CD3G_MACFA
ID CD3G_MACFA Reviewed; 181 AA.
AC Q95LI7;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 92.
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: Precursor;
GN Name=CD3G;
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].
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 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; AB073992; BAB71848.1; -; mRNA.
DR RefSeq; NP_001270839.1; NM_001283910.1.
DR AlphaFoldDB; Q95LI7; -.
DR BMRB; Q95LI7; -.
DR SMR; Q95LI7; -.
DR STRING; 9541.XP_005579857.1; -.
DR GeneID; 102134381; -.
DR CTD; 917; -.
DR eggNOG; ENOG502S4XC; Eukaryota.
DR Proteomes; UP000233100; 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; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..181
FT /note="T-cell surface glycoprotein CD3 gamma chain"
FT /id="PRO_0000014616"
FT TOPO_DOM 23..113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..97
FT /note="Ig-like"
FT DOMAIN 148..176
FT /note="ITAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOTIF 152..153
FT /note="Di-leucine motif"
FT /evidence="ECO:0000250|UniProtKB:P09693"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09693"
FT MOD_RES 147
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P09693"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..86
FT /evidence="ECO:0000250|UniProtKB:P09693"
SQ SEQUENCE 181 AA; 20530 MW; 1F8EA17D2446E5B9 CRC64;
MVQGKGLTGF ILAIILLQGS LAQSFEENRK LNVYNQEDGS VLLTCHVKNT NITWFKEGKM
IDILTAHKNK WNLGSNTKDP RGVYQCKGSK DKSKTLQVYY RMCQNCIELN AATILGFVFA
EIISIFFLAV GVYFIAGQDG VRQSRASDKQ TLLPNDQLYQ PLKDREDDQY SHLQGNQLRM
N
