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T-cell surface glycoprotein CD3 gamma chain (T-cell receptor T3 gamma chain) (CD antigen CD3g)

 CD3G_MOUSE              Reviewed;         182 AA.
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
16-JAN-2019, entry version 157.
RecName: Full=T-cell surface glycoprotein CD3 gamma chain;
AltName: Full=T-cell receptor T3 gamma chain;
AltName: CD_antigen=CD3g;
Flags: Precursor;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
PubMed=3655657; DOI=10.1084/jem.166.4.1186;
Haser W.G., Saito H., Koyama T., Tonegawa S.;
"Cloning and sequencing of murine T3 gamma cDNA from a subtractive
cDNA library.";
J. Exp. Med. 166:1186-1191(1987).
Krissansen G.W., Owen M.J., Fink P.J., Crumpton M.J.;
"Molecular cloning of the cDNA encoding the T3 gamma subunit of the
mouse T3/T cell antigen receptor complex.";
J. Immunol. 138:3513-3518(1987).
PubMed=2827170; DOI=10.1073/pnas.84.24.9131;
Saito H., Koyama T., Georgopoulos K., Clevers H., Haser W.G.,
Lebien T., Tonegawa S., Terhorst C.;
"Close linkage of the mouse and human CD3 gamma- and delta-chain genes
suggests that their transcription is controlled by common regulatory
Proc. Natl. Acad. Sci. U.S.A. 84:9131-9134(1987).
TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
PubMed=9524111; DOI=10.1093/emboj/17.7.1871;
Haks M.C., Krimpenfort P., Borst J., Kruisbeek A.M.;
"The CD3gamma chain is essential for development of both the
TCRalphabeta and TCRgammadelta lineages.";
EMBO J. 17:1871-1882(1998).
PubMed=25920998; DOI=10.1093/intimm/dxv022;
Lauritsen J.P., Boding L., Buus T.B., Kongsbak M., Levring T.B.,
Rode A.K., Bonefeld C.M., Geisler C.;
"Fine-tuning of T-cell development by the CD3gamma di-leucine-based
TCR-sorting motif.";
Int. Immunol. 27:393-404(2015).
-!- FUNCTION: Part of the TCR-CD3 complex present on T-lymphocyte cell
surface that plays an essential role in adaptive immune response.
When antigen presenting cells (APCs) activate T-cell receptor
(TCR), TCR-mediated signals are transmitted across the cell
membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3
chains contain immunoreceptor tyrosine-based activation motifs
(ITAMs) in their cytoplasmic domain. Upon TCR engagement, these
motifs become phosphorylated by Src family protein tyrosine
kinases LCK and FYN, resulting in the activation of downstream
signaling pathways. In addition to this role of signal
transduction in T-cell activation, CD3G plays an essential role in
the dynamic regulation of TCR expression at the cell surface.
Indeed, constitutive TCR cycling is dependent on the di-leucine-
based (diL) receptor-sorting motif present in CD3G
(PubMed:25920998). {ECO:0000250|UniProtKB:P09693,
ECO:0000269|PubMed:25920998, ECO:0000269|PubMed:9524111}.
-!- SUBUNIT: The TCR-CD3 complex is composed of a CD3D/CD3E and a
CD3G/CD3E heterodimers that preferentially associate with TCRalpha
and TCRbeta, respectively, to form TCRalpha/CD3E/CD3G and
TCRbeta/CD3G/CD3E trimers. In turn, the hexamer interacts with
CD3Z homodimer to form the TCR-CD3 complex. Alternatively,
TCRalpha and TCRbeta can be replaced by TCRgamma and TCRdelta.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
-!- PTM: Phosphorylated on Tyr residues after T-cell receptor
triggering by LCK in association with CD4/CD8. Phosphorylated also
by PKC; leading to the TCR complex down-regulation.
-!- DISRUPTION PHENOTYPE: The absence of CD3G results in a severe
reduction in the level of the TCR-CD3 at the cell surface of
thymocytes and peripheral T cells. The development of both the
TCRalphabeta and TCRgammadelta lineages are affected by the
absence of CD3G. {ECO:0000269|PubMed:9524111}.
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; Y00635; CAA68667.1; -; mRNA.
EMBL; M58149; AAA63289.1; ALT_SEQ; mRNA.
EMBL; M18227; AAA37400.1; -; Genomic_DNA.
EMBL; M18222; AAA37400.1; JOINED; Genomic_DNA.
EMBL; M18223; AAA37400.1; JOINED; Genomic_DNA.
EMBL; M18224; AAA37400.1; JOINED; Genomic_DNA.
