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T-cell surface glycoprotein CD8 alpha chain (T-cell surface glycoprotein Lyt-2) (CD antigen CD8a)

 CD8A_MOUSE              Reviewed;         247 AA.
P01731;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
27-SEP-2017, entry version 169.
RecName: Full=T-cell surface glycoprotein CD8 alpha chain;
AltName: Full=T-cell surface glycoprotein Lyt-2;
AltName: CD_antigen=CD8a;
Flags: Precursor;
Name=Cd8a; Synonyms=Lyt-2, Lyt2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=3927298; DOI=10.1073/pnas.82.15.5126;
Nakauchi H., Nolan G.P., Hsu C., Huang H.S., Kavathas P.,
Herzenberg L.A.;
"Molecular cloning of Lyt-2, a membrane glycoprotein marking a subset
of mouse T lymphocytes: molecular homology to its human counterpart,
Leu-2/T8, and to immunoglobulin variable regions.";
Proc. Natl. Acad. Sci. U.S.A. 82:5126-5130(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3935316; DOI=10.1016/0092-8674(85)90020-0;
Zamoyska R., Vollmer A.C., Sizer K.C., Liaw C.W., Parnes J.R.;
"Two Lyt-2 polypeptides arise from a single gene by alternative
splicing patterns of mRNA.";
Cell 43:153-163(1985).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3495785; DOI=10.1093/nar/15.10.4337;
Nakauchi H., Tagawa M., Nolan G.P., Herzenberg L.A.;
"Isolation and characterization of the gene for the murine T cell
differentiation antigen and immunoglobulin-related molecule, Lyt-2.";
Nucleic Acids Res. 15:4337-4347(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C.AKR;
PubMed=3267233; DOI=10.1007/BF00364233;
Youn H.J., Harriss J.V., Gottlieb P.D.;
"Nucleotide sequence analysis of the C.AKR Lyt-2a gene: structural
polymorphism in alleles encoding the Lyt-2.1 T-cell surface
alloantigen.";
Immunogenetics 28:345-352(1988).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3487583;
Liaw C.W., Zamoyska R., Parnes J.R.;
"Structure, sequence, and polymorphism of the Lyt-2 T cell
differentiation antigen gene.";
J. Immunol. 137:1037-1043(1986).
[6]
PHOSPHORYLATION.
PubMed=2512251;
DiSanto J.P., Klein J.S., Flomenberg N.;
"Phosphorylation and down-regulation of CD4 and CD8 in human CTLs and
mouse L cells.";
Immunogenetics 30:494-501(1989).
[7]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=1673361;
Fung-Leung W.P., Schilham M.W., Rahemtulla A., Kuendig T.M.,
Vollenweider M., Potter J., van Ewijk W., Mak T.W.;
"CD8 is needed for development of cytotoxic T cells but not helper T
cells.";
Cell 65:443-449(1991).
[8]
FUNCTION.
PubMed=15105501; DOI=10.1126/science.1092316;
Madakamutil L.T., Christen U., Lena C.J., Wang-Zhu Y., Attinger A.,
Sundarrajan M., Ellmeier W., von Herrath M.G., Jensen P.,
Littman D.R., Cheroutre H.;
"CD8alphaalpha-mediated survival and differentiation of CD8 memory T
cell precursors.";
Science 304:590-593(2004).
[9]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 28-152 IN COMPLEX WITH H-2KB.
PubMed=9806638; DOI=10.1016/S1074-7613(00)80635-4;
Kern P.S., Teng M.K., Smolyar A., Liu J.H., Liu J., Hussey R.E.,
Spoerl R., Chang H.-C., Reinherz E.L., Wang J.-H.;
"Structural basis of CD8 coreceptor function revealed by
crystallographic analysis of a murine CD8alphaalpha ectodomain
fragment in complex with H-2Kb.";
Immunity 9:519-530(1998).
