ID CD3E_MACFA Reviewed; 198 AA.
AC Q95LI5; Q95LI6;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 24-JAN-2024, entry version 92.
DE RecName: Full=T-cell surface glycoprotein CD3 epsilon chain;
DE AltName: CD_antigen=CD3e;
DE Flags: Precursor;
GN Name=CD3E;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLY-67 AND GLN-72.
RX PubMed=11515669; DOI=10.1111/j.1600-0684.2001.tb00002.x;
RA Uda A., Tanabayashi K., Mukai R., Yachi M., Nam K., Yamada A.;
RT "CD3 polymorphism in cynomolgus monkeys (Macaca fascicularis).";
RL J. Med. Primatol. 30:141-147(2001).
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; AB073993; BAB71849.1; -; mRNA.
DR EMBL; AB073994; BAB71850.1; -; mRNA.
DR RefSeq; NP_001270544.1; NM_001283615.1.
DR RefSeq; XP_015290838.1; XM_015435352.1.
DR AlphaFoldDB; Q95LI5; -.
DR BMRB; Q95LI5; -.
DR SMR; Q95LI5; -.
DR STRING; 9541.ENSMFAP00000002547; -.
DR ABCD; Q95LI5; 22 sequenced antibodies.
DR GeneID; 102133065; -.
DR KEGG; mcf:102133065; -.
DR CTD; 916; -.
DR eggNOG; ENOG502S8KB; Eukaryota.
DR OrthoDB; 5358054at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0042105; C:alpha-beta T cell receptor complex; IEA:UniProt.
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; Immunoglobulins; 1.
DR InterPro; IPR015484; CD3_esu/gsu/dsu.
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:SF9; T-CELL SURFACE GLYCOPROTEIN CD3 EPSILON CHAIN; 1.
DR PANTHER; PTHR10570; T-CELL SURFACE GLYCOPROTEIN CD3 GAMMA CHAIN / DELTA CHAIN; 1.
DR Pfam; PF16681; Ig_5; 1.
DR Pfam; PF02189; ITAM; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00077; ITAM; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 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..198
FT /note="T-cell surface glycoprotein CD3 epsilon chain"
FT /id="PRO_0000014608"
FT TOPO_DOM 22..117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 37..107
FT /note="Ig-like"
FT DOMAIN 169..196
FT /note="ITAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT REGION 152..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..183
FT /note="NUMB-binding region"
FT /evidence="ECO:0000250|UniProtKB:P07766"
FT MOD_RES 179
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07766,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 190
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07766,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT DISULFID 49..89
FT /evidence="ECO:0000250|UniProtKB:P22646"
FT VARIANT 67
FT /note="E -> G (in allele FN18-)"
FT /evidence="ECO:0000269|PubMed:11515669"
FT VARIANT 72
FT /note="R -> Q (in allele FN18-)"
FT /evidence="ECO:0000269|PubMed:11515669"
SQ SEQUENCE 198 AA; 22149 MW; 7E434250C432F50C CRC64;
MQSGTRWRVL GLCLLSIGVW GQDGNEEMGS ITQTPYQVSI SGTTVILTCS QHLGSEAQWQ
HNGKNKEDSG DRLFLPEFSE MEQSGYYVCY PRGSNPEDAS HHLYLKARVC ENCMEMDVMA
VATIVIVDIC ITLGLLLLVY YWSKNRKAKA KPVTRGAGAG GRQRGQNKER PPPVPNPDYE
PIRKGQQDLY SGLNQRRI
//
