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T-cell surface glycoprotein CD8 beta chain (Lymphocyte antigen 3) (T-cell membrane glycoprotein Ly-3) (T-cell surface glycoprotein Lyt-3) (CD antigen CD8b)

 CD8B_MOUSE              Reviewed;         213 AA.
P10300; Q31127; Q60966; Q61811;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
12-SEP-2018, entry version 168.
RecName: Full=T-cell surface glycoprotein CD8 beta chain;
AltName: Full=Lymphocyte antigen 3;
AltName: Full=T-cell membrane glycoprotein Ly-3;
AltName: Full=T-cell surface glycoprotein Lyt-3;
AltName: CD_antigen=CD8b;
Flags: Precursor;
Name=Cd8b; Synonyms=Cd8b1, Ly-3, Lyt-3, Lyt3;
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].
PubMed=2452747; DOI=10.1002/eji.1830180419;
Blanc D., Bron C., Gabert J., Letourneur F., McDonald H.R.,
Malissen B.;
"Gene transfer of the Ly-3 chain gene of the mouse CD8 molecular
complex: co-transfer with the Ly-2 polypeptide gene results in
detectable cell surface expression of the Ly-3 antigenic
determinants.";
Eur. J. Immunol. 18:613-619(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3258885;
Gorman S.D., Sun Y.H., Zamoyska R., Parnes J.R.;
"Molecular linkage of the Ly-3 and Ly-2 genes. Requirement of Ly-2 for
Ly-3 surface expression.";
J. Immunol. 140:3646-3653(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2784466;
Nakayama K., Shinkai Y., Okumura K., Nakauchi H.;
"Isolation and characterization of the mouse CD8 beta-chain (Ly-3)
genes. Absence of an intervening sequence between V- and J-like gene
segments.";
J. Immunol. 142:2540-2546(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3035575; DOI=10.1073/pnas.84.12.4210;
Nakauchi H., Shinkai Y., Okumura K.;
"Molecular cloning of Lyt-3, a membrane glycoprotein marking a subset
of mouse T lymphocytes: molecular homology to immunoglobulin and T-
cell receptor variable and joining regions.";
Proc. Natl. Acad. Sci. U.S.A. 84:4210-4214(1987).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=3498943; DOI=10.1073/pnas.84.19.6874;
Panaccio M., Gillespie M.T., Walker I.D., Kirszbaum L., Sharpe J.A.,
Tobias G.H., McKenzie I.F.C., Deacon N.J.;
"Molecular characterization of the murine cytotoxic T-cell membrane
glycoprotein Ly-3 (CD8).";
Proc. Natl. Acad. Sci. U.S.A. 84:6874-6878(1987).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE LYT-3-ALPHA).
STRAIN=NOD; TISSUE=Spleen, and Thymus;
PubMed=8537123;
Johnson-Tardieu J.M., Walworth E.W., Cornelius J.G., Ye X.,
Schuster S.M., Peck A.B.;
"Autoimmune diabetes-prone NOD mice express the Lyt2 alpha (Lyt2.1)
and Lyt3 alpha (Lyt3.1) alleles of CD8.";
Immunogenetics 43:6-12(1996).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE LYT-3A).
STRAIN=C.AKR; TISSUE=Liver;
PubMed=3169881; DOI=10.1007/BF00364234;
Youn H.J., Harriss J.V., Gottlieb P.D.;
"Structure and expression of the Lyt-3a gene of C.AKR mice.";
Immunogenetics 28:353-361(1988).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 205-213.
STRAIN=BALB/cJ; TISSUE=Thymus;
Deacon N.J.;
Submitted (JUN-1988) to the EMBL/GenBank/DDBJ databases.
[9]
FUNCTION.
PubMed=8108731;
Nakayama K., Nakayama K., Negishi I., Kuida K., Louie M.C.,
Kanagawa O., Nakauchi H., Loh D.Y.;
"Requirement for CD8 beta chain in positive selection of CD8-lineage T
cells.";
Science 263:1131-1133(1994).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=8064243;
Fung-Leung W.P., Kuendig T.M., Ngo K., Panakos J.,
De Sousa-Hitzler J., Wang E., Ohashi P.S., Mak T.W., Lau C.Y.;
"Reduced thymic maturation but normal effector function of CD8+ T
cells in CD8 beta gene-targeted mice.";
J. Exp. Med. 180:959-967(1994).
[11]
FUNCTION, AND INTERACTION WITH CD3D.
