CD8A_HUMAN
ID CD8A_HUMAN Reviewed; 235 AA.
AC P01732; B4DT80; D6W5M8; Q13970; Q4ZG17;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=T-cell surface glycoprotein CD8 alpha chain;
DE AltName: Full=T-lymphocyte differentiation antigen T8/Leu-2;
DE AltName: CD_antigen=CD8a;
DE Flags: Precursor;
GN Name=CD8A; Synonyms=MAL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3871356; DOI=10.1016/0092-8674(85)90138-2;
RA Littman D.R., Thomas Y., Maddon P.J., Chess L., Axel R.;
RT "The isolation and sequence of the gene encoding T8: a molecule defining
RT functional classes of T lymphocytes.";
RL Cell 40:237-246(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RX PubMed=3936473;
RA Parnes J.R., Sizer K.C., Sukhatme V.P., Hunkapiller T.;
RT "Structure of Leu-2/T8 as deduced from the sequence of a cDNA clone.";
RL Behring Inst. Mitt. 77:48-55(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3918796; DOI=10.1016/0092-8674(85)90207-7;
RA Sukhatme V.P., Sizer K.C., Vollmer A.C., Hunkapiller T., Parnes J.R.;
RT "The T cell differentiation antigen Leu-2/T8 is homologous to
RT immunoglobulin and T cell receptor variable regions.";
RL Cell 40:591-597(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2509342; DOI=10.1007/bf02425282;
RA Nakayama K., Tokito S., Okumura K., Nakauchi H.;
RT "Structure and expression of the gene encoding CD8 alpha chain (Leu-
RT 2/T8).";
RL Immunogenetics 30:393-397(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RX PubMed=2496167;
RA Norment A.M., Lonberg N., Lacy E., Littman D.R.;
RT "Alternatively spliced mRNA encodes a secreted form of human CD8 alpha.
RT Characterization of the human CD8 alpha gene.";
RL J. Immunol. 142:3312-3319(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Pericardium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE OF 168-235 (ISOFORMS 1 AND 2).
RX PubMed=2536941; DOI=10.1073/pnas.86.3.998;
RA Giblin P., Ledbetter J.A., Kavathas P.;
RT "A secreted form of the human lymphocyte cell surface molecule CD8 arises
RT from alternative splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:998-1002(1989).
RN [10]
RP SUBUNIT.
RX PubMed=6605969; DOI=10.1016/s0021-9258(17)43915-9;
RA Snow P.M., Terhorst C.;
RT "The T8 antigen is a multimeric complex of two distinct subunits on human
RT thymocytes but consists of homomultimeric forms on peripheral blood T
RT lymphocytes.";
RL J. Biol. Chem. 258:14675-14681(1983).
RN [11]
RP PHOSPHORYLATION.
RX PubMed=2512251; DOI=10.1007/bf02421181;
RA DiSanto J.P., Klein J.S., Flomenberg N.;
RT "Phosphorylation and down-regulation of CD4 and CD8 in human CTLs and mouse
RT L cells.";
RL Immunogenetics 30:494-501(1989).
RN [12]
RP INTERACTION WITH HLA-A*02:01.
RX PubMed=2784196; DOI=10.1038/338345a0;
RA Salter R.D., Norment A.M., Chen B.P., Clayberger C., Krensky A.M.,
RA Littman D.R., Parham P.;
RT "Polymorphism in the alpha 3 domain of HLA-A molecules affects binding to
RT CD8.";
RL Nature 338:345-347(1989).
RN [13]
RP GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=1460019; DOI=10.1016/s0021-9258(19)74024-1;
RA Pascale M.C., Erra M.C., Malagolini N., Serafini-Cessi F., Leone A.,
RA Bonatti S.;
RT "Post-translational processing of an O-glycosylated protein, the human CD8
RT glycoprotein, during the intracellular transport to the plasma membrane.";
RL J. Biol. Chem. 267:25196-25201(1992).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=7923932; DOI=10.1006/clin.1994.1195;
RA Schlesinger M., Chu F.N., Badamchian M., Jiang J.D., Roboz J.P.,
RA Goldstein A.L., Bekesi J.G.;
RT "A distinctive form of soluble CD8 is secreted by stimulated CD8+ cells in
RT HIV-1-infected and high-risk individuals.";
RL Clin. Immunol. Immunopathol. 73:252-260(1994).
