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T-cell surface glycoprotein CD3 epsilon chain (T-cell surface antigen T3/Leu-4 epsilon chain) (CD antigen CD3e)

 CD3E_MOUSE              Reviewed;         189 AA.
P22646;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
22-NOV-2017, entry version 155.
RecName: Full=T-cell surface glycoprotein CD3 epsilon chain;
AltName: Full=T-cell surface antigen T3/Leu-4 epsilon chain;
AltName: CD_antigen=CD3e;
Flags: Precursor;
Name=Cd3e;
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=3478717; DOI=10.1073/pnas.84.21.7649;
Gold D.P., Clevers H., Alarcon B., Dunlap S., Novotny J.,
Williams A.F., Terhorst C.;
"Evolutionary relationship between the T3 chains of the T-cell
receptor complex and the immunoglobulin supergene family.";
Proc. Natl. Acad. Sci. U.S.A. 84:7649-7653(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2973066; DOI=10.1073/pnas.85.22.8623;
Clevers H., Dunlap S., Saito H., Georgopoulos K., Wileman T.,
Terhorst C.;
"Characterization and expression of the murine CD3-epsilon gene.";
Proc. Natl. Acad. Sci. U.S.A. 85:8623-8627(1988).
[3]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9843989;
DeJarnette J.B., Sommers C.L., Huang K., Woodside K.J., Emmons R.,
Katz K., Shores E.W., Love P.E.;
"Specific requirement for CD3epsilon in T cell development.";
Proc. Natl. Acad. Sci. U.S.A. 95:14909-14914(1998).
[4]
FUNCTION.
PubMed=19956738; DOI=10.1371/journal.pbio.1000253;
Wang Y., Becker D., Vass T., White J., Marrack P., Kappler J.W.;
"A conserved CXXC motif in CD3epsilon is critical for T cell
development and TCR signaling.";
PLoS Biol. 7:E1000253-E1000253(2009).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
STRUCTURE BY NMR OF 22-100, AND DISULFIDE BONDS.
PubMed=11439187; DOI=10.1016/S0092-8674(01)00395-6;
Sun Z.J., Kim K.S., Wagner G., Reinherz E.L.;
"Mechanisms contributing to T cell receptor signaling and assembly
revealed by the solution structure of an ectodomain fragment of the
CD3 epsilon gamma heterodimer.";
Cell 105:913-923(2001).
[7]
FUNCTION, INTERACTION WITH NCK1, AND SUBCELLULAR LOCATION.
PubMed=24470497; DOI=10.4049/jimmunol.1203414;
Borroto A., Arellano I., Blanco R., Fuentes M., Orfao A., Dopfer E.P.,
Prouza M., Suchanek M., Schamel W.W., Alarcon B.;
"Relevance of Nck-CD3 epsilon interaction for T cell activation in
vivo.";
J. Immunol. 192:2042-2053(2014).
[8]
FUNCTION.
PubMed=24899501; DOI=10.4049/jimmunol.1400322;
Bettini M.L., Guy C., Dash P., Vignali K.M., Hamm D.E., Dobbins J.,
Gagnon E., Thomas P.G., Wucherpfennig K.W., Vignali D.A.;
"Membrane association of the CD3epsilon signaling domain is required
for optimal T cell development and function.";
J. Immunol. 193:258-267(2014).
-!- FUNCTION: Part of the TCR-CD3 complex present on T-lymphocyte cell
surface that plays an essential role in adaptive immune response.
When antigen presenting cells (APCs) activate T-cell receptor
(TCR), TCR-mediated signals are transmitted across the cell
membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3
chains contain immunoreceptor tyrosine-based activation motifs
(ITAMs) in their cytoplasmic domain. Upon TCR engagement, these
motifs become phosphorylated by Src family protein tyrosine
kinases LCK and FYN, resulting in the activation of downstream
signaling pathways. In addition of this role of signal
transduction in T-cell activation, CD3E plays an essential role in
correct T-cell developement (PubMed:19956738, PubMed:24899501).
Participates also in internalization and cell surface down-
regulation of TCR-CD3 complexes via endocytosis sequences present
in CD3E cytosolic region. {ECO:0000250|UniProtKB:P07766,
ECO:0000269|PubMed:19956738, ECO:0000269|PubMed:24470497,
ECO:0000269|PubMed:24899501, ECO:0000269|PubMed:9843989}.