[10]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 28-151 IN COMPLEX WITH CD8B
AND ANTIBODY, SUBUNIT, DISULFIDE BOND, AND GLYCOSYLATION AT ASN-69.
PubMed=18929574; DOI=10.1016/j.jmb.2008.09.069;
Shore D.A., Issafras H., Landais E., Teyton L., Wilson I.A.;
"The crystal structure of CD8 in complex with YTS156.7.7 Fab and
interaction with other CD8 antibodies define the binding mode of CD8
alphabeta to MHC class I.";
J. Mol. Biol. 384:1190-1202(2008).
-!- 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,
ECO:0000269|PubMed:15105501, ECO:0000269|PubMed:1673361}.
-!- 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,
ECO:0000269|PubMed:18929574, ECO:0000269|PubMed:9806638}.
-!- INTERACTION:
P06240:Lck; NbExp=2; IntAct=EBI-1433, EBI-1401;
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. Alternative splicing
involves excision of the transmembrane or cytoplasmic domains.;
Name=1;
IsoId=P01731-1; Sequence=Displayed;
-!- PTM: Palmitoylated, but association with CD8B seems to be more
important for the enrichment of CdD8A in lipid rafts.
{ECO:0000250|UniProtKB:P01732}.
-!- PTM: Phosphorylated in cytotoxic T-lymphocytes (CTLs) following
activation. {ECO:0000269|PubMed:2512251}.
-!- DISRUPTION PHENOTYPE: Cd8a-deficient mice prevent the development
of class I MHC restricted cytotoxic T-cells. However, maturation
of class II MHC restricted T-helper cells seems to be unaffected
by the absence of Cd8a. {ECO:0000269|PubMed:1673361}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M12825; AAA39476.1; -; mRNA.
EMBL; M16981; AAA39477.1; ALT_TERM; mRNA.
EMBL; M12052; AAA39478.1; -; mRNA.
EMBL; Y00157; CAA68352.2; -; Genomic_DNA.
EMBL; M22064; AAA39665.1; -; Genomic_DNA.
EMBL; M12977; AAA39475.1; -; Genomic_DNA.
EMBL; M12819; AAA39475.1; JOINED; Genomic_DNA.
EMBL; M12975; AAA39475.1; JOINED; Genomic_DNA.
EMBL; M12976; AAA39475.1; JOINED; Genomic_DNA.
CCDS; CCDS39507.1; -. [P01731-1]
PIR; A01998; RWMST2.
PIR; A29523; A29523.
PIR; A34954; A34954.
RefSeq; NP_001074579.1; NM_001081110.2. [P01731-1]
UniGene; Mm.1858; -.
PDB; 1BQH; X-ray; 2.80 A; G/H/I/K=28-156.
PDB; 1NEZ; X-ray; 2.10 A; G/H=28-149.
PDB; 2ARJ; X-ray; 2.88 A; Q/R=28-150.
PDB; 2ATP; X-ray; 2.40 A; A/C=28-149.
PDB; 3B9K; X-ray; 2.70 A; A/E=28-151.
PDB; 3DMM; X-ray; 2.60 A; C=23-188.
PDBsum; 1BQH; -.
PDBsum; 1NEZ; -.
PDBsum; 2ARJ; -.
PDBsum; 2ATP; -.
PDBsum; 3B9K; -.
PDBsum; 3DMM; -.
ProteinModelPortal; P01731; -.
SMR; P01731; -.
IntAct; P01731; 4.
MINT; MINT-7895757; -.
STRING; 10090.ENSMUSP00000068123; -.
PhosphoSitePlus; P01731; -.
EPD; P01731; -.
MaxQB; P01731; -.
PaxDb; P01731; -.
PRIDE; P01731; -.
Ensembl; ENSMUST00000066747; ENSMUSP00000068123; ENSMUSG00000053977. [P01731-1]
GeneID; 12525; -.
KEGG; mmu:12525; -.
UCSC; uc009cgr.1; mouse. [P01731-1]
CTD; 925; -.
