Alt. symbols: COPG

Approved name: COPI coat complex subunit gamma 1
Alt. names: coatomer protein complex, subunit gamma, coatomer protein complex, subunit gamma 1 | coat protein gamma-cop

Location: 3q21.3: 129249606 - 129277773 (+)
Gene type: protein_coding, 10 transcripts.

Scores: LoFtool: | pLI: 0.99849931 | LOEUF: 0.397

HGNC: 2236

NCBI: 22820, RefSeq: .0

Ensembl: ENSG00000181789.14

LRG_ | Status: none

OMIM: 615525

Expression | ProteinAtlas

Gene Ontology (GO)

• Molecular function:
• Cell component: endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum [GO:0005783]; Golgi membrane [GO:0000139]; COPI vesicle coat [GO:0030126]
• Biological process: endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; organelle transport along microtubule [GO:0072384]; protein secretion [GO:0009306]; intra-Golgi vesicle-mediated transport [GO:0006891]

Normal function

Dysfunction and disease

Biallelic mutations in this have have been linked to a subtype of combined immunodeficiency. In the study first describing this condition, patient fibroblasts showed comparable (to WT) expression levels of the mutant protein and co-immunoprecipitation assays suggested that mutant COPG1 integrated normally into the COPI complex. However, those patient fibroblasts showed impaired retrograde COPI transport, and direct binding of the mutant COPG1-K652E coatomer to the KDELR1 protein was disrupted. N evertheless, binding to ARFGAP1 was retained and that may have compensated for the defect. Vesicle formation was unaffected. Interestingly, embryonic fibroblasts from mutant mice expressing the K652E mutation, showed similar defects. The authors concluded that the impaired retrieval of KDEL-bearing chaperones to the ER causes exaggerated ER stress in activated B and T cells. [Load More]