COPA (gene)

Coatomer subunit alpha is a protein that in humans is encoded by the COPA gene.[5][6]

COPA
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCOPA, HEP-COP, AILJK, coatomer protein complex subunit alpha, alpha-COP, COPI coat complex subunit alpha
External IDsOMIM: 601924 MGI: 1334462 HomoloGene: 3218 GeneCards: COPA
Gene location (Human)
Chr.Chromosome 1 (human)[1]
Band1q23.2Start160,288,594 bp[1]
End160,343,273 bp[1]
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

1314

12847

Ensembl

ENSG00000122218

ENSMUSG00000026553

UniProt

P53621

Q8CIE6

RefSeq (mRNA)

NM_004371
NM_001098398

NM_009938

RefSeq (protein)

NP_001091868
NP_004362

NP_034068

Location (UCSC)Chr 1: 160.29 – 160.34 MbChr 1: 172.08 – 172.12 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

In eukaryotic cells, protein transport between the endoplasmic reticulum and Golgi compartments is mediated in part by non-clathrin-coated vesicular coat proteins (COPs). Seven coat proteins have been identified, and they represent subunits of a complex known as coatomer. The subunits are designated alpha-COP, beta-COP, beta-prime-COP, gamma-COP, delta-COP, epsilon-COP, and zeta-COP. The alpha-COP, encoded by COPA, shares high sequence similarity with RET1, the homologous alpha subunit of the coatomer complex in yeast.[7] Also, the N-terminal 25 amino acids of alpha-COP encode the bioactive peptide, xenin, which stimulates exocrine pancreatic secretion and may act as a gastrointestinal hormone. Alternative splicing results in multiple splice forms encoding distinct isoforms.[6]

Interactions

COPA (gene) has been shown to interact with COPE[8][9][10] and COPB1.[11]

References

  1. GRCh38: Ensembl release 89: ENSG00000122218 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000026553 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Chow VT, Quek HH (July 1996). "HEP-COP, a novel human gene whose product is highly homologous to the alpha-subunit of the yeast coatomer protein complex". Gene. 169 (2): 223–7. doi:10.1016/0378-1119(95)00738-5. PMID 8647451.
  6. "Entrez Gene: COPA coatomer protein complex, subunit alpha".
  7. Gerich B, Orci L, Tschochner H, Lottspeich F, Ravazzola M, Amherdt M, Wieland F, Harter C (April 1995). "Non-clathrin-coat protein alpha is a conserved subunit of coatomer and in Saccharomyces cerevisiae is essential for growth". Proc. Natl. Acad. Sci. U.S.A. 92 (8): 3229–33. Bibcode:1995PNAS...92.3229G. doi:10.1073/pnas.92.8.3229. PMC 42139. PMID 7724544.
  8. Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
  9. Eugster A, Frigerio G, Dale M, Duden R (August 2000). "COP I domains required for coatomer integrity, and novel interactions with ARF and ARF-GAP". EMBO J. 19 (15): 3905–17. doi:10.1093/emboj/19.15.3905. PMC 306616. PMID 10921873.
  10. Faulstich D, Auerbach S, Orci L, Ravazzola M, Wegchingel S, Lottspeich F, Stenbeck G, Harter C, Wieland FT, Tschochner H (October 1996). "Architecture of coatomer: molecular characterization of delta-COP and protein interactions within the complex". J. Cell Biol. 135 (1): 53–61. doi:10.1083/jcb.135.1.53. PMC 2121028. PMID 8858162.
  11. Lowe M, Kreis TE (November 1996). "In vivo assembly of coatomer, the COP-I coat precursor". J. Biol. Chem. 271 (48): 30725–30. doi:10.1074/jbc.271.48.30725. PMID 8940050.

Further reading


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