CD8A_RAT
ID CD8A_RAT Reviewed; 236 AA.
AC P07725;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=T-cell surface glycoprotein CD8 alpha chain;
DE AltName: Full=CD8 antigen 32 kDa chain;
DE AltName: Full=OX-8 membrane antigen;
DE AltName: CD_antigen=CD8a;
DE Flags: Precursor;
GN Name=Cd8a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3932064; DOI=10.1002/j.1460-2075.1985.tb03968.x;
RA Johnson P., Gagnon J., Barclay A.N., Williams A.F.;
RT "Purification, chain separation and sequence of the MRC OX-8 antigen, a
RT marker of rat cytotoxic T lymphocytes.";
RL EMBO J. 4:2539-2545(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP GLYCOSYLATION AT ASN-63; THR-144; THR-148; THR-152; THR-158 AND THR-160.
RX PubMed=1908233; DOI=10.1016/0006-291x(91)91019-9;
RA Gooley A.A., Classon B.J., Marschalek R., Williams K.L.;
RT "Glycosylation sites identified by detection of glycosylated amino acids
RT released from Edman degradation: the identification of Xaa-Pro-Xaa-Xaa as a
RT motif for Thr-O-glycosylation.";
RL Biochem. Biophys. Res. Commun. 178:1194-1200(1991).
CC -!- FUNCTION: Integral membrane glycoprotein that plays an essential role
CC in the immune response and serves multiple functions in responses
CC against both external and internal offenses. In T-cells, functions
CC primarily as a coreceptor for MHC class I molecule:peptide complex. The
CC antigens presented by class I peptides are derived from cytosolic
CC proteins while class II derived from extracellular proteins. Interacts
CC simultaneously with the T-cell receptor (TCR) and the MHC class I
CC proteins presented by antigen presenting cells (APCs). In turn,
CC recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK
CC then initiates different intracellular signaling pathways by
CC phosphorylating various substrates ultimately leading to lymphokine
CC production, motility, adhesion and activation of cytotoxic T-
CC lymphocytes (CTLs). This mechanism enables CTLs to recognize and
CC eliminate infected cells and tumor cells. In NK-cells, the presence of
CC CD8A homodimers at the cell surface provides a survival mechanism
CC allowing conjugation and lysis of multiple target cells. CD8A homodimer
CC molecules also promote the survival and differentiation of activated
CC lymphocytes into memory CD8 T-cells. {ECO:0000250|UniProtKB:P01732}.
CC -!- SUBUNIT: Forms disulfide-linked heterodimers with CD8B at the cell
CC surface. Forms also homodimers in several cell types including NK-cells
CC or peripheral blood T-lymphocytes. Interacts with the MHC class I HLA-
CC A/B2M dimer. Interacts with LCK in a zinc-dependent manner.
CC {ECO:0000250|UniProtKB:P01732}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01732};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P01732}.
CC Note=CD8A localizes to lipid rafts only when associated with its
CC partner CD8B. {ECO:0000250|UniProtKB:P01732}.
CC -!- PTM: Palmitoylated, but association with CD8B seems to be more
CC important for the enrichment of CD8A in lipid rafts.
CC {ECO:0000250|UniProtKB:P01732}.
CC -!- PTM: O-glycosylated. {ECO:0000250|UniProtKB:P01732}.
CC -!- PTM: Phosphorylated in cytotoxic T-lymphocytes (CTLs) following
CC activation. {ECO:0000250|UniProtKB:P01732}.
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DR EMBL; X03015; CAA26798.1; -; mRNA.
DR EMBL; BC088126; AAH88126.1; -; mRNA.
DR PIR; A24637; A24637.
DR RefSeq; NP_113726.1; NM_031538.2.
DR RefSeq; XP_006236692.1; XM_006236630.3.
DR RefSeq; XP_008761198.1; XM_008762976.2.
DR AlphaFoldDB; P07725; -.
DR SMR; P07725; -.
DR DIP; DIP-60779N; -.
DR IntAct; P07725; 1.
DR STRING; 10116.ENSRNOP00000009516; -.
DR GlyGen; P07725; 6 sites.
DR iPTMnet; P07725; -.
DR PhosphoSitePlus; P07725; -.
DR PaxDb; P07725; -.
DR Ensembl; ENSRNOT00000009515; ENSRNOP00000009516; ENSRNOG00000007178.
DR GeneID; 24930; -.
DR KEGG; rno:24930; -.
DR UCSC; RGD:2316; rat.
DR CTD; 925; -.
DR RGD; 2316; Cd8a.
DR eggNOG; ENOG502SAZN; Eukaryota.
DR GeneTree; ENSGT00940000156588; -.
DR HOGENOM; CLU_085753_0_0_1; -.
DR InParanoid; P07725; -.
DR OMA; FRMSPTQ; -.
DR OrthoDB; 1448152at2759; -.
DR PhylomeDB; P07725; -.
DR TreeFam; TF336070; -.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR PRO; PR:P07725; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000007178; Expressed in thymus and 17 other tissues.
DR Genevisible; P07725; RN.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0044853; C:plasma membrane raft; ISO:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0023024; F:MHC class I protein complex binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:RGD.
DR GO; GO:0045065; P:cytotoxic T cell differentiation; ISO:RGD.
DR GO; GO:0051607; P:defense response to virus; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; NAS:RGD.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; ISO:RGD.
DR GO; GO:0042110; P:T cell activation; IMP:RGD.
DR GO; GO:0002456; P:T cell mediated immunity; ISO:RGD.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR015468; CD8_asu.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR10441; PTHR10441; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..236
FT /note="T-cell surface glycoprotein CD8 alpha chain"
FT /id="PRO_0000014641"
FT TOPO_DOM 27..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..130
FT /note="Ig-like V-type"
FT REGION 150..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 211
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P01732"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:1908233"
FT CARBOHYD 144
FT /note="O-linked (GalNAc...) threonine; partial"
FT /evidence="ECO:0000269|PubMed:1908233"
FT CARBOHYD 148
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1908233"
FT CARBOHYD 152
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1908233"
FT CARBOHYD 158
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1908233"
FT CARBOHYD 160
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1908233"
FT DISULFID 47..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ 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
