CD8B_MOUSE
ID CD8B_MOUSE Reviewed; 213 AA.
AC P10300; Q31127; Q60966; Q61811;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=T-cell surface glycoprotein CD8 beta chain;
DE AltName: Full=Lymphocyte antigen 3;
DE AltName: Full=T-cell membrane glycoprotein Ly-3;
DE AltName: Full=T-cell surface glycoprotein Lyt-3;
DE AltName: CD_antigen=CD8b;
DE Flags: Precursor;
GN Name=Cd8b; Synonyms=Cd8b1, Ly-3, Lyt-3, Lyt3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2452747; DOI=10.1002/eji.1830180419;
RA Blanc D., Bron C., Gabert J., Letourneur F., McDonald H.R., Malissen B.;
RT "Gene transfer of the Ly-3 chain gene of the mouse CD8 molecular complex:
RT co-transfer with the Ly-2 polypeptide gene results in detectable cell
RT surface expression of the Ly-3 antigenic determinants.";
RL Eur. J. Immunol. 18:613-619(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3258885;
RA Gorman S.D., Sun Y.H., Zamoyska R., Parnes J.R.;
RT "Molecular linkage of the Ly-3 and Ly-2 genes. Requirement of Ly-2 for Ly-3
RT surface expression.";
RL J. Immunol. 140:3646-3653(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2784466;
RA Nakayama K., Shinkai Y., Okumura K., Nakauchi H.;
RT "Isolation and characterization of the mouse CD8 beta-chain (Ly-3) genes.
RT Absence of an intervening sequence between V- and J-like gene segments.";
RL J. Immunol. 142:2540-2546(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3035575; DOI=10.1073/pnas.84.12.4210;
RA Nakauchi H., Shinkai Y., Okumura K.;
RT "Molecular cloning of Lyt-3, a membrane glycoprotein marking a subset of
RT mouse T lymphocytes: molecular homology to immunoglobulin and T-cell
RT receptor variable and joining regions.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:4210-4214(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=3498943; DOI=10.1073/pnas.84.19.6874;
RA Panaccio M., Gillespie M.T., Walker I.D., Kirszbaum L., Sharpe J.A.,
RA Tobias G.H., McKenzie I.F.C., Deacon N.J.;
RT "Molecular characterization of the murine cytotoxic T-cell membrane
RT glycoprotein Ly-3 (CD8).";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6874-6878(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE LYT-3-ALPHA).
RC STRAIN=NOD; TISSUE=Spleen, and Thymus;
RX PubMed=8537123; DOI=10.1007/bf00186598;
RA Johnson-Tardieu J.M., Walworth E.W., Cornelius J.G., Ye X., Schuster S.M.,
RA Peck A.B.;
RT "Autoimmune diabetes-prone NOD mice express the Lyt2 alpha (Lyt2.1) and
RT Lyt3 alpha (Lyt3.1) alleles of CD8.";
RL Immunogenetics 43:6-12(1996).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE LYT-3A).
RC STRAIN=C.AKR; TISSUE=Liver;
RX PubMed=3169881; DOI=10.1007/bf00364234;
RA Youn H.J., Harriss J.V., Gottlieb P.D.;
RT "Structure and expression of the Lyt-3a gene of C.AKR mice.";
RL Immunogenetics 28:353-361(1988).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 205-213.
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RA Deacon N.J.;
RL Submitted (JUN-1988) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION.
RX PubMed=8108731; DOI=10.1126/science.8108731;
RA Nakayama K., Nakayama K., Negishi I., Kuida K., Louie M.C., Kanagawa O.,
RA Nakauchi H., Loh D.Y.;
RT "Requirement for CD8 beta chain in positive selection of CD8-lineage T
RT cells.";
RL Science 263:1131-1133(1994).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8064243; DOI=10.1084/jem.180.3.959;
RA Fung-Leung W.P., Kuendig T.M., Ngo K., Panakos J., De Sousa-Hitzler J.,
RA Wang E., Ohashi P.S., Mak T.W., Lau C.Y.;
RT "Reduced thymic maturation but normal effector function of CD8+ T cells in
RT CD8 beta gene-targeted mice.";
RL J. Exp. Med. 180:959-967(1994).
RN [11]
RP FUNCTION, AND INTERACTION WITH CD3D.