PubMed=12215456; DOI=10.1074/jbc.M208119200;
Doucey M.A., Goffin L., Naeher D., Michielin O., Baumgaertner P.,
Guillaume P., Palmer E., Luescher I.F.;
"CD3 delta establishes a functional link between the T cell receptor
and CD8.";
J. Biol. Chem. 278:3257-3264(2003).
[12]
DISRUPTION PHENOTYPE.
PubMed=19088062; DOI=10.1093/intimm/dxn130;
Angelov G.S., Guillaume P., Luescher I.F.;
"CD8beta knockout mice mount normal anti-viral CD8+ T cell responses
-- but why?";
Int. Immunol. 21:123-135(2009).
[13]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 22-136 IN COMPLEX WITH CD8A,
DISULFIDE BOND, AND SUBUNIT.
PubMed=16356863; DOI=10.1016/j.immuni.2005.11.002;
Chang H.C., Tan K., Ouyang J., Parisini E., Liu J.H., Le Y., Wang X.,
Reinherz E.L., Wang J.H.;
"Structural and mutational analyses of a CD8alphabeta heterodimer and
comparison with the CD8alphaalpha homodimer.";
Immunity 23:661-671(2005).
[14]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-138 IN COMPLEX WITH CD8A
AND ANTIBODY, SUBUNIT, AND DISULFIDE BOND.
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. A
palmitoylation site in the cytoplasmic tail of CD8B chain
contributes to partitioning of CD8 into the plasma membrane lipid
rafts where signaling proteins are enriched. Once LCK recruited,
it initiates different intracellular signaling pathways by
phosphorylating various substrates ultimately leading to
lymphokine production, motility, adhesion and activation of
cytotoxic T-lymphocytes (CTLs). Additionally, plays a critical
role in thymic selection of CD8+ T-cells.
{ECO:0000250|UniProtKB:P10966, ECO:0000269|PubMed:12215456,
ECO:0000269|PubMed:8064243, ECO:0000269|PubMed:8108731}.
-!- SUBUNIT: Forms disulfide-linked heterodimers with CD8A at the cell
surface. Interacts with CD3D; this interaction couples TCR-CD3
with CD8. Interacts with LCK. {ECO:0000250|UniProtKB:P10966,
ECO:0000269|PubMed:12215456, ECO:0000269|PubMed:16356863,
ECO:0000269|PubMed:18929574}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P10966};
Single-pass type I membrane protein. Note=Requires the partner
CD8A for efficient cell surface expression. The heterodimer
CD8A/CD8B localizes to lipid rafts due to CD8B cytoplasmic tail
palmitoylation. {ECO:0000250|UniProtKB:P10966}.
-!- PTM: Palmitoylated at the cytoplasmic tail and thereby targets the
heterodimer CD8A/CD8B to lipid rafts unlike CD8A homodimers.
{ECO:0000250|UniProtKB:P10966}.
-!- DISRUPTION PHENOTYPE: The lack of Cd8b reduces but does not
completely abolish thymic maturation of CD8+ T-cells. However,
Cd8-depleted mice mount normal primary cytotoxic CD8 responses
upon acute viral infections. {ECO:0000269|PubMed:19088062,
ECO:0000269|PubMed:8064243}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X07698; CAA30537.1; -; mRNA.
EMBL; M19504; AAA39454.1; -; mRNA.
EMBL; M26446; AAA39456.1; -; Genomic_DNA.
EMBL; M26441; AAA39456.1; JOINED; Genomic_DNA.
EMBL; M26442; AAA39456.1; JOINED; Genomic_DNA.
EMBL; M26443; AAA39456.1; JOINED; Genomic_DNA.
EMBL; M26444; AAA39456.1; JOINED; Genomic_DNA.
EMBL; M26445; AAA39456.1; JOINED; Genomic_DNA.
EMBL; M16799; AAA39479.1; -; mRNA.
EMBL; M17534; AAA39455.1; -; mRNA.
EMBL; U34882; AAA92534.1; -; mRNA.
EMBL; M22070; AAA39480.1; -; Genomic_DNA.
EMBL; M22065; AAA39480.1; JOINED; Genomic_DNA.
EMBL; M22066; AAA39480.1; JOINED; Genomic_DNA.
