COPA (gene)

Coatomer protein complex, subunit alpha
Identifiers
Symbols COPA; FLJ26320; HEP-COP
External IDs OMIM601924 MGI1334462 HomoloGene3218 GeneCards: COPA Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 1314 12847
Ensembl ENSG00000122218 ENSMUSG00000026553
UniProt P53621 n/a
RefSeq (mRNA) NM_001098398.1 NM_009938.4
RefSeq (protein) NP_001091868.1 NP_034068.3
Location (UCSC) Chr 1:
160.26 – 160.31 Mb
Chr 1:
174.01 – 174.05 Mb
PubMed search [1] [2]

Coatomer subunit alpha is a protein that in humans is encoded by the COPA gene.[1][2]

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 RET1P, the alpha subunit of the coatomer complex in yeast. 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.[2]

Interactions

COPA (gene) has been shown to interact with COPE[3][4][5] and COPB1.[4][6]

References

  1. ^ Chow VT, Quek HH (Jul 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. 
  2. ^ a b "Entrez Gene: COPA coatomer protein complex, subunit alpha". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1314. 
  3. ^ Stelzl, Ulrich; Worm Uwe, Lalowski Maciej, Haenig Christian, Brembeck Felix H, Goehler Heike, Stroedicke Martin, Zenkner Martina, Schoenherr Anke, Koeppen Susanne, Timm Jan, Mintzlaff Sascha, Abraham Claudia, Bock Nicole, Kietzmann Silvia, Goedde Astrid, Toksöz Engin, Droege Anja, Krobitsch Sylvia, Korn Bernhard, Birchmeier Walter, Lehrach Hans, Wanker Erich E (Sep. 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell (United States) 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. ISSN 0092-8674. PMID 16169070. 
  4. ^ a b Eugster, A; Frigerio G, Dale M, Duden R (Aug. 2000). "COP I domains required for coatomer integrity, and novel interactions with ARF and ARF-GAP". EMBO J. (ENGLAND) 19 (15): 3905–17. doi:10.1093/emboj/19.15.3905. ISSN 0261-4189. PMC 306616. PMID 10921873. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=306616. 
  5. ^ Faulstich, D; Auerbach S, Orci L, Ravazzola M, Wegchingel S, Lottspeich F, Stenbeck G, Harter C, Wieland F T, Tschochner H (Oct. 1996). "Architecture of coatomer: molecular characterization of delta-COP and protein interactions within the complex". J. Cell Biol. (UNITED STATES) 135 (1): 53–61. doi:10.1083/jcb.135.1.53. ISSN 0021-9525. PMC 2121028. PMID 8858162. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2121028. 
  6. ^ Lowe, M; Kreis T E (Nov. 1996). "In vivo assembly of coatomer, the COP-I coat precursor". J. Biol. Chem. (UNITED STATES) 271 (48): 30725–30. doi:10.1074/jbc.271.48.30725. ISSN 0021-9258. PMID 8940050. 

Further reading