CD8A_CANLF
ID CD8A_CANLF Reviewed; 239 AA.
AC P33706;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=T-cell surface glycoprotein CD8 alpha chain;
DE AltName: CD_antigen=CD8a;
DE Flags: Precursor;
GN Name=CD8A;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Beagle; TISSUE=Thymus;
RX PubMed=8091416; DOI=10.1111/j.1399-0039.1994.tb02320.x;
RA Gorman S.D., Frewin M.R., Cobbold S.P., Waldmann H.;
RT "Isolation and expression of cDNA encoding the canine CD4 and CD8 alpha
RT antigens.";
RL Tissue Antigens 43:184-188(1994).
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; L14287; AAB02294.1; -; mRNA.
DR RefSeq; NP_001002935.1; NM_001002935.2.
DR AlphaFoldDB; P33706; -.
DR SMR; P33706; -.
DR STRING; 9612.ENSCAFP00000011083; -.
DR PaxDb; P33706; -.
DR Ensembl; ENSCAFT00000064515; ENSCAFP00000063493; ENSCAFG00000007464.
DR Ensembl; ENSCAFT00030012805; ENSCAFP00030011196; ENSCAFG00030006889.
DR Ensembl; ENSCAFT00040028987; ENSCAFP00040025182; ENSCAFG00040015717.
DR Ensembl; ENSCAFT00845023463; ENSCAFP00845018419; ENSCAFG00845013158.
DR GeneID; 403157; -.
DR KEGG; cfa:403157; -.
DR CTD; 925; -.
DR VEuPathDB; HostDB:ENSCAFG00845013158; -.
DR VGNC; VGNC:38980; CD8A.
DR eggNOG; ENOG502SAZN; Eukaryota.
DR GeneTree; ENSGT00940000156588; -.
DR HOGENOM; CLU_085753_0_0_1; -.
DR InParanoid; P33706; -.
DR OMA; FRMSPTQ; -.
DR OrthoDB; 1448152at2759; -.
DR TreeFam; TF336070; -.
DR Proteomes; UP000002254; Chromosome 17.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0045065; P:cytotoxic T cell differentiation; IBA:GO_Central.
DR GO; GO:0002456; P:T cell mediated immunity; IBA:GO_Central.
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 SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..239
FT /note="T-cell surface glycoprotein CD8 alpha chain"
FT /id="PRO_0000014636"
FT TOPO_DOM 22..186
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..139
FT /note="Ig-like V-type"
FT REGION 143..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 210
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P01732"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 239 AA; 26036 MW; 1018579779A5CB7B CRC64;
MASRVTALLL PLALLLRAAA ASGPSRFRMT PPKVVGQLHA QVELQCQVLL STAAPGCSWL
YQRNEPAARP VFLMYISQSR AKPAEGLDTK HISGQKKTDS TYSLTLSRFR KEDEGYYFCS
VLSNSILYFS PFVPVFLPVK PPTTPAPRPP TRAPTNASKP VSPRGETCRP AAGSAVKTSG
LDFACEIYIW APLAGTCAVL LLSLVITIIC NHRNRRRVCK CPRPVVRPGG KPSPSEKYV