RN [15]
RP SUBUNIT, AND INTERACTION WITH HLA-G.
RX PubMed=12853576; DOI=10.1073/pnas.1431057100;
RA Shiroishi M., Tsumoto K., Amano K., Shirakihara Y., Colonna M., Braud V.M.,
RA Allan D.S.J., Makadzange A., Rowland-Jones S., Willcox B.E., Jones E.Y.,
RA van der Merwe P.A., Kumagai I., Maenaka K.;
RT "Human inhibitory receptors Ig-like transcript 2 (ILT2) and ILT4 compete
RT with CD8 for MHC class I binding and bind preferentially to HLA-G.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8856-8861(2003).
RN [16]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16236125; DOI=10.1111/j.1365-2567.2005.02235.x;
RA Addison E.G., North J., Bakhsh I., Marden C., Haq S., Al-Sarraj S.,
RA Malayeri R., Wickremasinghe R.G., Davies J.K., Lowdell M.W.;
RT "Ligation of CD8alpha on human natural killer cells prevents activation-
RT induced apoptosis and enhances cytolytic activity.";
RL Immunology 116:354-361(2005).
RN [17]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=17678538; DOI=10.1186/1471-2172-8-12;
RA Gibbings D.J., Marcet-Palacios M., Sekar Y., Ng M.C., Befus A.D.;
RT "CD8 alpha is expressed by human monocytes and enhances Fc gamma R-
RT dependent responses.";
RL BMC Immunol. 8:12-12(2007).
RN [18]
RP SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-206, AND MUTAGENESIS OF
RP CYS-206.
RX PubMed=17341584; DOI=10.1074/jbc.m701027200;
RA Pang D.J., Hayday A.C., Bijlmakers M.J.;
RT "CD8 Raft localization is induced by its assembly into CD8alpha beta
RT heterodimers, Not CD8alpha alpha homodimers.";
RL J. Biol. Chem. 282:13884-13894(2007).
RN [19]
RP FUNCTION.
RX PubMed=23657257; DOI=10.1038/nature12110;
RA Zhu J., Peng T., Johnston C., Phasouk K., Kask A.S., Klock A., Jin L.,
RA Diem K., Koelle D.M., Wald A., Robins H., Corey L.;
RT "Immune surveillance by CD8alphaalpha+ skin-resident T cells in human
RT herpes virus infection.";
RL Nature 497:494-497(2013).
RN [20]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=26082771; DOI=10.3389/fmicb.2015.00557;
RA Schuster P., Thomann S., Werner M., Vollmer J., Schmidt B.;
RT "A subset of human plasmacytoid dendritic cells expresses CD8alpha upon
RT exposure to herpes simplex virus type 1.";
RL Front. Microbiol. 6:557-557(2015).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 22-135, AND DISULFIDE BOND.
RX PubMed=1547508; DOI=10.1016/0092-8674(92)90085-q;
RA Leahy D.J., Axel R., Hendrickson W.A.;
RT "Crystal structure of a soluble form of the human T cell coreceptor CD8 at
RT 2.6-A resolution.";
RL Cell 68:1145-1162(1992).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 22-141 IN COMPLEX WITH HLA-A/B2M
RP DIMER, AND DISULFIDE BOND.
RX PubMed=9177355; DOI=10.1038/42523;
RA Gao G.F., Tormo J., Gerth U.C., Wyer J.R., McMichael A.J., Stuart D.I.,
RA Bell J.I., Jones E.Y., Jakobsen B.K.;
RT "Crystal structure of the complex between human CD8alpha(alpha) and HLA-
RT A2.";
RL Nature 387:630-634(1997).
RN [23]
RP STRUCTURE BY NMR OF 209-227 IN COMPLEX WITH LCK.
