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

 CD3E_HUMAN              Reviewed;         207 AA.
P07766; A8K997;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
22-NOV-2017, entry version 190.
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; Synonyms=T3E;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3012357; DOI=10.1038/321431a0;
Gold D.P., Puck J.M., Pettey C.L., Cho M., Coligan J., Woody J.N.,
Terhorst C.;
"Isolation of cDNA clones encoding the 20K non-glycosylated
polypeptide chain of the human T-cell receptor/T3 complex.";
Nature 321:431-434(1986).
[2]
SEQUENCE REVISION.
Terhorst C.;
Submitted (JAN-1987) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Blood;
PubMed=3267235; DOI=10.1073/pnas.85.21.8156;
Clevers H.C., Dunlap S., Wileman T.E., Terhorst C.;
"Human CD3-epsilon gene contains three miniexons and is transcribed
from a non-TATA promoter.";
Proc. Natl. Acad. Sci. U.S.A. 85:8156-8160(1988).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Blood;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, AND PHOSPHORYLATION BY LCK.
PubMed=2470098;
Barber E.K., Dasgupta J.D., Schlossman S.F., Trevillyan J.M.,
Rudd C.E.;
"The CD4 and CD8 antigens are coupled to a protein-tyrosine kinase
(p56lck) that phosphorylates the CD3 complex.";
Proc. Natl. Acad. Sci. U.S.A. 86:3277-3281(1989).
[8]
TISSUE SPECIFICITY.
PubMed=1387664;
Lanier L.L., Chang C., Spits H., Phillips J.H.;
"Expression of cytoplasmic CD3 epsilon proteins in activated human
adult natural killer (NK) cells and CD3 gamma, delta, epsilon
complexes in fetal NK cells. Implications for the relationship of NK
and T lymphocytes.";
J. Immunol. 149:1876-1880(1992).
[9]
INVOLVEMENT IN IMD18, AND FUNCTION.
PubMed=8490660; DOI=10.1038/ng0193-77;
Soudais C., de Villartay J.P., Le Deist F., Fischer A.,
Lisowska-Grospierre B.;
"Independent mutations of the human CD3-epsilon gene resulting in a T
cell receptor/CD3 complex immunodeficiency.";
Nat. Genet. 3:77-81(1993).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10384095;
Borroto A., Lama J., Niedergang F., Dautry-Varsat A., Alarcon B.,
Alcover A.;
"The CD3 epsilon subunit of the TCR contains endocytosis signals.";
J. Immunol. 163:25-31(1999).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=12522270; DOI=10.1073/pnas.2436191100;
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,
Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
"Profiling of tyrosine phosphorylation pathways in human cells using
mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[13]
INVOLVEMENT IN IMD18, AND FUNCTION.
PubMed=15546002; DOI=10.1172/JCI22588;
de Saint Basile G., Geissmann F., Flori E., Uring-Lambert B.,
Soudais C., Cavazzana-Calvo M., Durandy A., Jabado N., Fischer A.,
Le Deist F.;
"Severe combined immunodeficiency caused by deficiency in either the
delta or the epsilon subunit of CD3.";
J. Clin. Invest. 114:1512-1517(2004).
[14]
FUNCTION, INTERACTION WITH CD6, AND SUBCELLULAR LOCATION.
PubMed=15294938; DOI=10.4049/jimmunol.173.4.2262;
Gimferrer I., Calvo M., Mittelbrunn M., Farnos M., Sarrias M.R.,
Enrich C., Vives J., Sanchez-Madrid F., Lozano F.;
"Relevance of CD6-mediated interactions in T cell activation and
proliferation.";
J. Immunol. 173:2262-2270(2004).
[15]
INTERACTION WITH NCK1.
PubMed=15972658;
Szymczak A.L., Workman C.J., Gil D., Dilioglou S., Vignali K.M.,
Palmer E., Vignali D.A.;
"The CD3epsilon proline-rich sequence, and its interaction with Nck,
is not required for T cell development and function.";
J. Immunol. 175:270-275(2005).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-188, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-188, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
FUNCTION, INTERACTION WITH NUMB, AND REGION.
PubMed=26507128; DOI=10.1093/intimm/dxv060;
Martin-Blanco N., Jimenez Teja D., Bretones G., Borroto A.,
Caraballo M., Screpanti I., Leon J., Alarcon B., Canelles M.;
"CD3epsilon recruits Numb to promote TCR degradation.";
Int. Immunol. 28:127-137(2016).
