COPA (gene)

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Coatomer protein complex, subunit alpha
Symbols COPA ; HEP-COP
External IDs OMIM601924 MGI1334462 HomoloGene3218 GeneCards: COPA Gene
RNA expression pattern
PBB GE COPA 208684 at tn.png
PBB GE COPA 214336 s at tn.png
More reference expression data
Species Human Mouse
Entrez 1314 12847
Ensembl ENSG00000122218 ENSMUSG00000026553
UniProt P53621 Q8CIE6
RefSeq (mRNA) NM_001098398 NM_009938
RefSeq (protein) NP_001091868 NP_034068
Location (UCSC) Chr 1:
160.26 – 160.31 Mb
Chr 1:
172.08 – 172.12 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.[3] 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]


COPA (gene) has been shown to interact with COPE[4][5][6] and COPB1.[7]


  1. ^ 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. 
  2. ^ a b "Entrez Gene: COPA coatomer protein complex, subunit alpha". 
  3. ^ 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. doi:10.1073/pnas.92.8.3229. PMC 42139. PMID 7724544. 
  4. ^ 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. PMID 16169070. 
  5. ^ 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. 
  6. ^ 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. 
  7. ^ 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. 

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