RX PubMed=14500983; DOI=10.1126/science.1085643;
RA Kim P.W., Sun Z.Y., Blacklow S.C., Wagner G., Eck M.J.;
RT "A zinc clasp structure tethers Lck to T cell coreceptors CD4 and CD8.";
RL Science 301:1725-1728(2003).
RN [24]
RP VARIANT CD8 DEFICIENCY SER-111, AND MUTAGENESIS OF GLY-111.
RX PubMed=11435463; DOI=10.1172/jci10993;
RA de la Calle-Martin O., Hernandez M., Ordi J., Casamitjana N.,
RA Arostegui J.I., Caragol I., Ferrando M., Labrador M.,
RA Rodriguez-Sanchez J.L., Espanol T.;
RT "Familial CD8 deficiency due to a mutation in the CD8 alpha gene.";
RL J. Clin. Invest. 108:117-123(2001).
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:0000269|PubMed:16236125,
CC ECO:0000269|PubMed:17678538, ECO:0000269|PubMed:23657257,
CC ECO:0000269|PubMed:26082771}.
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. One HLA-A molecule (mainly via nonpolymorphic alpha-3
CC domain) interacts with one CD8A homodimer (via CDR-like loop)
CC (PubMed:2784196, PubMed:9177355). Interacts with LCK in a zinc-
CC dependent manner. Interacts with HLA-G; this interaction is direct and
CC might down-regulate T cell receptor signaling.
CC {ECO:0000269|PubMed:12853576, ECO:0000269|PubMed:14500983,
CC ECO:0000269|PubMed:2784196, ECO:0000269|PubMed:6605969,
CC ECO:0000269|PubMed:9177355}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:1460019, ECO:0000269|PubMed:17341584,
CC ECO:0000269|PubMed:17678538}; Single-pass type I membrane protein.
CC Note=CD8A localizes to lipid rafts only when associated with its
CC partner CD8B. {ECO:0000269|PubMed:17341584}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted
CC {ECO:0000269|PubMed:7923932}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=membrane, mCD8alpha;
CC IsoId=P01732-1; Sequence=Displayed;
CC Name=2; Synonyms=secreted, sCD8alpha;
CC IsoId=P01732-2; Sequence=VSP_012653;
CC Name=3;
CC IsoId=P01732-3; Sequence=VSP_054438;
CC -!- TISSUE SPECIFICITY: CD8 on thymus-derived T-cells usually consists of a
CC disulfide-linked alpha/CD8A and a beta/CD8B chain. Less frequently, CD8
CC can be expressed as a CD8A homodimer. A subset of natural killer cells,
CC memory T-cells, intraepithelial lymphocytes, monocytes and dendritic
CC cells expresses CD8A homodimers. Expressed at the cell surface of
CC plasmacytoid dendritic cells upon herpes simplex virus-1 stimulation.
CC {ECO:0000269|PubMed:16236125, ECO:0000269|PubMed:17678538,
CC ECO:0000269|PubMed:26082771}.
CC -!- PTM: Palmitoylated, but association with CD8B seems to be more
CC important for the enrichment of CD8A in lipid rafts.
CC {ECO:0000269|PubMed:17341584}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:1460019}.
CC -!- PTM: Phosphorylated in cytotoxic T-lymphocytes (CTLs) following
CC activation. {ECO:0000269|PubMed:2512251}.
CC -!- DISEASE: CD8 deficiency, familial (CD8 deficiency) [MIM:608957]: An
CC immunologic defect characterized by absence of CD8+ cells, leading to
CC recurrent bacterial infections. {ECO:0000269|PubMed:11435463}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- WEB RESOURCE: Name=CD8Abase; Note=CD8A mutation db;
CC URL="http://structure.bmc.lu.se/idbase/CD8Abase/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CD8 entry;
CC URL="https://en.wikipedia.org/wiki/CD8";
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DR EMBL; M26315; AAA79217.1; -; Genomic_DNA.
DR EMBL; M26313; AAA79217.1; JOINED; Genomic_DNA.
DR EMBL; M26314; AAA79217.1; JOINED; Genomic_DNA.
DR EMBL; M26315; AAA79218.1; -; Genomic_DNA.
