CD3G_SHEEP
ID CD3G_SHEEP Reviewed; 147 AA.
AC P18439;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=T-cell surface glycoprotein CD3 gamma chain;
DE AltName: Full=T-cell receptor T3 gamma chain;
DE AltName: CD_antigen=CD3g;
DE Flags: Fragment;
GN Name=CD3G;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphocyte;
RX PubMed=2143727; DOI=10.1002/eji.1830200715;
RA Hein W.R., Tunnacliffe A.;
RT "Characterization of the CD3 gamma and delta invariant subunits of the
RT sheep T cell antigen receptor.";
RL Eur. J. Immunol. 20:1505-1511(1990).
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 to this role of signal
CC transduction in T-cell activation, CD3G plays an essential role in the
CC dynamic regulation of TCR expression at the cell surface. Indeed,
CC constitutive TCR cycling is dependent on the di-leucine-based (diL)
CC receptor-sorting motif present in CD3G. {ECO:0000250|UniProtKB:P09693}.
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. {ECO:0000250|UniProtKB:P09693}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P09693};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09693}.
CC -!- DOMAIN: A di-leucine motif and a tyrosine-based motif are individually
CC sufficient to induce both endocytosis and delivery to lysosomes.
CC {ECO:0000250|UniProtKB:P09693}.
CC -!- PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by
CC LCK in association with CD4/CD8. Phosphorylated also by PKC; leading to
CC the TCR complex down-regulation. {ECO:0000250|UniProtKB:P09693}.
CC -!- PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by
CC LCK in association with CD4/CD8. {ECO:0000250|UniProtKB:P04234}.
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DR EMBL; X52994; CAA37183.1; -; mRNA.
DR PIR; A43547; A43547.
DR AlphaFoldDB; P18439; -.
DR SMR; P18439; -.
DR STRING; 9940.ENSOARP00000009931; -.
DR eggNOG; ENOG502S4XC; Eukaryota.
DR Proteomes; UP000002356; 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; ISS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR GO; GO:0070228; P:regulation of lymphocyte apoptotic process; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR015484; CD3_esu/gsu/dsu.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032052; Ig_4.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
DR PANTHER; PTHR10570; PTHR10570; 1.
DR Pfam; PF16680; Ig_4; 1.
DR Pfam; PF02189; ITAM; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00077; ITAM; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS51055; ITAM_1; 1.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN <1..147
FT /note="T-cell surface glycoprotein CD3 gamma chain"
FT /id="PRO_0000072672"
FT TOPO_DOM <1..85
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 7..64
FT /note="Ig-like"
FT DOMAIN 119..147
FT /note="ITAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOTIF 123..124
FT /note="Di-leucine motif"
FT /evidence="ECO:0000250|UniProtKB:P09693"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09693"
FT MOD_RES 118
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P09693"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 16..57
FT /evidence="ECO:0000250|UniProtKB:P09693"
FT NON_TER 1
SQ SEQUENCE 147 AA; 16723 MW; 116B33773033D6B8 CRC64;
VKVDDNQEDG SVILICVTDE KKITWLKDMK EISSGDTNKL TWDLGSSTKD PRGIYECKGS
SNESKSLQIY YRMCQNCIEL NLATVAGFIF TEIVSIFLLA VGVYFIAGQE GVRQSRASDK
QTLLNNDQLY QPLKEREDDQ YSHLRKK
