CD3E_CANLF
ID CD3E_CANLF Reviewed; 202 AA.
AC P27597;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=T-cell surface glycoprotein CD3 epsilon chain;
DE AltName: CD_antigen=CD3e;
DE Flags: Precursor;
GN Name=CD3E;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1828779; DOI=10.1007/bf00216700;
RA Nash R.A., Scherf U., Storb R.;
RT "Molecular cloning of the CD3 epsilon subunit of the T-cell receptor/CD3
RT complex in dog.";
RL Immunogenetics 33:396-398(1991).
CC -!- FUNCTION: Part of the TCR-CD3 complex present on T-lymphocyte cell
CC surface that plays an essential role in adaptive immune response. When
CC antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-
CC mediated signals are transmitted across the cell membrane by the CD3
CC chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor
CC tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain.
CC Upon TCR engagement, these motifs become phosphorylated by Src family
CC protein tyrosine kinases LCK and FYN, resulting in the activation of
CC downstream signaling pathways. In addition of this role of signal
CC transduction in T-cell activation, CD3E plays an essential role in
CC correct T-cell development. Initiates the TCR-CD3 complex assembly by
CC forming the two heterodimers CD3D/CD3E and CD3G/CD3E. Participates also
CC in internalization and cell surface down-regulation of TCR-CD3
CC complexes via endocytosis sequences present in CD3E cytosolic region.
CC {ECO:0000250|UniProtKB:P07766}.
CC -!- SUBUNIT: The TCR-CD3 complex is composed of a CD3D/CD3E and a CD3G/CD3E
CC heterodimers that preferentially associate with TCRalpha and TCRbeta,
CC respectively, to form TCRalpha/CD3E/CD3G and TCRbeta/CD3G/CD3E trimers.
CC In turn, the hexamer interacts with CD3Z homodimer to form the TCR-CD3
CC complex. Alternatively, TCRalpha and TCRbeta can be replaced by
CC TCRgamma and TCRdelta. Interacts with CD6. Interacts with NCK1.
CC Interacts with NUMB; this interaction is important for TCR-CD3
CC internalization and subsequent degradation.
CC {ECO:0000250|UniProtKB:P07766}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P07766};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P07766}.
CC -!- PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by
CC LCK in association with CD4/CD8. {ECO:0000250|UniProtKB:P07766}.
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DR EMBL; M55410; AAA30834.1; -; mRNA.
DR PIR; I46195; I46195.
DR RefSeq; NP_001003379.1; NM_001003379.1.
DR AlphaFoldDB; P27597; -.
DR SMR; P27597; -.
DR STRING; 9615.ENSCAFP00000052947; -.
DR PaxDb; P27597; -.
DR Ensembl; ENSCAFT00030015394; ENSCAFP00030013424; ENSCAFG00030008350.
DR Ensembl; ENSCAFT00040002328; ENSCAFP00040001989; ENSCAFG00040001243.
DR GeneID; 442981; -.
DR CTD; 916; -.
DR eggNOG; ENOG502S8KB; Eukaryota.
DR HOGENOM; CLU_117945_0_0_1; -.
DR InParanoid; P27597; -.
DR OMA; RVCENCV; -.
DR OrthoDB; 1362562at2759; -.
DR TreeFam; TF335892; -.
DR Reactome; R-CFA-202424; Downstream TCR signaling.
DR Reactome; R-CFA-202427; Phosphorylation of CD3 and TCR zeta chains.
DR Reactome; R-CFA-202430; Translocation of ZAP-70 to Immunological synapse.
DR Reactome; R-CFA-202433; Generation of second messenger molecules.
DR Reactome; R-CFA-389948; PD-1 signaling.
DR Proteomes; UP000002254; Unplaced.
DR Bgee; ENSCAFG00000012802; Expressed in thymus and 41 other tissues.
DR GO; GO:0042105; C:alpha-beta T cell receptor complex; IBA:GO_Central.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:0035739; P:CD4-positive, alpha-beta T cell proliferation; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0045060; P:negative thymic T cell selection; IEA:Ensembl.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; IEA:Ensembl.
DR GO; GO:0033634; P:positive regulation of cell-cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IEA:Ensembl.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0002669; P:positive regulation of T cell anergy; IEA:Ensembl.
DR GO; GO:0045059; P:positive thymic T cell selection; IBA:GO_Central.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0002870; P:T cell anergy; IEA:Ensembl.
DR GO; GO:0031295; P:T cell costimulation; IEA:Ensembl.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR015484; CD3_esu/gsu/dsu.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
DR PANTHER; PTHR10570; PTHR10570; 1.
DR Pfam; PF02189; ITAM; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00077; ITAM; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51055; ITAM_1; 1.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Cell membrane; Disulfide bond; Immunity;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..202
FT /note="T-cell surface glycoprotein CD3 epsilon chain"
FT /id="PRO_0000014605"
FT TOPO_DOM 22..122
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 37..107
FT /note="Ig-like"
FT DOMAIN 173..200
FT /note="ITAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT REGION 156..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..187
FT /note="NUMB-binding region"
FT /evidence="ECO:0000250|UniProtKB:P07766"
FT MOD_RES 183
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07766,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 194
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07766,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT DISULFID 54..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 202 AA; 22642 MW; E5779E0A44B8316E CRC64;
MQSRNLWRIL GLCLLSVGAW GQDEDFKASD DLTSISPEKR FKVSISGTEV VVTCPDVFGY
DNIKWEKNDN LVEGASNREL SQKEFSEVDD SGYYACYADS IKEKSYLYLR ARVCANCIEV
NLMAVVTIIV ADICLTLGLL LMVYYWSKTR KANAKPVMRG TGAGSRPRGQ NKEKPPPVPN
PDYEPIRKGQ QDLYSGLNQR GI
