COPA (gene)

COPA
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	5A1U, 5A1V, 5A1W, 5A1X, 5A1Y
Identifiers
Aliases	COPA, HEP-COP, AILJK, coatomer protein complex subunit alpha, alpha-COP, COPI coat complex subunit alpha
External IDs	OMIM: 601924; MGI: 1334462; HomoloGene: 3218; GeneCards: COPA; OMA:COPA - orthologs
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	171,949,897 bp
RNA expression pattern
	Top expressed in
	stromal cell of endometrium; ; islet of Langerhans; ; pituitary gland; ; ganglionic eminence; ; anterior pituitary; ; inferior ganglion of vagus nerve; ; corpus callosum; ; smooth muscle tissue; ; pylorus; ; cardia;
	Top expressed in
	calvaria; ; molar; ; ascending aorta; ; dermis; ; aortic valve; ; parotid gland; ; stroma of bone marrow; ; genital tubercle; ; lacrimal gland; ; foot;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	hormone activity; structural molecule activity;
Cellular component	cytoplasm; cytosol; Golgi apparatus; membrane; Golgi membrane; COPI-coated vesicle membrane; transport vesicle; extracellular region; membrane coat; COPI vesicle coat; extracellular exosome; cytoplasmic vesicle; endoplasmic reticulum membrane; extracellular space;
Biological process	retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; pancreatic juice secretion; endoplasmic reticulum to Golgi vesicle-mediated transport; protein transport; intracellular protein transport; intra-Golgi vesicle-mediated transport; vesicle-mediated transport; transport; regulation of signaling receptor activity; signal transduction;
	Sources:Amigo / QuickGO
Orthologs
	1314
	12847
	n/a
	ENSMUSG00000026553
	P53621
	Q8CIE6
	NM_004371; NM_001098398
	NM_009938
	NP_001091868; NP_004362
	NP_034068
	Wikidata
View/Edit Human	View/Edit Mouse

Coatomer subunit alpha is a protein that in humans is encoded by the COPA gene.^[4]^[5]

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.^[6] 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.^[5]

Interactions

COPA (gene) has been shown to interact with COPE^[7]^[8]^[9] and COPB1.^[10]

References

^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000026553 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ ^a ^b "Entrez Gene: COPA coatomer protein complex, subunit alpha".
^ 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.
^ 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.
^ 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.
^ 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.
^ 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.