CD3G_PIG
ID CD3G_PIG Reviewed; 182 AA.
AC Q5PXD3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yang H., Wileman T.;
RT "Structural differences between the CD3 molecules expressed at the surface
RT of alpha beta- and gamma delta-T cells revealed by monoclonal antibodies.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; AY823638; AAV80704.1; -; mRNA.
DR RefSeq; NP_001008686.1; NM_001008686.1.
DR RefSeq; XP_005653762.1; XM_005653705.2.
DR RefSeq; XP_005653763.1; XM_005653706.2.
DR RefSeq; XP_005653764.1; XM_005653707.2.
DR AlphaFoldDB; Q5PXD3; -.
DR SMR; Q5PXD3; -.
DR STRING; 9823.ENSSSCP00000016017; -.
DR PaxDb; Q5PXD3; -.
DR PRIDE; Q5PXD3; -.
DR Ensembl; ENSSSCT00065099089; ENSSSCP00065043480; ENSSSCG00065071966.
DR Ensembl; ENSSSCT00065099108; ENSSSCP00065043496; ENSSSCG00065071966.
DR Ensembl; ENSSSCT00070006663; ENSSSCP00070005433; ENSSSCG00070003473.
DR Ensembl; ENSSSCT00070006675; ENSSSCP00070005445; ENSSSCG00070003473.
DR GeneID; 494013; -.
DR KEGG; ssc:494013; -.
DR CTD; 917; -.
DR eggNOG; ENOG502S4XC; Eukaryota.
DR HOGENOM; CLU_115449_0_0_1; -.
DR InParanoid; Q5PXD3; -.
DR OMA; DRENDQY; -.
DR OrthoDB; 1466902at2759; -.
DR TreeFam; TF335892; -.
DR Reactome; R-SSC-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-SSC-202424; Downstream TCR signaling.
DR Reactome; R-SSC-202427; Phosphorylation of CD3 and TCR zeta chains.
DR Reactome; R-SSC-202430; Translocation of ZAP-70 to Immunological synapse.
DR Reactome; R-SSC-202433; Generation of second messenger molecules.
DR Reactome; R-SSC-2029481; FCGR activation.
DR Reactome; R-SSC-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-SSC-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-SSC-389948; PD-1 signaling.
DR Reactome; R-SSC-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-SSC-8856828; Clathrin-mediated endocytosis.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 9.
DR Genevisible; Q5PXD3; SS.
DR GO; GO:0042105; C:alpha-beta T cell receptor complex; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0045059; P:positive thymic T cell selection; IBA:GO_Central.
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:0000255"
FT CHAIN 23..182
FT /note="T-cell surface glycoprotein CD3 gamma chain"
FT /id="PRO_0000238449"
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 23..98
FT /note="Ig-like"
FT DOMAIN 149..177
FT /note="ITAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOTIF 153..154
FT /note="Di-leucine motif"
FT /evidence="ECO:0000250|UniProtKB:P09693"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09693"
FT MOD_RES 148
FT /note="Phosphoserine; by PKC"
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|UniProtKB:P09693"
SQ SEQUENCE 182 AA; 20461 MW; 037F78AA546F3EA1 CRC64;
MEQGKHLAGL ILAITLLQGT MAQLKEGKHS VLLDDNREDG SVLLTCGLPD QNIRWFKDGK
EICSLNNSRS TCNLGSSSKD PRGIYWCEGS KENSKRLQVY YRMCQNCIEL NSATVSGFIF
TEIISLFFLA VGVYFIAGQD GVRQSRASDK QTLLSNDQLY QPLKDREDDQ YSHLQGNNSR
KN
