CD3E_RABIT
ID CD3E_RABIT Reviewed; 198 AA.
AC Q9TUF9;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=T-cell surface glycoprotein CD3 epsilon chain;
DE AltName: CD_antigen=CD3e;
DE Flags: Precursor;
GN Name=CD3E;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Isono T., Nishimura M.;
RT "Rabbit CD3 epsilon.";
RL Submitted (NOV-1999) 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; AB035151; BAA86993.1; -; mRNA.
DR RefSeq; NP_001075470.1; NM_001082001.1.
DR AlphaFoldDB; Q9TUF9; -.
DR SMR; Q9TUF9; -.
DR DIP; DIP-6067N; -.
DR STRING; 9986.ENSOCUP00000019523; -.
DR GeneID; 100008616; -.
DR KEGG; ocu:100008616; -.
DR CTD; 916; -.
DR eggNOG; ENOG502S8KB; Eukaryota.
DR InParanoid; Q9TUF9; -.
DR OrthoDB; 1362562at2759; -.
DR Proteomes; UP000001811; 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..198
FT /note="T-cell surface glycoprotein CD3 epsilon chain"
FT /id="PRO_0000014611"
FT TOPO_DOM 22..120
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..106
FT /note="Ig-like"
FT DOMAIN 169..196
FT /note="ITAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT REGION 153..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..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 198 AA; 22232 MW; E9F354E30D454D50 CRC64;
MRAGTLWRVL ALWLLSVAAW GQEDDDHADD YTQKLFTVSI SGTRVVLTCP VEAEGGDIHW
ERDEKSLPNT KKELDLTDFS EMEHSGYYSC YVGTKNKENE HILYLKARVC EACMEVDLTT
VASIVVADVC VTLGLLLLVY YWSKNRKAKC KPVTRGAGAG GRPRGQNKER PPPVPNPDYE
PIRKGQRDLY SGLNQRGI
