ID   CD3G_MOUSE              Reviewed;         182 AA.
AC   P11942;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   24-JAN-2024, entry version 182.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3655657; DOI=10.1084/jem.166.4.1186;
RA   Haser W.G., Saito H., Koyama T., Tonegawa S.;
RT   "Cloning and sequencing of murine T3 gamma cDNA from a subtractive cDNA
RT   library.";
RL   J. Exp. Med. 166:1186-1191(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2952720;
RA   Krissansen G.W., Owen M.J., Fink P.J., Crumpton M.J.;
RT   "Molecular cloning of the cDNA encoding the T3 gamma subunit of the mouse
RT   T3/T cell antigen receptor complex.";
RL   J. Immunol. 138:3513-3518(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2827170; DOI=10.1073/pnas.84.24.9131;
RA   Saito H., Koyama T., Georgopoulos K., Clevers H., Haser W.G., Lebien T.,
RA   Tonegawa S., Terhorst C.;
RT   "Close linkage of the mouse and human CD3 gamma- and delta-chain genes
RT   suggests that their transcription is controlled by common regulatory
RT   elements.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:9131-9134(1987).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9524111; DOI=10.1093/emboj/17.7.1871;
RA   Haks M.C., Krimpenfort P., Borst J., Kruisbeek A.M.;
RT   "The CD3gamma chain is essential for development of both the TCRalphabeta
RT   and TCRgammadelta lineages.";
RL   EMBO J. 17:1871-1882(1998).
RN   [6]
RP   FUNCTION.
RX   PubMed=25920998; DOI=10.1093/intimm/dxv022;
RA   Lauritsen J.P., Boding L., Buus T.B., Kongsbak M., Levring T.B., Rode A.K.,
RA   Bonefeld C.M., Geisler C.;
RT   "Fine-tuning of T-cell development by the CD3gamma di-leucine-based TCR-
RT   sorting motif.";
RL   Int. Immunol. 27:393-404(2015).
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 (PubMed:25920998).
CC       {ECO:0000250|UniProtKB:P09693, ECO:0000269|PubMed:25920998,
CC       ECO:0000269|PubMed:9524111}.
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: Membrane; Single-pass type I membrane protein.
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   -!- DISRUPTION PHENOTYPE: The absence of CD3G results in a severe reduction
CC       in the level of the TCR-CD3 at the cell surface of thymocytes and
CC       peripheral T cells. The development of both the TCRalphabeta and
CC       TCRgammadelta lineages are affected by the absence of CD3G.
CC       {ECO:0000269|PubMed:9524111}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Y00635; CAA68667.1; -; mRNA.
DR   EMBL; M58149; AAA63289.1; ALT_SEQ; mRNA.
DR   EMBL; M18227; AAA37400.1; -; Genomic_DNA.
DR   EMBL; M18222; AAA37400.1; JOINED; Genomic_DNA.
DR   EMBL; M18223; AAA37400.1; JOINED; Genomic_DNA.
DR   EMBL; M18224; AAA37400.1; JOINED; Genomic_DNA.
DR   EMBL; M18225; AAA37400.1; JOINED; Genomic_DNA.
DR   EMBL; M18226; AAA37400.1; JOINED; Genomic_DNA.
DR   EMBL; BC027528; AAH27528.1; -; mRNA.
DR   CCDS; CCDS23123.1; -.
DR   PIR; A39952; A28508.
DR   RefSeq; NP_033980.1; NM_009850.2.
DR   PDB; 1JBJ; NMR; -; A=23-103.
DR   PDBsum; 1JBJ; -.
DR   AlphaFoldDB; P11942; -.
DR   SMR; P11942; -.
DR   CORUM; P11942; -.
DR   ELM; P11942; -.
DR   IntAct; P11942; 1.
DR   STRING; 10090.ENSMUSP00000002101; -.
DR   GlyCosmos; P11942; 1 site, No reported glycans.
DR   GlyGen; P11942; 1 site.
DR   iPTMnet; P11942; -.
DR   PhosphoSitePlus; P11942; -.
DR   EPD; P11942; -.
DR   jPOST; P11942; -.
DR   PaxDb; 10090-ENSMUSP00000002101; -.
