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

 CD3G_HUMAN              Reviewed;         182 AA.
P09693; Q2HIZ6;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
22-NOV-2017, entry version 167.
RecName: Full=T-cell surface glycoprotein CD3 gamma chain;
AltName: Full=T-cell receptor T3 gamma chain;
AltName: CD_antigen=CD3g;
Flags: Precursor;
Name=CD3G; Synonyms=T3G;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2944745;
Krissansen G.W., Owen M.J., Verbi W., Crumpton M.J.;
"Primary structure of the T3 gamma subunit of the T3/T cell antigen
receptor complex deduced from cDNA sequences: evolution of the T3
gamma and delta subunits.";
EMBO J. 5:1799-1808(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2826124;
Tunnacliffe A., Buluwela L., Rabbitts T.H.;
"Physical linkage of three CD3 genes on human chromosome 11.";
EMBO J. 6:2953-2957(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[4]
PROTEIN SEQUENCE OF 139-182, AND PHOSPHORYLATION AT SER-145 AND
SER-148.
PubMed=2540970; DOI=10.1111/j.1432-1033.1989.tb14693.x;
Alexander D., Goris J., Marais R., Rothbard J., Merlevede W.,
Crumpton M.J.;
"Dephosphorylation of the human T lymphocyte CD3 antigen.";
Eur. J. Biochem. 181:55-65(1989).
[5]
PHOSPHORYLATION AT SER-145 AND SER-148.
PubMed=3112151;
Davies A.A., Cantrell D.A., Hexham J.M., Parker P.J., Rothbard J.,
Crumpton M.J.;
"The human T3 gamma chain is phosphorylated at serine 126 in response
to T lymphocyte activation.";
J. Biol. Chem. 262:10918-10921(1987).
[6]
FUNCTION, AND PHOSPHORYLATION BY LCK.
PubMed=2470098;
Barber E.K., Dasgupta J.D., Schlossman S.F., Trevillyan J.M.,
Rudd C.E.;
"The CD4 and CD8 antigens are coupled to a protein-tyrosine kinase
(p56lck) that phosphorylates the CD3 complex.";
Proc. Natl. Acad. Sci. U.S.A. 86:3277-3281(1989).
[7]
MUTAGENESIS OF LEU-153; LEU-154; TYR-160 AND LEU-163.
PubMed=1535555; DOI=10.1016/0092-8674(92)90636-Q;
Letourneur F., Klausner R.D.;
"A novel di-leucine motif and a tyrosine-based motif independently
mediate lysosomal targeting and endocytosis of CD3 chains.";
Cell 69:1143-1157(1992).
[8]
INVOLVEMENT IN IMD17.
PubMed=1635567; DOI=10.1056/NEJM199208203270805;
Arnaiz-Villena A., Timon M., Corell A., Perez-Aciego P.,
Martin-Villa J.M., Regueiro J.R.;
"Brief report: primary immunodeficiency caused by mutations in the
gene encoding the CD3-gamma subunit of the T-lymphocyte receptor.";
N. Engl. J. Med. 327:529-533(1992).
[9]
FUNCTION, PHOSPHORYLATION AT SER-148, AND MUTAGENESIS OF LEU-153 AND
LEU-154.
PubMed=8187769;
Dietrich J., Hou X., Wegener A.M., Geisler C.;
"CD3 gamma contains a phosphoserine-dependent di-leucine motif
involved in down-regulation of the T cell receptor.";
EMBO J. 13:2156-2166(1994).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION AT ASN-52 AND
ASN-92.
PubMed=8636209;
Dietrich J., Neisig A., Hou X., Wegener A.M., Gajhede M., Geisler C.;
"Role of CD3 gamma in T cell receptor assembly.";
J. Cell Biol. 132:299-310(1996).
[11]
REVIEW ON FUNCTION.
PubMed=14995914;
Geisler C.;
"TCR trafficking in resting and stimulated T cells.";
Crit. Rev. Immunol. 24:67-86(2004).
[12]
INVOLVEMENT IN IMD17.
PubMed=17277165; DOI=10.4049/jimmunol.178.4.2556;
Recio M.J., Moreno-Pelayo M.A., Kilic S.S., Guardo A.C., Sanal O.,
Allende L.M., Perez-Flores V., Mencia A., Modamio-Hoeybjoer S.,
Seoane E., Regueiro J.R.;
"Differential biological role of CD3 chains revealed by human
immunodeficiencies.";
J. Immunol. 178:2556-2564(2007).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 23-103 IN COMPLEX WITH CD3E
AND ANTIBODY, SUBUNIT, AND DISULFIDE BOND.
PubMed=15136729; DOI=10.1073/pnas.0402295101;
Kjer-Nielsen L., Dunstone M.A., Kostenko L., Ely L.K., Beddoe T.,
Mifsud N.A., Purcell A.W., Brooks A.G., McCluskey J., Rossjohn J.;
"Crystal structure of the human T cell receptor CD3 epsilon gamma
heterodimer complexed to the therapeutic mAb OKT3.";
Proc. Natl. Acad. Sci. U.S.A. 101:7675-7680(2004).