[19]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 186-203 IN COMPLEX WITH SYK,
AND PHOSPHORYLATION AT TYR-188 AND TYR-199.
PubMed=9698567; DOI=10.1006/jmbi.1998.1964;
Fuetterer K., Wong J., Grucza R.A., Chan A.C., Waksman G.;
"Structural basis for Syk tyrosine kinase ubiquity in signal
transduction pathways revealed by the crystal structure of its
regulatory SH2 domains bound to a dually phosphorylated ITAM
peptide.";
J. Mol. Biol. 281:523-537(1998).
[20]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 21-118 IN COMPLEX WITH CD3G
AND ANTIBODY, SUBUNIT, AND DISULFIDE BOND.
PubMed=15136729; DOI=10.1073/pnas.0402295101;
Kjer-Nielsen L., Dunstone M.A., Kostenko L., Ely L.K., Beddoe T.,
Mifsud N.A., Purcell A.W., Brooks A.G., McCluskey J., Rossjohn J.;
"Crystal structure of the human T cell receptor CD3 epsilon gamma
heterodimer complexed to the therapeutic mAb OKT3.";
Proc. Natl. Acad. Sci. U.S.A. 101:7675-7680(2004).
[21]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 23-126 IN COMPLEX WITH CD3D
AND ANTIBODY FRAGMENT, SUBUNIT, AND DISULFIDE BOND.
PubMed=15534202; DOI=10.1073/pnas.0407359101;
Arnett K.L., Harrison S.C., Wiley D.C.;
"Crystal structure of a human CD3-epsilon/delta dimer in complex with
a UCHT1 single-chain antibody fragment.";
Proc. Natl. Acad. Sci. U.S.A. 101:16268-16273(2004).
-!- 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 (PubMed:2470098). In addition of this role of
signal transduction in T-cell activation, CD3E plays an essential
role in correct T-cell developement. Initiates the TCR-CD3 complex
assembly by forming the two heterodimers CD3D/CD3E and CD3G/CD3E.
Participates also in internalization and cell surface down-
regulation of TCR-CD3 complexes via endocytosis sequences present
in CD3E cytosolic region (PubMed:10384095, PubMed:26507128).
{ECO:0000269|PubMed:10384095, ECO:0000269|PubMed:15294938,
ECO:0000269|PubMed:15546002, ECO:0000269|PubMed:2470098,
ECO:0000269|PubMed:26507128, ECO:0000269|PubMed:8490660}.
-!- 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 (PubMed:15294938). Interacts with NCK1
(PubMed:15972658). Interacts with NUMB; this interaction is
important for TCR-CD3 internalization and subsequent degradation
(PubMed:26507128). {ECO:0000269|PubMed:15136729,
ECO:0000269|PubMed:15294938, ECO:0000269|PubMed:15534202,
ECO:0000269|PubMed:15972658, ECO:0000269|PubMed:26507128,
ECO:0000269|PubMed:9698567}.
-!- INTERACTION:
Q8TE68:EPS8L1; NbExp=6; IntAct=EBI-1211297, EBI-7487998;
P16333:NCK1; NbExp=6; IntAct=EBI-1211297, EBI-389883;
P43405:SYK; NbExp=6; IntAct=EBI-1211297, EBI-78302;
P43403:ZAP70; NbExp=3; IntAct=EBI-1211297, EBI-1211276;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10384095,
ECO:0000269|PubMed:15294938}; Single-pass type I membrane protein
{ECO:0000305}.
-!- PTM: Phosphorylated on Tyr residues after T-cell receptor
triggering by LCK in association with CD4/CD8.
{ECO:0000269|PubMed:2470098}.
-!- DISEASE: Immunodeficiency 18 (IMD18) [MIM:615615]: An autosomal
recessive primary immunodeficiency characterized by onset in
infancy or early childhood of recurrent infections. The severity
is variable, encompassing both a mild immunodeficiency and severe
combined immunodeficiency (SCID), resulting in early death without
bone marrow transplantation in some patients. Immunologic work-up
of the IMD18 SCID patients shows a T cell-negative, B cell-
positive, natural killer (NK) cell-positive phenotype, whereas T-
cell development is not impaired in the mild form of IMD18.