MGI; MGI:88346; Cd8a.
eggNOG; ENOG410IWN3; Eukaryota.
eggNOG; ENOG410Z6EI; LUCA.
GeneTree; ENSGT00510000048935; -.
HOGENOM; HOG000004794; -.
HOVERGEN; HBG008488; -.
InParanoid; P01731; -.
KO; K06458; -.
OMA; RVCKCPR; -.
OrthoDB; EOG091G0YIT; -.
PhylomeDB; P01731; -.
TreeFam; TF336070; -.
EvolutionaryTrace; P01731; -.
PRO; PR:P01731; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000053977; -.
CleanEx; MM_CD8A; -.
ExpressionAtlas; P01731; baseline and differential.
Genevisible; P01731; MM.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0044853; C:plasma membrane raft; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
GO; GO:0045065; P:cytotoxic T cell differentiation; IMP:MGI.
GO; GO:0051607; P:defense response to virus; IDA:MGI.
GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IDA:MGI.
GO; GO:0002456; P:T cell mediated immunity; IMP:MGI.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR015468; CD8_asu.
InterPro; IPR007110; Ig-like_dom.
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; Alternative splicing; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein; Immunity;
Immunoglobulin domain; Lipoprotein; Membrane; Palmitate;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 27
CHAIN 28 247 T-cell surface glycoprotein CD8 alpha
chain.
/FTId=PRO_0000014639.
TOPO_DOM 28 196 Extracellular. {ECO:0000255}.
TRANSMEM 197 217 Helical. {ECO:0000255}.
TOPO_DOM 218 247 Cytoplasmic. {ECO:0000255}.
DOMAIN 28 139 Ig-like V-type.
CARBOHYD 69 69 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18929574}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
CARBOHYD 150 150 N-linked (GlcNAc...) asparagine.
DISULFID 53 129 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:18929574}.
VARIANT 105 105 M -> V (in strain: C.AKR).
CONFLICT 81 81 Missing (in Ref. 3; AAA39477/CAA68352).
{ECO:0000305}.
STRAND 33 39 {ECO:0000244|PDB:1NEZ}.
STRAND 41 43 {ECO:0000244|PDB:1NEZ}.
STRAND 49 57 {ECO:0000244|PDB:1NEZ}.
STRAND 63 71 {ECO:0000244|PDB:1NEZ}.
STRAND 78 83 {ECO:0000244|PDB:1NEZ}.
STRAND 85 87 {ECO:0000244|PDB:1NEZ}.
STRAND 90 92 {ECO:0000244|PDB:1NEZ}.
TURN 94 97 {ECO:0000244|PDB:1NEZ}.
HELIX 98 100 {ECO:0000244|PDB:1NEZ}.
STRAND 102 107 {ECO:0000244|PDB:1NEZ}.
TURN 108 110 {ECO:0000244|PDB:1NEZ}.
STRAND 111 118 {ECO:0000244|PDB:1NEZ}.
HELIX 121 123 {ECO:0000244|PDB:1NEZ}.
STRAND 125 133 {ECO:0000244|PDB:1NEZ}.
STRAND 136 139 {ECO:0000244|PDB:1NEZ}.
STRAND 143 147 {ECO:0000244|PDB:1NEZ}.
SEQUENCE 247 AA; 27456 MW; 22D0D78ECEC3EA04 CRC64;
MASPLTRFLS LNLLLLGESI ILGSGEAKPQ APELRIFPKK MDAELGQKVD LVCEVLGSVS
QGCSWLFQNS SSKLPQPTFV VYMASSHNKI TWDEKLNSSK LFSAMRDTNN KYVLTLNKFS
KENEGYYFCS VISNSVMYFS SVVPVLQKVN STTTKPVLRT PSPVHPTGTS QPQRPEDCRP
RGSVKGTGLD FACDIYIWAP LAGICVALLL SLIITLICYH RSRKRVCKCP RPLVRQEGKP
RPSEKIV


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