COPA (gene)

From Wikipedia, the free encyclopedia


Coatomer protein complex, subunit alpha
Identifiers
Symbol(s) COPA; FLJ26320; HEP-COP
External IDs OMIM: 601924 MGI1334462 HomoloGene3218
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 1314 12847
Ensembl ENSG00000122218 ENSMUSG00000026553
Uniprot P53621 n/a
Refseq NM_004371 (mRNA)
NP_004362 (protein)
NM_009938 (mRNA)
NP_034068 (protein)
Location Chr 1: 158.53 - 158.58 Mb Chr 1: 173.92 - 173.96 Mb
Pubmed search [1] [2]

Coatomer protein complex, subunit alpha, also known as COPA, is a human gene.[1]

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.[1]

[edit] References

[edit] Further reading

  • Feurle GE (1998). "Xenin--a review.". Peptides 19 (3): 609–15. PMID 9533652. 
  • Feurle GE, Hamscher G, Kusiek R, et al. (1992). "Identification of xenin, a xenopsin-related peptide, in the human gastric mucosa and its effect on exocrine pancreatic secretion.". J. Biol. Chem. 267 (31): 22305–9. PMID 1429581. 
  • Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol.". Nature 364 (6439): 732–4. doi:10.1038/364732a0. PMID 8355790. 
  • Lowe M, Kreis TE (1996). "In vitro assembly and disassembly of coatomer.". J. Biol. Chem. 270 (52): 31364–71. PMID 8537409. 
  • Chow VT, Quek HH (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. PMID 8647451. 
  • Fiedler K, Veit M, Stamnes MA, Rothman JE (1996). "Bimodal interaction of coatomer with the p24 family of putative cargo receptors.". Science 273 (5280): 1396–9. PMID 8703076. 
  • Faulstich D, Auerbach S, Orci L, et al. (1996). "Architecture of coatomer: molecular characterization of delta-COP and protein interactions within the complex.". J. Cell Biol. 135 (1): 53–61. PMID 8858162. 
  • Lowe M, Kreis TE (1997). "In vivo assembly of coatomer, the COP-I coat precursor.". J. Biol. Chem. 271 (48): 30725–30. PMID 8940050. 
  • Quek HH, Chow VT (1997). "Molecular and cellular studies of the human homolog of the 160-kD alpha-subunit of the coatomer protein complex.". DNA Cell Biol. 16 (3): 275–80. PMID 9115636. 
  • Quek HH, Chow VT (1997). "Genomic organization and mapping of the human HEP-COP gene (COPA) to 1q.". Cytogenet. Cell Genet. 76 (3-4): 139–43. PMID 9186507. 
  • Hansen K, Rönnstrand L, Rorsman C, et al. (1997). "Association of coatomer proteins with the beta-receptor for platelet-derived growth factor.". Biochem. Biophys. Res. Commun. 235 (3): 455–60. doi:10.1006/bbrc.1997.6821. PMID 9207175. 
  • Chow VT, Quek HH (1997). "Alpha coat protein COPA (HEP-COP): presence of an Alu repeat in cDNA and identity of the amino terminus to xenin.". Ann. Hum. Genet. 61 (Pt 4): 369–73. doi:10.1046/j.1469-1809.1997.6140369.x. PMID 9365789. 
  • Pavel J, Harter C, Wieland FT (1998). "Reversible dissociation of coatomer: functional characterization of a beta/delta-coat protein subcomplex.". Proc. Natl. Acad. Sci. U.S.A. 95 (5): 2140–5. PMID 9482852. 
  • Harter C, Wieland FT (1998). "A single binding site for dilysine retrieval motifs and p23 within the gamma subunit of coatomer.". Proc. Natl. Acad. Sci. U.S.A. 95 (20): 11649–54. PMID 9751720. 
  • Zhang T, Hong W (2001). "Ykt6 forms a SNARE complex with syntaxin 5, GS28, and Bet1 and participates in a late stage in endoplasmic reticulum-Golgi transport.". J. Biol. Chem. 276 (29): 27480–7. doi:10.1074/jbc.M102786200. PMID 11323436. 
  • Yang JS, Lee SY, Gao M, et al. (2002). "ARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coat.". J. Cell Biol. 159 (1): 69–78. doi:10.1083/jcb.200206015. PMID 12379802. 
  • Xu Y, Martin S, James DE, Hong W (2003). "GS15 forms a SNARE complex with syntaxin 5, GS28, and Ykt6 and is implicated in traffic in the early cisternae of the Golgi apparatus.". Mol. Biol. Cell 13 (10): 3493–507. doi:10.1091/mbc.E02-01-0004. PMID 12388752. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Wong N, Chan A, Lee SW, et al. (2003). "Positional mapping for amplified DNA sequences on 1q21-q22 in hepatocellular carcinoma indicates candidate genes over-expression.". J. Hepatol. 38 (3): 298–306. PMID 12586295.