{ECO:0000269|PubMed:15546002, ECO:0000269|PubMed:8490660}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- WEB RESOURCE: Name=CD3Ebase; Note=CD3E mutation db;
URL="http://structure.bmc.lu.se/idbase/CD3Ebase/";
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EMBL; X03884; CAA27516.1; -; mRNA.
EMBL; M23323; AAA52295.1; -; Genomic_DNA.
EMBL; M23317; AAA52295.1; JOINED; Genomic_DNA.
EMBL; M23318; AAA52295.1; JOINED; Genomic_DNA.
EMBL; M23319; AAA52295.1; JOINED; Genomic_DNA.
EMBL; M23320; AAA52295.1; JOINED; Genomic_DNA.
EMBL; M23321; AAA52295.1; JOINED; Genomic_DNA.
EMBL; L34846; AAA52295.1; JOINED; Genomic_DNA.
EMBL; M23322; AAA52295.1; JOINED; Genomic_DNA.
EMBL; AK292612; BAF85301.1; -; mRNA.
EMBL; CH471065; EAW67364.1; -; Genomic_DNA.
EMBL; BC049847; AAH49847.1; -; mRNA.
CCDS; CCDS31685.1; -.
PIR; A32069; A32069.
RefSeq; NP_000724.1; NM_000733.3.
UniGene; Hs.3003; -.
PDB; 1A81; X-ray; 3.00 A; B/D/F/H/J/L=186-203.
PDB; 1SY6; X-ray; 2.10 A; A=21-118.
PDB; 1XIW; X-ray; 1.90 A; A/E=23-126.
PDB; 2ROL; NMR; -; B=181-192.
PDBsum; 1A81; -.
PDBsum; 1SY6; -.
PDBsum; 1XIW; -.
PDBsum; 2ROL; -.
DisProt; DP00506; -.
ProteinModelPortal; P07766; -.
SMR; P07766; -.
BioGrid; 107354; 25.
ELM; P07766; -.
IntAct; P07766; 16.
MINT; MINT-7213890; -.
STRING; 9606.ENSP00000354566; -.
ChEMBL; CHEMBL1975; -.
DrugBank; DB00075; Muromonab.
GuidetoPHARMACOLOGY; 2742; -.
iPTMnet; P07766; -.
PhosphoSitePlus; P07766; -.
BioMuta; CD3E; -.
DMDM; 1345708; -.
MaxQB; P07766; -.
PaxDb; P07766; -.
PeptideAtlas; P07766; -.
PRIDE; P07766; -.
DNASU; 916; -.
Ensembl; ENST00000361763; ENSP00000354566; ENSG00000198851.
GeneID; 916; -.
KEGG; hsa:916; -.
UCSC; uc001psq.5; human.
CTD; 916; -.
DisGeNET; 916; -.
EuPathDB; HostDB:ENSG00000198851.9; -.
GeneCards; CD3E; -.
HGNC; HGNC:1674; CD3E.
HPA; CAB000010; -.
HPA; CAB072863; -.
HPA; CAB072864; -.
HPA; HPA040957; -.
HPA; HPA043955; -.
MalaCards; CD3E; -.
MIM; 186830; gene.
MIM; 615615; phenotype.
neXtProt; NX_P07766; -.
OpenTargets; ENSG00000198851; -.
Orphanet; 169160; T-B+ severe combined immunodeficiency due to CD3delta/CD3epsilon/CD3zeta.
PharmGKB; PA26216; -.
eggNOG; ENOG410IYD1; Eukaryota.
eggNOG; ENOG41123JN; LUCA.
GeneTree; ENSGT00510000048592; -.
HOGENOM; HOG000290664; -.
HOVERGEN; HBG102121; -.
InParanoid; P07766; -.
KO; K06451; -.
OMA; QRGQNKE; -.
OrthoDB; EOG091G0PKE; -.
PhylomeDB; P07766; -.
TreeFam; TF335892; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse.
Reactome; R-HSA-202433; Generation of second messenger molecules.
Reactome; R-HSA-389948; PD-1 signaling.
SignaLink; P07766; -.
SIGNOR; P07766; -.
ChiTaRS; CD3E; human.
EvolutionaryTrace; P07766; -.
GeneWiki; T-cell_surface_glycoprotein_CD3_epsilon_chain; -.
GenomeRNAi; 916; -.
PRO; PR:P07766; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000198851; -.
