006236692.1; XM_006236630.3.
RefSeq; XP_008761198.1; XM_008762976.2.
UniGene; Rn.10306; -.
ProteinModelPortal; P07725; -.
SMR; P07725; -.
DIP; DIP-60779N; -.
IntAct; P07725; 1.
STRING; 10116.ENSRNOP00000009516; -.
iPTMnet; P07725; -.
PhosphoSitePlus; P07725; -.
PaxDb; P07725; -.
PRIDE; P07725; -.
Ensembl; ENSRNOT00000009515; ENSRNOP00000009516; ENSRNOG00000007178.
GeneID; 24930; -.
KEGG; rno:24930; -.
UCSC; RGD:2316; rat.
CTD; 925; -.
RGD; 2316; Cd8a.
eggNOG; ENOG410IWN3; Eukaryota.
eggNOG; ENOG410Z6EI; LUCA.
GeneTree; ENSGT00510000048935; -.
HOGENOM; HOG000004794; -.
HOVERGEN; HBG008488; -.
InParanoid; P07725; -.
KO; K06458; -.
OMA; RVCKCPR; -.
OrthoDB; EOG091G0YIT; -.
PhylomeDB; P07725; -.
TreeFam; TF336070; -.
Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
PRO; PR:P07725; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000007178; -.
Genevisible; P07725; RN.
GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0044853; C:plasma membrane raft; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
GO; GO:0045065; P:cytotoxic T cell differentiation; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; NAS:RGD.
GO; GO:0042110; P:T cell activation; IMP:RGD.
GO; GO:0002456; P:T cell mediated immunity; IBA:GO_Central.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR015468; CD8_asu.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
PANTHER; PTHR10441; PTHR10441; 1.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
Adaptive immunity; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Immunity; Immunoglobulin domain; Lipoprotein; Membrane;
Palmitate; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 236 T-cell surface glycoprotein CD8 alpha
chain.
/FTId=PRO_0000014641.
TOPO_DOM 27 189 Extracellular. {ECO:0000255}.
TRANSMEM 190 210 Helical. {ECO:0000255}.
TOPO_DOM 211 236 Cytoplasmic. {ECO:0000255}.
DOMAIN 27 130 Ig-like V-type.
LIPID 211 211 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P01732}.
CARBOHYD 63 63 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:1908233}.
CARBOHYD 144 144 O-linked (GalNAc...) threonine; partial.
{ECO:0000269|PubMed:1908233}.
CARBOHYD 148 148 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:1908233}.
CARBOHYD 152 152 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:1908233}.
CARBOHYD 158 158 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:1908233}.
CARBOHYD 160 160 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:1908233}.
DISULFID 47 119 {ECO:0000255|PROSITE-ProRule:PRU00114}.
SEQUENCE 236 AA; 26196 MW; ADFAC54E4C99C1BE CRC64;
MASRVICFLS LNLLLLDVIT RLQVSGQLQL SPKKVDAEIG QEVKLTCEVL RDTSQGCSWL
FRNSSSELLQ PTFIIYVSSS RSKLNDILDP NLFSARKENN KYILTLSKFS TKNQGYYFCS
ITSNSVMYFS PLVPVFQKVN SIITKPVTRA PTPVPPPTGT PRPLRPEACR PGASGSVEGM
GLGFACDIYI WAPLAGICAV LLLSLVITLI CCHRNRRRVC KCPRPLVKPR PSEKFV


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