-!- SUBUNIT: The TCR-CD3 complex is composed of a CD3D/CD3E and a
CD3G/CD3E heterodimers that preferentially associate with TCRalpha
and TCRbeta, respectively, to form TCRalpha/CD3E/CD3G and
TCRbeta/CD3G/CD3E trimers. In turn, the hexamer interacts with
CD3Z homodimer to form the TCR-CD3 complex. Alternatively,
TCRalpha and TCRbeta can be replaced by TCRgamma and TCRdelta.
Interacts with CD6. Interacts with NCK1 (PubMed:24470497).
{ECO:0000250|UniProtKB:P07766, ECO:0000269|PubMed:24470497}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24470497};
Single-pass type I membrane protein
{ECO:0000250|UniProtKB:P07766}.
-!- PTM: Phosphorylated on Tyr residues after T-cell receptor
triggering by LCK in association with CD4/CD8.
{ECO:0000250|UniProtKB:P07766}.
-!- DISRUPTION PHENOTYPE: Absence of CD3E leads to the complete
absence of mature T-cells. Thymocyte development is arrested at
the early double-negative (DN) stage.
{ECO:0000269|PubMed:9843989}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; J02990; AAA40296.1; -; mRNA.
EMBL; M23376; AAA72720.1; -; Genomic_DNA.
EMBL; M23370; AAA72720.1; JOINED; Genomic_DNA.
EMBL; M23371; AAA72720.1; JOINED; Genomic_DNA.
EMBL; M23372; AAA72720.1; JOINED; Genomic_DNA.
EMBL; M23373; AAA72720.1; JOINED; Genomic_DNA.
EMBL; M23374; AAA72720.1; JOINED; Genomic_DNA.
EMBL; M23375; AAA72720.1; JOINED; Genomic_DNA.
CCDS; CCDS23125.1; -.
PIR; A31348; A31348.
RefSeq; NP_031674.1; NM_007648.4.
RefSeq; XP_006510029.1; XM_006509966.3.
UniGene; Mm.210361; -.
PDB; 1JBJ; NMR; -; A=22-100.
PDB; 1XMW; NMR; -; A=22-100.
PDB; 2K4F; NMR; -; A=134-189.
PDB; 3R08; X-ray; 4.10 A; E=22-100.
PDBsum; 1JBJ; -.
PDBsum; 1XMW; -.
PDBsum; 2K4F; -.
PDBsum; 3R08; -.
ProteinModelPortal; P22646; -.
SMR; P22646; -.
BioGrid; 198596; 6.
CORUM; P22646; -.
IntAct; P22646; 3.
MINT; MINT-7895702; -.
STRING; 10090.ENSMUSP00000099896; -.
iPTMnet; P22646; -.
PhosphoSitePlus; P22646; -.
SwissPalm; P22646; -.
EPD; P22646; -.
MaxQB; P22646; -.
PaxDb; P22646; -.
PRIDE; P22646; -.
Ensembl; ENSMUST00000102832; ENSMUSP00000099896; ENSMUSG00000032093.
GeneID; 12501; -.
KEGG; mmu:12501; -.
UCSC; uc009pez.1; mouse.
CTD; 916; -.
MGI; MGI:88332; Cd3e.
eggNOG; ENOG410IYD1; Eukaryota.
eggNOG; ENOG41123JN; LUCA.
GeneTree; ENSGT00510000048592; -.
HOGENOM; HOG000290664; -.
HOVERGEN; HBG102121; -.
InParanoid; P22646; -.
KO; K06451; -.
OMA; QRGQNKE; -.
OrthoDB; EOG091G0PKE; -.
PhylomeDB; P22646; -.
TreeFam; TF335892; -.
Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-MMU-202424; Downstream TCR signaling.
Reactome; R-MMU-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-MMU-202430; Translocation of ZAP-70 to Immunological synapse.
Reactome; R-MMU-202433; Generation of second messenger molecules.
Reactome; R-MMU-389948; PD-1 signaling.
EvolutionaryTrace; P22646; -.
PRO; PR:P22646; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032093; -.
CleanEx; MM_CD3E; -.
ExpressionAtlas; P22646; baseline and differential.
Genevisible; P22646; MM.
GO; GO:0042105; C:alpha-beta T cell receptor complex; IDA:MGI.