RX PubMed=12215456; DOI=10.1074/jbc.m208119200;
RA Doucey M.A., Goffin L., Naeher D., Michielin O., Baumgaertner P.,
RA Guillaume P., Palmer E., Luescher I.F.;
RT "CD3 delta establishes a functional link between the T cell receptor and
RT CD8.";
RL J. Biol. Chem. 278:3257-3264(2003).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=19088062; DOI=10.1093/intimm/dxn130;
RA Angelov G.S., Guillaume P., Luescher I.F.;
RT "CD8beta knockout mice mount normal anti-viral CD8+ T cell responses -- but
RT why?";
RL Int. Immunol. 21:123-135(2009).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 22-136 IN COMPLEX WITH CD8A,
RP DISULFIDE BOND, AND SUBUNIT.
RX PubMed=16356863; DOI=10.1016/j.immuni.2005.11.002;
RA Chang H.C., Tan K., Ouyang J., Parisini E., Liu J.H., Le Y., Wang X.,
RA Reinherz E.L., Wang J.H.;
RT "Structural and mutational analyses of a CD8alphabeta heterodimer and
RT comparison with the CD8alphaalpha homodimer.";
RL Immunity 23:661-671(2005).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-138 IN COMPLEX WITH CD8A AND
RP ANTIBODY, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=18929574; DOI=10.1016/j.jmb.2008.09.069;
RA Shore D.A., Issafras H., Landais E., Teyton L., Wilson I.A.;
RT "The crystal structure of CD8 in complex with YTS156.7.7 Fab and
RT interaction with other CD8 antibodies define the binding mode of CD8
RT alphabeta to MHC class I.";
RL J. Mol. Biol. 384:1190-1202(2008).
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. A
CC palmitoylation site in the cytoplasmic tail of CD8B chain contributes
CC to partitioning of CD8 into the plasma membrane lipid rafts where
CC signaling proteins are enriched. Once LCK recruited, it initiates
CC different intracellular signaling pathways by phosphorylating various
CC substrates ultimately leading to lymphokine production, motility,
CC adhesion and activation of cytotoxic T-lymphocytes (CTLs).
CC Additionally, plays a critical role in thymic selection of CD8+ T-
CC cells. {ECO:0000250|UniProtKB:P10966, ECO:0000269|PubMed:12215456,
CC ECO:0000269|PubMed:8064243, ECO:0000269|PubMed:8108731}.
CC -!- SUBUNIT: Forms disulfide-linked heterodimers with CD8A at the cell
CC surface. Interacts with CD3D; this interaction couples TCR-CD3 with
CC CD8. Interacts with LCK. {ECO:0000250|UniProtKB:P10966,
CC ECO:0000269|PubMed:12215456, ECO:0000269|PubMed:16356863,
CC ECO:0000269|PubMed:18929574}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P10966}; Single-
CC pass type I membrane protein. Note=Requires the partner CD8A for
CC efficient cell surface expression. The heterodimer CD8A/CD8B localizes
CC to lipid rafts due to CD8B cytoplasmic tail palmitoylation.
CC {ECO:0000250|UniProtKB:P10966}.
CC -!- PTM: Palmitoylated at the cytoplasmic tail and thereby targets the
CC heterodimer CD8A/CD8B to lipid rafts unlike CD8A homodimers.
CC {ECO:0000250|UniProtKB:P10966}.
CC -!- DISRUPTION PHENOTYPE: The lack of Cd8b reduces but does not completely
CC abolish thymic maturation of CD8+ T-cells. However, Cd8-depleted mice
CC mount normal primary cytotoxic CD8 responses upon acute viral
CC infections. {ECO:0000269|PubMed:19088062, ECO:0000269|PubMed:8064243}.
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DR EMBL; X07698; CAA30537.1; -; mRNA.
DR EMBL; M19504; AAA39454.1; -; mRNA.
DR EMBL; M26446; AAA39456.1; -; Genomic_DNA.
DR EMBL; M26441; AAA39456.1; JOINED; Genomic_DNA.
DR EMBL; M26442; AAA39456.1; JOINED; Genomic_DNA.
DR EMBL; M26443; AAA39456.1; JOINED; Genomic_DNA.
DR EMBL; M26444; AAA39456.1; JOINED; Genomic_DNA.
DR EMBL; M26445; AAA39456.1; JOINED; Genomic_DNA.
DR EMBL; M16799; AAA39479.1; -; mRNA.
DR EMBL; M17534; AAA39455.1; -; mRNA.
DR EMBL; U34882; AAA92534.1; -; mRNA.
DR EMBL; M22070; AAA39480.1; -; Genomic_DNA.
DR EMBL; M22065; AAA39480.1; JOINED; Genomic_DNA.
DR EMBL; M22066; AAA39480.1; JOINED; Genomic_DNA.
DR EMBL; M22067; AAA39480.1; JOINED; Genomic_DNA.