CleanEx; HS_CD3E; -.
ExpressionAtlas; P07766; baseline and differential.
Genevisible; P07766; HS.
GO; GO:0042105; C:alpha-beta T cell receptor complex; IEA:Ensembl.
GO; GO:0044297; C:cell body; IEA:Ensembl.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0042101; C:T cell receptor complex; IDA:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IMP:CAFA.
GO; GO:0019901; F:protein kinase binding; NAS:UniProtKB.
GO; GO:0030159; F:receptor signaling complex scaffold activity; NAS:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
GO; GO:0005057; F:signal transducer activity, downstream of receptor; TAS:ProtInc.
GO; GO:0042608; F:T cell receptor binding; NAS:UniProtKB.
GO; GO:0004888; F:transmembrane signaling receptor activity; NAS:UniProtKB.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0007166; P:cell surface receptor signaling pathway; NAS:UniProtKB.
GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
GO; GO:0016358; P:dendrite development; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:Ensembl.
GO; GO:0045060; P:negative thymic T cell selection; IEA:Ensembl.
GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IEA:Ensembl.
GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0045086; P:positive regulation of interleukin-2 biosynthetic process; IEA:Ensembl.
GO; GO:0032753; P:positive regulation of interleukin-4 production; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
GO; GO:0002669; P:positive regulation of T cell anergy; IEA:Ensembl.
GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:UniProtKB.
GO; GO:0006461; P:protein complex assembly; NAS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IMP:CAFA.
GO; GO:0042981; P:regulation of apoptotic process; NAS:UniProtKB.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0007172; P:signal complex assembly; TAS:ProtInc.
GO; GO:0042110; P:T cell activation; NAS:UniProtKB.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR015484; CD3_esu/gsu/dsu.
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; 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 22
CHAIN 23 207 T-cell surface glycoprotein CD3 epsilon
chain.
/FTId=PRO_0000014607.
TOPO_DOM 23 126 Extracellular. {ECO:0000255}.
TRANSMEM 127 152 Helical. {ECO:0000255}.
TOPO_DOM 153 207 Cytoplasmic. {ECO:0000255}.
DOMAIN 32 112 Ig-like.
DOMAIN 178 205 ITAM. {ECO:0000255|PROSITE-
ProRule:PRU00379}.
REGION 175 192 NUMB-binding region.
{ECO:0000269|PubMed:26507128}.
MOD_RES 188 188 Phosphotyrosine.
{ECO:0000244|PubMed:15592455,
ECO:0000244|PubMed:19690332,
ECO:0000255|PROSITE-ProRule:PRU00379,
ECO:0000269|PubMed:9698567}.
MOD_RES 199 199 Phosphotyrosine. {ECO:0000255|PROSITE-
ProRule:PRU00379,
ECO:0000269|PubMed:9698567}.
DISULFID 49 98 {ECO:0000269|PubMed:15136729,
ECO:0000269|PubMed:15534202}.
STRAND 37 41 {ECO:0000244|PDB:1XIW}.
STRAND 44 48 {ECO:0000244|PDB:1XIW}.
STRAND 57 61 {ECO:0000244|PDB:1XIW}.
STRAND 64 69 {ECO:0000244|PDB:1XIW}.
STRAND 75 78 {ECO:0000244|PDB:1XIW}.
STRAND 81 84 {ECO:0000244|PDB:1XIW}.
HELIX 89 92 {ECO:0000244|PDB:1XIW}.
STRAND 94 100 {ECO:0000244|PDB:1XIW}.
HELIX 105 107 {ECO:0000244|PDB:1XIW}.
STRAND 110 116 {ECO:0000244|PDB:1XIW}.
HELIX 193 195 {ECO:0000244|PDB:1A81}.
SEQUENCE 207 AA; 23147 MW; A1603D01CE9957D7 CRC64;
MQSGTHWRVL GLCLLSVGVW GQDGNEEMGG ITQTPYKVSI SGTTVILTCP QYPGSEILWQ
HNDKNIGGDE DDKNIGSDED HLSLKEFSEL EQSGYYVCYP RGSKPEDANF YLYLRARVCE
NCMEMDVMSV ATIVIVDICI TGGLLLLVYY WSKNRKAKAK PVTRGAGAGG RQRGQNKERP
PPVPNPDYEP IRKGQRDLYS GLNQRRI


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