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
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; ; lacrimal gland; ; foot; ; islet of Langerhans; ; body of femur;
	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

Last updated April 03, 2024

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]

Related Research Articles

COPI is a coatomer, a protein complex that coats vesicles transporting proteins from the cis end of the Golgi complex back to the rough endoplasmic reticulum (ER), where they were originally synthesized, and between Golgi compartments. This type of transport is retrograde transport, in contrast to the anterograde transport associated with the COPII protein. The name "COPI" refers to the specific coat protein complex that initiates the budding process on the cis-Golgi membrane. The coat consists of large protein subcomplexes that are made of seven different protein subunits, namely α, β, β', γ, δ, ε and ζ.

The coatomer is a protein complex that coats membrane-bound transport vesicles. Two types of coatomers are known:

ADP-ribosylation factor 1 is a protein that in humans is encoded by the ARF1 gene.

Coatomer subunit beta is a protein that in humans is encoded by the COPB1 gene.

Guanine nucleotide-binding protein G(z) subunit alpha is a protein that in humans is encoded by the GNAZ gene.

Regulator of G-protein signaling 19 is a protein that in humans is encoded by the RGS19 gene.

Coatomer subunit epsilon is a protein that in humans is encoded by the COPE gene.

Coatomer subunit beta is a protein that is encoded by the COPB2 gene in humans.

Coatomer subunit gamma-2 is a protein that in humans is encoded by the COPG2 gene.

Coatomer subunit gamma is a protein that in humans is encoded by the COPG gene. It is one of seven proteins in the COPI coatomer complex that coats vesicles as they bud from the Golgi complex.

ADP-ribosylation factor 5 is a protein that in humans is encoded by the ARF5 gene.

Mediator of RNA polymerase II transcription subunit 17 is an enzyme that in humans is encoded by the MED17 gene.

Conserved oligomeric Golgi complex subunit 7 is a protein that in humans is encoded by the COG7 gene.

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3 is a protein that in humans is encoded by the GNG3 gene.

Protein transport protein Sec61 subunit alpha isoform 1 is a protein that in humans is encoded by the SEC61A1 gene.

Conserved oligomeric Golgi complex subunit 1 is a protein that in humans is encoded by the COG1 gene.

Coatomer subunit zeta-1 is a protein that in humans is encoded by the COPZ1 gene.

Caveolin-2 is a protein that in humans is encoded by the CAV2 gene.

Clathrin adaptor proteins, also known as adaptins, are vesicular transport adaptor proteins associated with clathrin. These proteins are synthesized in the ribosomes, processed in the endoplasmic reticulum and transported from the Golgi apparatus to the trans-Golgi network, and from there via small carrier vesicles to their final destination compartment. The association between adaptins and clathrin are important for vesicular cargo selection and transporting. Clathrin coats contain both clathrin and adaptor complexes that link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Therefore, adaptor proteins are responsible for the recruitment of cargo molecules into a growing clathrin-coated pits. The two major types of clathrin adaptor complexes are the heterotetrameric vesicular transport adaptor proteins (AP1-5), and the monomeric GGA adaptors. Adaptins are distantly related to the other main type of vesicular transport proteins, the coatomer subunits, sharing between 16% and 26% of their amino acid sequence.

The C-terminal domain ofBeta2-adaptin is a protein domain is involved in cell trafficking by aiding import and export of substances in and out of the cell.

References

1 2 3 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.
1 2 "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.

External links

Human COPA genome location and COPA gene details page in the UCSC Genome Browser .

Feurle GE (1998). "Xenin--a review". Peptides. 19 (3): 609–15. doi:10.1016/S0196-9781(97)00378-1. PMID 9533652. S2CID 43430216.
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. doi: 10.1016/S0021-9258(18)41670-5 . 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. Bibcode:1993Natur.364..732O. doi:10.1038/364732a0. PMID 8355790. S2CID 4348442.
Lowe M, Kreis TE (1996). "In vitro assembly and disassembly of coatomer". J. Biol. Chem. 270 (52): 31364–71. doi: 10.1074/jbc.270.52.31364 . PMID 8537409.
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. Bibcode:1996Sci...273.1396F. doi:10.1126/science.273.5280.1396. PMID 8703076. S2CID 13159384.
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. doi:10.1083/jcb.135.1.53. PMC 2121028 . PMID 8858162.
Lowe M, Kreis TE (1997). "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.
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. doi:10.1089/dna.1997.16.275. 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. doi:10.1159/000134532. 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. S2CID 41227737.
Pavel J, Harter C, Wieland FT (1998). "Reversible dissociation of coatomer: Functional characterization of a β/δ-coat protein subcomplex". Proc. Natl. Acad. Sci. U.S.A. 95 (5): 2140–5. Bibcode:1998PNAS...95.2140P. doi: 10.1073/pnas.95.5.2140 . PMC 19276 . PMID 9482852.
Harter C, Wieland FT (1998). "A single binding site for dilysine retrieval motifs and p23 within the γ subunit of coatomer". Proc. Natl. Acad. Sci. U.S.A. 95 (20): 11649–54. Bibcode:1998PNAS...9511649H. doi: 10.1073/pnas.95.20.11649 . PMC 21695 . 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. PMC 2173491 . 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" (PDF). Mol. Biol. Cell. 13 (10): 3493–507. doi:10.1091/mbc.E02-01-0004. PMC 129961 . 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. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . 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. doi:10.1016/S0168-8278(02)00412-9. PMID 12586295.

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[refGRCm38Ensembl-1] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000026553 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8647451-4] 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.

[entrez-5] 1 2 "Entrez Gene: COPA coatomer protein complex, subunit alpha".

[pmid7724544-6] 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.

[pmid16169070-7] 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.

[pmid10921873-8] 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.

[pmid8858162-9] 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.

[pmid8940050-10] 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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