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T-cell surface glycoprotein CD8 alpha chain (CD antigen CD8a)

 CD8A_BOVIN              Reviewed;         242 AA.
P31783;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
25-OCT-2017, entry version 111.
RecName: Full=T-cell surface glycoprotein CD8 alpha chain;
AltName: CD_antigen=CD8a;
Flags: Precursor;
Name=CD8A;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Thymus;
PubMed=1628904;
Lalor P., Bucci C., Fornaro M., Rattazzi M.C., Nakauchi H.,
Herzenberg L.A., Alberti S.;
"Molecular cloning, reconstruction and expression of the gene encoding
the alpha-chain of the bovine CD8 -- definition of three peptide
regions conserved across species.";
Immunology 76:95-102(1992).
-!- 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; X59416; CAA42051.1; -; mRNA.
PIR; S25663; S25663.
RefSeq; NP_776440.1; NM_174015.1.
UniGene; Bt.50; -.
PDB; 5EBG; X-ray; 1.80 A; A/B=25-139.
PDBsum; 5EBG; -.
ProteinModelPortal; P31783; -.
SMR; P31783; -.
STRING; 9913.ENSBTAP00000028175; -.
PaxDb; P31783; -.
PRIDE; P31783; -.
GeneID; 281060; -.
KEGG; bta:281060; -.
CTD; 925; -.
eggNOG; ENOG410IWN3; Eukaryota.
eggNOG; ENOG410Z6EI; LUCA.
HOGENOM; HOG000004794; -.
HOVERGEN; HBG008488; -.
InParanoid; P31783; -.
KO; K06458; -.
Proteomes; UP000009136; Unplaced.
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:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
GO; GO:0045065; P:cytotoxic T cell differentiation; IBA:GO_Central.
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.
SMART; SM00406; IGv; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain;
Lipoprotein; Membrane; Palmitate; Reference proteome; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 242 T-cell surface glycoprotein CD8 alpha
chain.
/FTId=PRO_0000014635.
TOPO_DOM 26 189 Extracellular. {ECO:0000255}.
TRANSMEM 190 214 Helical. {ECO:0000255}.
TOPO_DOM 215 242 Cytoplasmic. {ECO:0000255}.
DOMAIN 26 140 Ig-like V-type.
LIPID 213 213 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P01732}.
DISULFID 47 120 {ECO:0000255|PROSITE-ProRule:PRU00114}.
STRAND 28 33 {ECO:0000244|PDB:5EBG}.
STRAND 43 51 {ECO:0000244|PDB:5EBG}.
STRAND 58 63 {ECO:0000244|PDB:5EBG}.
STRAND 65 67 {ECO:0000244|PDB:5EBG}.
STRAND 72 80 {ECO:0000244|PDB:5EBG}.
TURN 90 92 {ECO:0000244|PDB:5EBG}.
STRAND 93 97 {ECO:0000244|PDB:5EBG}.
STRAND 99 109 {ECO:0000244|PDB:5EBG}.
HELIX 112 114 {ECO:0000244|PDB:5EBG}.
STRAND 116 124 {ECO:0000244|PDB:5EBG}.
STRAND 127 130 {ECO:0000244|PDB:5EBG}.
STRAND 134 137 {ECO:0000244|PDB:5EBG}.
SEQUENCE 242 AA; 26417 MW; 91481320EF05195E CRC64;
MASLLTALIL PLALLLLDAA KVLGSLSFRM SPTQKETRLG EKVELQCELL QSGMATGCSW
LRHIPGDDPR PTFLMYLSAQ RVKLAEGLDP RHISGAKVSG TKFQLTLSSF LQEDQGYYFC
SVVSNSILYF SNFVPVFLPA KPATTPAMRP SSAAPTSAPQ TRSVSPRSEV CRTSAGSAVD
TSRLDFACNI YIWAPLVGTC GVLLLSLVIT GICYRRNRRR VCKCPRPVVR QGGKPNLSEK
YV


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