DR EMBL; M22068; AAA39480.1; JOINED; Genomic_DNA.
DR EMBL; M22069; AAA39480.1; JOINED; Genomic_DNA.
DR EMBL; X07997; CAA30803.1; -; mRNA.
DR CCDS; CCDS39506.1; -.
DR PIR; A30585; A30585.
DR RefSeq; NP_033988.1; NM_009858.2.
DR PDB; 2ATP; X-ray; 2.40 A; B/D=22-136.
DR PDB; 3B9K; X-ray; 2.70 A; B/F=22-138.
DR PDB; 3DMM; X-ray; 2.60 A; D=19-168.
DR PDBsum; 2ATP; -.
DR PDBsum; 3B9K; -.
DR PDBsum; 3DMM; -.
DR AlphaFoldDB; P10300; -.
DR SMR; P10300; -.
DR ComplexPortal; CPX-6702; CD8alpha-beta complex.
DR IntAct; P10300; 3.
DR MINT; P10300; -.
DR STRING; 10090.ENSMUSP00000070131; -.
DR GlyGen; P10300; 1 site.
DR iPTMnet; P10300; -.
DR PhosphoSitePlus; P10300; -.
DR SwissPalm; P10300; -.
DR EPD; P10300; -.
DR PaxDb; P10300; -.
DR PRIDE; P10300; -.
DR ProteomicsDB; 265633; -.
DR ABCD; P10300; 2 sequenced antibodies.
DR DNASU; 12526; -.
DR Ensembl; ENSMUST00000065248; ENSMUSP00000070131; ENSMUSG00000053044.
DR GeneID; 12526; -.
DR KEGG; mmu:12526; -.
DR UCSC; uc009cgp.1; mouse.
DR CTD; 12526; -.
DR MGI; MGI:88347; Cd8b1.
DR VEuPathDB; HostDB:ENSMUSG00000053044; -.
DR eggNOG; ENOG502SANQ; Eukaryota.
DR GeneTree; ENSGT00510000048998; -.
DR HOGENOM; CLU_089344_0_0_1; -.
DR InParanoid; P10300; -.
DR OMA; RLWLRIH; -.
DR OrthoDB; 1377095at2759; -.
DR PhylomeDB; P10300; -.
DR TreeFam; TF338028; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR BioGRID-ORCS; 12526; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Cd8b1; mouse.
DR EvolutionaryTrace; P10300; -.
DR PRO; PR:P10300; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P10300; protein.
DR Bgee; ENSMUSG00000053044; Expressed in thymus and 39 other tissues.
DR ExpressionAtlas; P10300; baseline and differential.
DR Genevisible; P10300; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0043235; C:receptor complex; IPI:ComplexPortal.
DR GO; GO:0015026; F:coreceptor activity; IEA:InterPro.
DR GO; GO:0042288; F:MHC class I protein binding; IEA:InterPro.
DR GO; GO:0002250; P:adaptive immune response; IC:ComplexPortal.
DR GO; GO:0050776; P:regulation of immune response; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR042414; CD8B.
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; PTHR11292; PTHR11292; 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; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT CHAIN 22..213
FT /note="T-cell surface glycoprotein CD8 beta chain"
FT /id="PRO_0000014644"
FT TOPO_DOM 22..175
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..133
FT /note="Ig-like V-type"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:16356863, ECO:0000269|PubMed:18929574"
FT VARIANT 98
FT /note="R -> S (in allele Lyt-3A)"
FT VARIANT 122..200
FT /note="Missing (in allele Lyt-3-alpha)"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:2ATP"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:2ATP"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:2ATP"
FT STRAND 49..59
FT /evidence="ECO:0007829|PDB:2ATP"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:3B9K"
FT STRAND 64..73
FT /evidence="ECO:0007829|PDB:2ATP"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:2ATP"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:2ATP"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:2ATP"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:2ATP"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:2ATP"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2ATP"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:2ATP"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:2ATP"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:2ATP"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:2ATP"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:2ATP"
SQ SEQUENCE 213 AA; 24288 MW; 138D2DCA43215BDB CRC64;
MQPWLWLVFS MKLAALWSSS ALIQTPSSLL VQTNHTAKMS CEVKSISKLT SIYWLRERQD
PKDKYFEFLA SWSSSKGVLY GESVDKKRNI ILESSDSRRP FLSIMNVKPE DSDFYFCATV
GSPKMVFGTG TKLTVVDVLP TTAPTKKTTL KMKKKKQCPF PHPETQKGLT CSLTTLSLLV
VCILLLLAFL GVAVYFYCVR RRARIHFMKQ FHK