-!- 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 (PubMed:2470098). 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 (PubMed:8187769). Indeed, constitutive TCR cycling is
dependent on the di-leucine-based (diL) receptor-sorting motif
present in CD3G. {ECO:0000269|PubMed:2470098,
ECO:0000269|PubMed:8187769, ECO:0000269|PubMed:8636209}.
-!- 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.
{ECO:0000269|PubMed:15136729}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8636209};
Single-pass type I membrane protein.
-!- DOMAIN: A di-leucine motif and a tyrosine-based motif are
individually sufficient to induce both endocytosis and delivery to
lysosomes.
-!- PTM: Phosphorylated on Tyr residues after T-cell receptor
triggering by LCK in association with CD4/CD8 (PubMed:2470098).
Phosphorylated also by PKC; leading to the TCR complex down-
regulation (PubMed:8187769). {ECO:0000269|PubMed:2470098,
ECO:0000269|PubMed:8187769}.
-!- PTM: Phosphorylated on Tyr residues after T-cell receptor
triggering by LCK in association with CD4/CD8.
{ECO:0000250|UniProtKB:P04234}.
-!- DISEASE: Immunodeficiency 17 (IMD17) [MIM:615607]: An autosomal
recessive primary immunodeficiency characterized by highly
variable clinical severity. Some patients have onset of severe
recurrent infections in early infancy that may be lethal, whereas
others may be only mildly affected or essentially asymptomatic
into young adulthood. More severely affected patients may have
evidence of autoimmune disease or enteropathy. The immunologic
pattern is similar among patients, showing partial T-cell
lymphopenia, decreased amounts of the CD3 complex, and impaired
proliferative responses to T-cell receptor dependent stimuli. The
phenotype in some patients is reminiscent of severe combined
immunodeficiency. {ECO:0000269|PubMed:1635567,
ECO:0000269|PubMed:17277165}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=CD3Gbase; Note=CD3G mutation db;
URL="http://structure.bmc.lu.se/idbase/CD3Gbase/";
-!- WEB RESOURCE: Name=Wikipedia; Note=CD3 receptor entry;
URL="https://en.wikipedia.org/wiki/CD3_receptor";
-----------------------------------------------------------------------
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EMBL; X04145; CAA27764.1; -; mRNA.
EMBL; X06026; CAA29428.1; -; Genomic_DNA.
EMBL; X06027; CAA29428.1; JOINED; Genomic_DNA.
EMBL; X06028; CAA29428.1; JOINED; Genomic_DNA.
EMBL; X06029; CAA29428.1; JOINED; Genomic_DNA.
EMBL; X06030; CAA29428.1; JOINED; Genomic_DNA.
EMBL; X06031; CAA29428.1; JOINED; Genomic_DNA.
EMBL; BC113830; AAI13831.1; -; mRNA.
CCDS; CCDS8395.1; -.
PIR; A25468; A25468.
RefSeq; NP_000064.1; NM_000073.2.
RefSeq; XP_006719004.1; XM_006718941.2.
UniGene; Hs.2259; -.
PDB; 1SY6; X-ray; 2.10 A; A=23-103.
PDBsum; 1SY6; -.
DisProt; DP00508; -.
ProteinModelPortal; P09693; -.
SMR; P09693; -.
BioGrid; 107355; 3.
ELM; P09693; -.
IntAct; P09693; 1.
MINT; MINT-4656150; -.
STRING; 9606.ENSP00000431445; -.
ChEMBL; CHEMBL2364168; -.
DrugBank; DB00075; Muromonab.
iPTMnet; P09693; -.
PhosphoSitePlus; P09693; -.
BioMuta; CD3G; -.
DMDM; 115993; -.
MaxQB; P09693; -.
PaxDb; P09693; -.
PeptideAtlas; P09693; -.
PRIDE; P09693; -.
Ensembl; ENST00000532917; ENSP00000431445; ENSG00000160654.
GeneID; 917; -.
KEGG; hsa:917; -.
UCSC; uc001psu.3; human.
CTD; 917; -.
DisGeNET; 917; -.
EuPathDB; HostDB:ENSG00000160654.9; -.
GeneCards; CD3G; -.
HGNC; HGNC:1675; CD3G.
HPA; CAB017520; -.
HPA; HPA038494; -.
MalaCards; CD3G; -.
MIM; 186740; gene.
MIM; 615607; phenotype.
neXtProt; NX_P09693; -.
OpenTargets; ENSG00000160654; -.
Orphanet; 169082; Combined immunodeficiency due to CD3gamma deficiency.
PharmGKB; PA26217; -.
eggNOG; ENOG410IWAX; Eukaryota.
eggNOG; ENOG410Y2TD; LUCA.
GeneTree; ENSGT00510000046930; -.
