P09693 · CD3G_HUMAN
- ProteinT-cell surface glycoprotein CD3 gamma chain
- GeneCD3G
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids182 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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
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
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameT-cell surface glycoprotein CD3 gamma chain
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP09693
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 23-116 | Extracellular | ||||
Sequence: QSIKGNHLVKVYDYQEDGSVLLTCDAEAKNITWFKDGKMIGFLTEDKKKWNLGSNAKDPRGMYQCKGSQNKSKPLQVYYRMCQNCIELNAATIS | ||||||
Transmembrane | 117-137 | Helical | ||||
Sequence: GFLFAEIVSIFVLAVGVYFIA | ||||||
Topological domain | 138-182 | Cytoplasmic | ||||
Sequence: GQDGVRQSRASDKQTLLPNDQLYQPLKDREDDQYSHLQGNQLRRN |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Immunodeficiency 17 (IMD17)
- Note
- DescriptionAn 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.
- See alsoMIM:615607
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_049854 | 131 | in dbSNP:rs3753058 | |||
Sequence: V → F | ||||||
Mutagenesis | 153 | Abolishes lysosomal targeting. | ||||
Sequence: L → A | ||||||
Mutagenesis | 153 | Diminished but persistent lysosomal targeting. | ||||
Sequence: L → I | ||||||
Mutagenesis | 154 | Abolishes lysosomal targeting. | ||||
Sequence: L → A | ||||||
Mutagenesis | 154 | Diminished but persistent lysosomal targeting. | ||||
Sequence: L → A | ||||||
Mutagenesis | 154 | No effect. | ||||
Sequence: L → I | ||||||
Mutagenesis | 160 | Abolishes lysosomal targeting. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 163 | Abolishes lysosomal targeting. | ||||
Sequence: L → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 229 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-22 | UniProt | |||||
Sequence: MEQGKGLAVLILAIILLQGTLA | |||||||
Chain | PRO_0000014615 | 23-182 | UniProt | T-cell surface glycoprotein CD3 gamma chain | |||
Sequence: QSIKGNHLVKVYDYQEDGSVLLTCDAEAKNITWFKDGKMIGFLTEDKKKWNLGSNAKDPRGMYQCKGSQNKSKPLQVYYRMCQNCIELNAATISGFLFAEIVSIFVLAVGVYFIAGQDGVRQSRASDKQTLLPNDQLYQPLKDREDDQYSHLQGNQLRRN | |||||||
Disulfide bond | 46↔87 | UniProt | |||||
Sequence: CDAEAKNITWFKDGKMIGFLTEDKKKWNLGSNAKDPRGMYQC | |||||||
Glycosylation | 52 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 92 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue | 145 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 148 | UniProt | Phosphoserine; by PKC | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 148 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 160 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 171 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 172 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
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).
Phosphorylated also by PKC; leading to the TCR complex down-regulation (PubMed:8187769).
Phosphorylated on Tyr residues after T-cell receptor triggering by LCK in association with CD4/CD8.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
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.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P09693 | EMP1 P54849 | 3 | EBI-3862428, EBI-4319440 | |
BINARY | P09693 | KTN1 Q86UP2-3 | 3 | EBI-3862428, EBI-12007212 | |
BINARY | P09693 | LAT O43561-2 | 3 | EBI-3862428, EBI-8070286 | |
BINARY | P09693 | MAL P21145 | 3 | EBI-3862428, EBI-3932027 | |
BINARY | P09693 | PMP22 Q01453 | 3 | EBI-3862428, EBI-2845982 | |
BINARY | P09693 | TMEM19 Q96HH6 | 3 | EBI-3862428, EBI-741829 | |
BINARY | P09693 | TMEM203 Q969S6 | 3 | EBI-3862428, EBI-12274070 | |
BINARY | P09693 | TMEM262 E9PQX1 | 3 | EBI-3862428, EBI-17180389 | |
BINARY | P09693 | TMEM54 Q969K7 | 3 | EBI-3862428, EBI-3922833 |
Protein-protein interaction databases
Miscellaneous
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 37-94 | Ig-like | ||||
Sequence: QEDGSVLLTCDAEAKNITWFKDGKMIGFLTEDKKKWNLGSNAKDPRGMYQCKGSQNKS | ||||||
Domain | 149-177 | ITAM | ||||
Sequence: DKQTLLPNDQLYQPLKDREDDQYSHLQGN | ||||||
Motif | 153-154 | Di-leucine motif | ||||
Sequence: LL |
Domain
A di-leucine motif and a tyrosine-based motif are individually sufficient to induce both endocytosis and delivery to lysosomes.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length182
- Mass (Da)20,469
- Last updated1989-07-01 v1
- ChecksumEE65C0186FB9872B
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
J3KNA5 | J3KNA5_HUMAN | CD3G | 40 | ||
A8MUH3 | A8MUH3_HUMAN | CD3G | 138 | ||
A0A3B3IUD8 | A0A3B3IUD8_HUMAN | CD3G | 11 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X04145 EMBL· GenBank· DDBJ | CAA27764.1 EMBL· GenBank· DDBJ | mRNA | ||
X06026 EMBL· GenBank· DDBJ | CAA29428.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X06027 EMBL· GenBank· DDBJ | CAA29428.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X06028 EMBL· GenBank· DDBJ | CAA29428.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X06029 EMBL· GenBank· DDBJ | CAA29428.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X06030 EMBL· GenBank· DDBJ | CAA29428.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X06031 EMBL· GenBank· DDBJ | CAA29428.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC113830 EMBL· GenBank· DDBJ | AAI13831.1 EMBL· GenBank· DDBJ | mRNA |