DR   ProteomicsDB; 281268; -.
DR   ABCD; P11942; 1 sequenced antibody.
DR   Antibodypedia; 4306; 465 antibodies from 41 providers.
DR   DNASU; 12502; -.
DR   Ensembl; ENSMUST00000002101.12; ENSMUSP00000002101.6; ENSMUSG00000002033.15.
DR   GeneID; 12502; -.
DR   KEGG; mmu:12502; -.
DR   UCSC; uc009pex.2; mouse.
DR   AGR; MGI:88333; -.
DR   CTD; 917; -.
DR   MGI; MGI:88333; Cd3g.
DR   VEuPathDB; HostDB:ENSMUSG00000002033; -.
DR   eggNOG; ENOG502S4XC; Eukaryota.
DR   GeneTree; ENSGT00940000153312; -.
DR   HOGENOM; CLU_115449_0_0_1; -.
DR   InParanoid; P11942; -.
DR   OMA; QYGHLQG; -.
DR   OrthoDB; 4266454at2759; -.
DR   PhylomeDB; P11942; -.
DR   TreeFam; TF335892; -.
DR   Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-MMU-202424; Downstream TCR signaling.
DR   Reactome; R-MMU-202427; Phosphorylation of CD3 and TCR zeta chains.
DR   Reactome; R-MMU-202430; Translocation of ZAP-70 to Immunological synapse.
DR   Reactome; R-MMU-202433; Generation of second messenger molecules.
DR   Reactome; R-MMU-2029481; FCGR activation.
DR   Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
DR   Reactome; R-MMU-389948; PD-1 signaling.
DR   Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR   BioGRID-ORCS; 12502; 4 hits in 77 CRISPR screens.
DR   ChiTaRS; Cd3g; mouse.
DR   EvolutionaryTrace; P11942; -.
DR   PRO; PR:P11942; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; P11942; Protein.
DR   Bgee; ENSMUSG00000002033; Expressed in thymus and 62 other cell types or tissues.
DR   ExpressionAtlas; P11942; baseline and differential.
DR   GO; GO:0042105; C:alpha-beta T cell receptor complex; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
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:0045059; P:positive thymic T cell selection; IBA:GO_Central.
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; Immunoglobulins; 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:SF8; T-CELL SURFACE GLYCOPROTEIN CD3 GAMMA CHAIN; 1.
DR   PANTHER; PTHR10570; T-CELL SURFACE GLYCOPROTEIN CD3 GAMMA CHAIN / DELTA CHAIN; 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; Immunoglobulin; 1.
DR   PROSITE; PS51055; ITAM_1; 1.
DR   Genevisible; P11942; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Adaptive immunity; Disulfide bond; Glycoprotein; Immunity;
KW   Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT   CHAIN           23..182
FT                   /note="T-cell surface glycoprotein CD3 gamma chain"
FT                   /id="PRO_0000014617"
FT   TOPO_DOM        23..116
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..182
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          37..94
FT                   /note="Ig-like"
FT   DOMAIN          149..177
FT                   /note="ITAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT   MOD_RES         145
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09693"
FT   MOD_RES         148
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09693"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        46..87
FT                   /evidence="ECO:0000250"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:1JBJ"
FT   STRAND          41..45
FT                   /evidence="ECO:0007829|PDB:1JBJ"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:1JBJ"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:1JBJ"
FT   STRAND          73..76
FT                   /evidence="ECO:0007829|PDB:1JBJ"
FT   STRAND          82..91
FT                   /evidence="ECO:0007829|PDB:1JBJ"
FT   STRAND          93..100
FT                   /evidence="ECO:0007829|PDB:1JBJ"
SQ   SEQUENCE   182 AA;  20234 MW;  7F9D8D44A5C360D5 CRC64;
     MEQRKGLAGL FLVISLLQGT VAQTNKAKNL VQVDGSRGDG SVLLTCGLTD KTIKWLKDGS
     IISPLNATKN TWNLGNNAKD PRGTYQCQGA KETSNPLQVY YRMCENCIEL NIGTISGFIF
     AEVISIFFLA LGVYLIAGQD GVRQSRASDK QTLLQNEQLY QPLKDREYDQ YSHLQGNQLR
     KK
//