DR EMBL; M26313; AAA79218.1; JOINED; Genomic_DNA.
DR EMBL; M26314; AAA79218.1; JOINED; Genomic_DNA.
DR EMBL; M12824; AAA61133.1; -; mRNA.
DR EMBL; M12828; AAB04637.1; -; mRNA.
DR EMBL; M27161; AAA59674.1; -; Genomic_DNA.
DR EMBL; AK300089; BAG61892.1; -; mRNA.
DR EMBL; AC064848; AAX88864.1; -; Genomic_DNA.
DR EMBL; AC112696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAW99438.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99439.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99440.1; -; Genomic_DNA.
DR CCDS; CCDS1992.1; -. [P01732-1]
DR CCDS; CCDS1993.1; -. [P01732-2]
DR PIR; A30604; RWHUT8.
DR RefSeq; NP_001139345.1; NM_001145873.1. [P01732-1]
DR RefSeq; NP_001759.3; NM_001768.6. [P01732-1]
DR RefSeq; NP_741969.1; NM_171827.3. [P01732-2]
DR PDB; 1AKJ; X-ray; 2.65 A; D/E=22-141.
DR PDB; 1CD8; X-ray; 2.60 A; A=22-135.
DR PDB; 1Q69; NMR; -; A=209-227.
DR PDB; 2HP4; X-ray; 2.10 A; A/B=22-135.
DR PDB; 3QZW; X-ray; 2.80 A; G/H/I/J=22-135.
DR PDBsum; 1AKJ; -.
DR PDBsum; 1CD8; -.
DR PDBsum; 1Q69; -.
DR PDBsum; 2HP4; -.
DR PDBsum; 3QZW; -.
DR AlphaFoldDB; P01732; -.
DR SMR; P01732; -.
DR BioGRID; 107363; 93.
DR ComplexPortal; CPX-6741; CD8alpha-beta complex.
DR ComplexPortal; CPX-6743; CD8alpha-alpha complex.
DR CORUM; P01732; -.
DR IntAct; P01732; 6.
DR STRING; 9606.ENSP00000386559; -.
DR GlyGen; P01732; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; P01732; -.
DR PhosphoSitePlus; P01732; -.
DR SwissPalm; P01732; -.
DR BioMuta; CD8A; -.
DR DMDM; 116035; -.
DR jPOST; P01732; -.
DR MassIVE; P01732; -.
DR PaxDb; P01732; -.
DR PeptideAtlas; P01732; -.
DR PRIDE; P01732; -.
DR ProteomicsDB; 5085; -.
DR ProteomicsDB; 51452; -. [P01732-1]
DR ProteomicsDB; 51453; -. [P01732-2]
DR ABCD; P01732; 1 sequenced antibody.
DR Antibodypedia; 3495; 5216 antibodies from 57 providers.
DR CPTC; P01732; 1 antibody.
DR DNASU; 925; -.
DR Ensembl; ENST00000283635.8; ENSP00000283635.3; ENSG00000153563.16. [P01732-1]
DR Ensembl; ENST00000352580.7; ENSP00000321631.3; ENSG00000153563.16. [P01732-2]
DR Ensembl; ENST00000409511.6; ENSP00000386559.2; ENSG00000153563.16. [P01732-1]
DR GeneID; 925; -.
DR KEGG; hsa:925; -.
DR MANE-Select; ENST00000283635.8; ENSP00000283635.3; NM_001768.7; NP_001759.3.
DR UCSC; uc002srt.4; human. [P01732-1]
DR CTD; 925; -.
DR DisGeNET; 925; -.
DR GeneCards; CD8A; -.
DR HGNC; HGNC:1706; CD8A.
DR HPA; ENSG00000153563; Tissue enriched (lymphoid).
DR MalaCards; CD8A; -.
DR MIM; 186910; gene.
DR MIM; 608957; phenotype.
DR neXtProt; NX_P01732; -.
DR OpenTargets; ENSG00000153563; -.
DR Orphanet; 169085; Susceptibility to respiratory infections associated with CD8alpha chain mutation.
DR PharmGKB; PA26244; -.
DR VEuPathDB; HostDB:ENSG00000153563; -.