HOGENOM; HOG000015287; -.
HOVERGEN; HBG005278; -.
InParanoid; P09693; -.
KO; K06452; -.
OMA; DRENDQY; -.
OrthoDB; EOG091G0MXQ; -.
PhylomeDB; P09693; -.
TreeFam; TF335892; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse.
Reactome; R-HSA-202433; Generation of second messenger molecules.
Reactome; R-HSA-2029481; FCGR activation.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
Reactome; R-HSA-389948; PD-1 signaling.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
SIGNOR; P09693; -.
ChiTaRS; CD3G; human.
EvolutionaryTrace; P09693; -.
GeneWiki; CD3G; -.
GenomeRNAi; 917; -.
PRO; PR:P09693; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000160654; -.
CleanEx; HS_CD3G; -.
ExpressionAtlas; P09693; baseline and differential.
Genevisible; P09693; HS.
GO; GO:0042105; C:alpha-beta T cell receptor complex; IEA:Ensembl.
GO; GO:0030665; C:clathrin-coated vesicle membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0042101; C:T cell receptor complex; NAS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IMP:CAFA.
GO; GO:0030159; F:receptor signaling complex scaffold activity; NAS:UniProtKB.
GO; GO:0042608; F:T cell receptor binding; NAS:UniProtKB.
GO; GO:0004888; F:transmembrane signaling receptor activity; IMP:UniProtKB.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007166; P:cell surface receptor signaling pathway; IMP:UniProtKB.
GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:UniProtKB.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0006461; P:protein complex assembly; NAS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IMP:CAFA.
GO; GO:0015031; P:protein transport; IMP:UniProtKB.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0070228; P:regulation of lymphocyte apoptotic process; IMP:UniProtKB.
GO; GO:0042110; P:T cell activation; NAS:UniProtKB.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
Gene3D; 2.60.40.10; -; 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; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
Immunoglobulin domain; Membrane; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 22
CHAIN 23 182 T-cell surface glycoprotein CD3 gamma
chain.
/FTId=PRO_0000014615.
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-
ProRule:PRU00379}.
MOTIF 153 154 Di-leucine motif.
{ECO:0000269|PubMed:8187769}.
MOD_RES 145 145 Phosphoserine.
{ECO:0000269|PubMed:2540970,
ECO:0000269|PubMed:3112151}.
MOD_RES 148 148 Phosphoserine; by PKC.
{ECO:0000269|PubMed:2540970,
ECO:0000269|PubMed:3112151,
ECO:0000269|PubMed:8187769}.
CARBOHYD 52 52 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8636209}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8636209}.
DISULFID 46 87 {ECO:0000269|PubMed:15136729}.
VARIANT 131 131 V -> F (in dbSNP:rs3753058).
/FTId=VAR_049854.
MUTAGEN 153 153 L->A: Abolishes lysosomal targeting.
{ECO:0000269|PubMed:1535555,
ECO:0000269|PubMed:8187769}.
MUTAGEN 153 153 L->I: Diminished but persistent lysosomal
targeting. {ECO:0000269|PubMed:1535555}.
MUTAGEN 154 154 L->A: Abolishes lysosomal targeting.
{ECO:0000269|PubMed:8187769}.
MUTAGEN 154 154 L->A: Diminished but persistent lysosomal
targeting. {ECO:0000269|PubMed:1535555}.
MUTAGEN 154 154 L->I: No effect.
{ECO:0000269|PubMed:1535555}.
MUTAGEN 160 160 Y->A: Abolishes lysosomal targeting.
{ECO:0000269|PubMed:1535555}.
MUTAGEN 163 163 L->A: Abolishes lysosomal targeting.
{ECO:0000269|PubMed:1535555}.
TURN 26 28 {ECO:0000244|PDB:1SY6}.
STRAND 31 33 {ECO:0000244|PDB:1SY6}.
STRAND 38 46 {ECO:0000244|PDB:1SY6}.
STRAND 50 57 {ECO:0000244|PDB:1SY6}.
STRAND 60 68 {ECO:0000244|PDB:1SY6}.
STRAND 72 76 {ECO:0000244|PDB:1SY6}.
HELIX 77 79 {ECO:0000244|PDB:1SY6}.
STRAND 82 92 {ECO:0000244|PDB:1SY6}.
STRAND 97 102 {ECO:0000244|PDB:1SY6}.
SEQUENCE 182 AA; 20469 MW; EE65C0186FB9872B CRC64;
MEQGKGLAVL ILAIILLQGT LAQSIKGNHL VKVYDYQEDG SVLLTCDAEA KNITWFKDGK
MIGFLTEDKK KWNLGSNAKD PRGMYQCKGS QNKSKPLQVY YRMCQNCIEL NAATISGFLF
AEIVSIFVLA VGVYFIAGQD GVRQSRASDK QTLLPNDQLY QPLKDREDDQ YSHLQGNQLR
RN


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