EMBL; M22067; AAA39480.1; JOINED; Genomic_DNA.
EMBL; M22068; AAA39480.1; JOINED; Genomic_DNA.
EMBL; M22069; AAA39480.1; JOINED; Genomic_DNA.
EMBL; X07997; CAA30803.1; -; mRNA.
CCDS; CCDS39506.1; -.
PIR; A30585; A30585.
RefSeq; NP_033988.1; NM_009858.2.
UniGene; Mm.333148; -.
PDB; 2ATP; X-ray; 2.40 A; B/D=22-136.
PDB; 3B9K; X-ray; 2.70 A; B/F=22-138.
PDB; 3DMM; X-ray; 2.60 A; D=19-168.
PDBsum; 2ATP; -.
PDBsum; 3B9K; -.
PDBsum; 3DMM; -.
ProteinModelPortal; P10300; -.
SMR; P10300; -.
IntAct; P10300; 3.
MINT; P10300; -.
STRING; 10090.ENSMUSP00000070131; -.
iPTMnet; P10300; -.
PhosphoSitePlus; P10300; -.
SwissPalm; P10300; -.
EPD; P10300; -.
PaxDb; P10300; -.
PRIDE; P10300; -.
Ensembl; ENSMUST00000065248; ENSMUSP00000070131; ENSMUSG00000053044.
GeneID; 12526; -.
KEGG; mmu:12526; -.
UCSC; uc009cgp.1; mouse.
CTD; 12526; -.
MGI; MGI:88347; Cd8b1.
eggNOG; ENOG410IY5X; Eukaryota.
eggNOG; ENOG410ZF37; LUCA.
GeneTree; ENSGT00510000048998; -.
HOGENOM; HOG000008681; -.
HOVERGEN; HBG105700; -.
InParanoid; P10300; -.
KO; K06459; -.
OMA; MRIYWLR; -.
OrthoDB; EOG091G0T5W; -.
PhylomeDB; P10300; -.
TreeFam; TF338028; -.
Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
EvolutionaryTrace; P10300; -.
PRO; PR:P10300; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000053044; Expressed in 47 organ(s), highest expression level in thymus.
CleanEx; MM_CD8B1; -.
ExpressionAtlas; P10300; baseline and differential.
Genevisible; P10300; 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:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
Gene3D; 2.60.40.10; -; 1.
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.
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; Complete proteome; Disulfide bond;
Glycoprotein; Immunity; Immunoglobulin domain; Membrane; Polymorphism;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 21
CHAIN 22 213 T-cell surface glycoprotein CD8 beta
chain.
/FTId=PRO_0000014644.
TOPO_DOM 22 175 Extracellular. {ECO:0000255}.
TRANSMEM 176 196 Helical. {ECO:0000255}.
TOPO_DOM 197 213 Cytoplasmic. {ECO:0000255}.
DOMAIN 22 133 Ig-like V-type.
CARBOHYD 34 34 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 41 117 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:16356863,
ECO:0000269|PubMed:18929574}.
VARIANT 98 98 R -> S (in allele Lyt-3A).
VARIANT 122 200 Missing (in allele Lyt-3-alpha).
STRAND 22 25 {ECO:0000244|PDB:2ATP}.
STRAND 27 31 {ECO:0000244|PDB:2ATP}.
STRAND 37 43 {ECO:0000244|PDB:2ATP}.
STRAND 49 59 {ECO:0000244|PDB:2ATP}.
STRAND 60 63 {ECO:0000244|PDB:3B9K}.
STRAND 64 73 {ECO:0000244|PDB:2ATP}.
TURN 74 76 {ECO:0000244|PDB:2ATP}.
STRAND 77 80 {ECO:0000244|PDB:2ATP}.
HELIX 82 84 {ECO:0000244|PDB:2ATP}.
TURN 85 87 {ECO:0000244|PDB:2ATP}.
STRAND 90 94 {ECO:0000244|PDB:2ATP}.
STRAND 97 99 {ECO:0000244|PDB:2ATP}.
STRAND 101 104 {ECO:0000244|PDB:2ATP}.
HELIX 109 111 {ECO:0000244|PDB:2ATP}.
STRAND 113 120 {ECO:0000244|PDB:2ATP}.
STRAND 125 127 {ECO:0000244|PDB:2ATP}.
STRAND 131 135 {ECO:0000244|PDB:2ATP}.
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


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