DR eggNOG; ENOG502SAZN; Eukaryota.
DR GeneTree; ENSGT00940000156588; -.
DR HOGENOM; CLU_085753_0_0_1; -.
DR InParanoid; P01732; -.
DR OMA; FRMSPTQ; -.
DR PhylomeDB; P01732; -.
DR TreeFam; TF336070; -.
DR PathwayCommons; P01732; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; P01732; -.
DR SIGNOR; P01732; -.
DR BioGRID-ORCS; 925; 22 hits in 1066 CRISPR screens.
DR ChiTaRS; CD8A; human.
DR EvolutionaryTrace; P01732; -.
DR GeneWiki; CD8A; -.
DR GenomeRNAi; 925; -.
DR Pharos; P01732; Tbio.
DR PRO; PR:P01732; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P01732; protein.
DR Bgee; ENSG00000153563; Expressed in thymus and 135 other tissues.
DR ExpressionAtlas; P01732; baseline and differential.
DR Genevisible; P01732; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IPI:ComplexPortal.
DR GO; GO:0042101; C:T cell receptor complex; NAS:UniProtKB.
DR GO; GO:0015026; F:coreceptor activity; NAS:UniProtKB.
DR GO; GO:0042288; F:MHC class I protein binding; NAS:UniProtKB.
DR GO; GO:0023024; F:MHC class I protein complex binding; IDA:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IC:ComplexPortal.
DR GO; GO:0019882; P:antigen processing and presentation; NAS:UniProtKB.
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:0006955; P:immune response; NAS:UniProtKB.
DR GO; GO:0042110; P:T cell activation; IDA:ComplexPortal.
DR GO; GO:0002456; P:T cell mediated immunity; IBA:GO_Central.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:ComplexPortal.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; NAS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
KW Disease variant; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT CHAIN 22..235
FT /note="T-cell surface glycoprotein CD8 alpha chain"
FT /id="PRO_0000014638"
FT TOPO_DOM 22..182
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..135
FT /note="Ig-like V-type"
FT LIPID 206
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:17341584"
FT DISULFID 43..115
FT /evidence="ECO:0000269|PubMed:1547508,
FT ECO:0000269|PubMed:9177355"
FT VAR_SEQ 1
FT /note="M -> MRNQAPGRPKGATFPPRRPTGSRAPPLAPELRAKQRPGERVM (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054438"
FT VAR_SEQ 172..209
FT /note="VHTRGLDFACDIYIWAPLAGTCGVLLLSLVITLYCNHR -> G (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_012653"
FT VARIANT 111
FT /note="G -> S (in CD8 deficiency; prevents CD8 expression;
FT dbSNP:rs121918660)"
FT /evidence="ECO:0000269|PubMed:11435463"
FT /id="VAR_021020"
FT MUTAGEN 111
FT /note="G->R: Prevents CD8 expression."
FT /evidence="ECO:0000269|PubMed:11435463"
FT MUTAGEN 206
FT /note="C->A: Complete loss of palmitoylation."
FT /evidence="ECO:0000269|PubMed:17341584"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:2HP4"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:2HP4"
FT STRAND 54..64
FT /evidence="ECO:0007829|PDB:2HP4"
FT STRAND 68..77
FT /evidence="ECO:0007829|PDB:2HP4"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:2HP4"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:2HP4"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:2HP4"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2HP4"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:2HP4"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:2HP4"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2HP4"
SQ SEQUENCE 235 AA; 25729 MW; FCCA29BAA73726BB CRC64;
MALPVTALLL PLALLLHAAR PSQFRVSPLD RTWNLGETVE LKCQVLLSNP TSGCSWLFQP
RGAAASPTFL LYLSQNKPKA AEGLDTQRFS GKRLGDTFVL TLSDFRRENE GYYFCSALSN
SIMYFSHFVP VFLPAKPTTT PAPRPPTPAP TIASQPLSLR PEACRPAAGG AVHTRGLDFA
CDIYIWAPLA GTCGVLLLSL VITLYCNHRN RRRVCKCPRP VVKSGDKPSL SARYV
