CD3E_PIG
ID CD3E_PIG Reviewed; 196 AA.
AC Q7YRN2;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=T-cell surface glycoprotein CD3 epsilon chain;
DE AltName: CD_antigen=CD3e;
DE Flags: Precursor;
GN Name=CD3E;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang J., Yang H., Guo X.;
RT "Cloning and sequencing of porcine CD3 epsilon.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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; AY323829; AAP85530.1; -; mRNA.
DR RefSeq; NP_999392.1; NM_214227.1.
DR AlphaFoldDB; Q7YRN2; -.
DR SMR; Q7YRN2; -.
DR STRING; 9823.ENSSSCP00000016015; -.
DR PaxDb; Q7YRN2; -.
DR PeptideAtlas; Q7YRN2; -.
DR GeneID; 397455; -.
DR KEGG; ssc:397455; -.
DR CTD; 916; -.
DR eggNOG; ENOG502S8KB; Eukaryota.
DR InParanoid; Q7YRN2; -.
DR OrthoDB; 1362562at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0042105; C:alpha-beta T cell receptor complex; IEA:UniProt.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR015484; CD3_esu/gsu/dsu.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
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 SUPFAM; SSF48726; SSF48726; 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..196
FT /note="T-cell surface glycoprotein CD3 epsilon chain"
FT /id="PRO_0000014610"
FT TOPO_DOM 22..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..102
FT /note="Ig-like"
FT DOMAIN 167..194
FT /note="ITAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT REGION 150..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..181
FT /note="NUMB-binding region"
FT /evidence="ECO:0000250|UniProtKB:P07766"
FT MOD_RES 177
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07766,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 188
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07766,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT DISULFID 49..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 196 AA; 22198 MW; B1840232E575964E CRC64;
MPSGNLWKVL GLCLLSVGAW GQEDIERPDE DTQKTFKVSI SGDKVELTCP EDPESEKMTW
KRNDMQIYES YDNYMLLESF SEVENSGYYT CTVGEKTSHR LYLKARVCEN CVEVDLMAVV
TIIVVDICIT LGLLMVVYYY SKSRKAKAMP VTRGAGAGGR PRGQNRERPP PVPNPDYEPI
RKGQRDLYSG LNQRGR