GO; GO:0044297; C:cell body; IDA:ARUK-UCL.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0043197; C:dendritic spine; IDA:ARUK-UCL.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0001772; C:immunological synapse; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
GO; GO:0042101; C:T cell receptor complex; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
GO; GO:0004871; F:signal transducer activity; IDA:MGI.
GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0097190; P:apoptotic signaling pathway; IDA:MGI.
GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
GO; GO:0021549; P:cerebellum development; IMP:ARUK-UCL.
GO; GO:0016358; P:dendrite development; IMP:ARUK-UCL.
GO; GO:0046649; P:lymphocyte activation; IMP:MGI.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IDA:MGI.
GO; GO:0045060; P:negative thymic T cell selection; IDA:MGI.
GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IDA:MGI.
GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IDA:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:MGI.
GO; GO:0045086; P:positive regulation of interleukin-2 biosynthetic process; IDA:MGI.
GO; GO:0032753; P:positive regulation of interleukin-4 production; IDA:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0050870; P:positive regulation of T cell activation; IDA:MGI.
GO; GO:0002669; P:positive regulation of T cell anergy; IDA:MGI.
GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:MGI.
GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0031295; P:T cell costimulation; IGI:MGI.
GO; GO:0050852; P:T cell receptor signaling pathway; IDA:MGI.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR015484; CD3_esu/gsu/dsu.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
PANTHER; PTHR10570; PTHR10570; 1.
Pfam; PF02189; ITAM; 1.
SMART; SM00408; IGc2; 1.
SMART; SM00077; ITAM; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS51055; ITAM_1; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Cell membrane; Complete proteome;
Disulfide bond; Immunity; Immunoglobulin domain; Membrane;
Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 21
CHAIN 22 189 T-cell surface glycoprotein CD3 epsilon
chain.
/FTId=PRO_0000014609.
TOPO_DOM 23 108 Extracellular. {ECO:0000255}.
TRANSMEM 109 134 Helical. {ECO:0000255}.
TOPO_DOM 135 189 Cytoplasmic. {ECO:0000255}.
DOMAIN 23 99 Ig-like.
DOMAIN 160 187 ITAM. {ECO:0000255|PROSITE-
ProRule:PRU00379}.
MOD_RES 170 170 Phosphotyrosine.
{ECO:0000250|UniProtKB:P07766,
ECO:0000255|PROSITE-ProRule:PRU00379}.
MOD_RES 181 181 Phosphotyrosine.
{ECO:0000250|UniProtKB:P07766,
ECO:0000255|PROSITE-ProRule:PRU00379}.
DISULFID 42 83 {ECO:0000244|PDB:1JBJ,
ECO:0000269|PubMed:11439187}.
STRAND 30 34 {ECO:0000244|PDB:1JBJ}.
STRAND 37 41 {ECO:0000244|PDB:1JBJ}.
STRAND 51 54 {ECO:0000244|PDB:1JBJ}.
STRAND 57 59 {ECO:0000244|PDB:1JBJ}.
STRAND 65 71 {ECO:0000244|PDB:1JBJ}.
TURN 74 76 {ECO:0000244|PDB:1JBJ}.
STRAND 79 84 {ECO:0000244|PDB:1JBJ}.
STRAND 94 96 {ECO:0000244|PDB:1JBJ}.
TURN 135 137 {ECO:0000244|PDB:2K4F}.
HELIX 144 146 {ECO:0000244|PDB:2K4F}.
HELIX 168 170 {ECO:0000244|PDB:2K4F}.
HELIX 179 182 {ECO:0000244|PDB:2K4F}.
HELIX 183 185 {ECO:0000244|PDB:2K4F}.
TURN 186 188 {ECO:0000244|PDB:2K4F}.
SEQUENCE 189 AA; 21393 MW; 5CE92F784FA13B96 CRC64;
MRWNTFWGIL CLSLLAVGTC QDDAENIEYK VSISGTSVEL TCPLDSDENL KWEKNGQELP
QKHDKHLVLQ DFSEVEDSGY YVCYTPASNK NTYLYLKARV CEYCVEVDLT AVAIIIIVDI
CITLGLLMVI YYWSKNRKAK AKPVTRGTGA GSRPRGQNKE RPPPVPNPDY EPIRKGQRDL
YSGLNQRAV


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