EMBL; M18225; AAA37400.1; JOINED; Genomic_DNA.
EMBL; M18226; AAA37400.1; JOINED; Genomic_DNA.
EMBL; BC027528; AAH27528.1; -; mRNA.
CCDS; CCDS23123.1; -.
PIR; A39952; A28508.
RefSeq; NP_033980.1; NM_009850.2.
UniGene; Mm.335106; -.
PDB; 1JBJ; NMR; -; A=23-103.
PDBsum; 1JBJ; -.
ProteinModelPortal; P11942; -.
SMR; P11942; -.
CORUM; P11942; -.
ELM; P11942; -.
IntAct; P11942; 1.
STRING; 10090.ENSMUSP00000002101; -.
iPTMnet; P11942; -.
PhosphoSitePlus; P11942; -.
EPD; P11942; -.
PaxDb; P11942; -.
PRIDE; P11942; -.
Ensembl; ENSMUST00000002101; ENSMUSP00000002101; ENSMUSG00000002033.
GeneID; 12502; -.
KEGG; mmu:12502; -.
UCSC; uc009pex.2; mouse.
CTD; 917; -.
MGI; MGI:88333; Cd3g.
eggNOG; ENOG410IWAX; Eukaryota.
GeneTree; ENSGT00940000153312; -.
HOGENOM; HOG000015287; -.
HOVERGEN; HBG005278; -.
InParanoid; P11942; -.
KO; K06452; -.
OrthoDB; 1466902at2759; -.
PhylomeDB; P11942; -.
TreeFam; TF335892; -.
Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-MMU-202424; Downstream TCR signaling.
Reactome; R-MMU-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-MMU-202430; Translocation of ZAP-70 to Immunological synapse.
Reactome; R-MMU-202433; Generation of second messenger molecules.
Reactome; R-MMU-2029481; FCGR activation.
Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
Reactome; R-MMU-389948; PD-1 signaling.
Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
EvolutionaryTrace; P11942; -.
PRO; PR:P11942; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000002033; Expressed in 102 organ(s), highest expression level in thymus.
CleanEx; MM_CD3G; -.
ExpressionAtlas; P11942; baseline and differential.
Genevisible; P11942; MM.
GO; GO:0042105; C:alpha-beta T cell receptor complex; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0004888; F:transmembrane signaling receptor activity; ISS:UniProtKB.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007163; P:establishment or maintenance of cell polarity; ISS:UniProtKB.
GO; GO:0045059; P:positive thymic T cell selection; IBA:GO_Central.
GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
GO; GO:0015031; P:protein transport; ISS:UniProtKB.
GO; GO:0070228; P:regulation of lymphocyte apoptotic process; ISS:UniProtKB.
GO; GO:0030217; P:T cell differentiation; IBA:GO_Central.
Gene3D;; -; 1.
InterPro; IPR015484; CD3_esu/gsu/dsu.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR032052; Ig_4.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
PANTHER; PTHR10570; PTHR10570; 1.
Pfam; PF16680; Ig_4; 1.
Pfam; PF02189; ITAM; 1.
SMART; SM00408; IGc2; 1.
SMART; SM00077; ITAM; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS51055; ITAM_1; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Complete proteome; Disulfide bond;
Glycoprotein; Immunity; Immunoglobulin domain; Membrane;
Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
CHAIN 23 182 T-cell surface glycoprotein CD3 gamma
TOPO_DOM 23 116 Extracellular. {ECO:0000255}.
TRANSMEM 117 137 Helical. {ECO:0000255}.
TOPO_DOM 138 182 Cytoplasmic. {ECO:0000255}.
DOMAIN 37 94 Ig-like.
DOMAIN 149 177 ITAM. {ECO:0000255|PROSITE-
MOD_RES 145 145 Phosphoserine.
MOD_RES 148 148 Phosphoserine.
CARBOHYD 66 66 N-linked (GlcNAc...) asparagine.
DISULFID 46 87 {ECO:0000250}.
STRAND 37 39 {ECO:0000244|PDB:1JBJ}.
STRAND 41 45 {ECO:0000244|PDB:1JBJ}.
STRAND 47 49 {ECO:0000244|PDB:1JBJ}.
STRAND 53 57 {ECO:0000244|PDB:1JBJ}.
STRAND 73 76 {ECO:0000244|PDB:1JBJ}.
STRAND 82 91 {ECO:0000244|PDB:1JBJ}.
STRAND 93 100 {ECO:0000244|PDB:1JBJ}.
SEQUENCE 182 AA; 20234 MW; 7F9D8D44A5C360D5 CRC64;

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