COPG

COPG1

Identifiers

COPG1, COPG, coatomer protein complex subunit gamma 1, COPI coat complex subunit gamma 1

External IDs

OMIM: 615525; MGI: 1858696; GeneCards: COPG1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1R4X

Gene location (Human)

Chr.	Chromosome 3 (human)

Band	3q21.3	Start	129,249,606 bp
Band	3q21.3	End	129,277,773 bp

Gene location (Mouse)

Chr.	Chromosome 6 (mouse)

Band	6 D1\|6 39.13 cM	Start	87,864,796 bp
Band	6 D1\|6 39.13 cM	End	87,890,577 bp

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

stromal cell of endometrium

anterior pituitary

body of pancreas

mucosa of transverse colon

islet of Langerhans

minor salivary glands

right lobe of thyroid gland

body of stomach

right adrenal gland

rectum

Top expressed in

yolk sac

dentate gyrus of hippocampal formation granule cell

molar

superior frontal gyrus

supraoptic nucleus

pituitary gland

dermis

central gray substance of midbrain

islet of Langerhans

crypt of lieberkuhn of small intestine

More reference expression data


More reference expression data

Gene ontology
Molecular function	protein binding structural molecule activity
Cellular component	cytoplasm membrane coat COPI-coated vesicle membrane membrane transport vesicle cytosol cytoplasmic vesicle Golgi apparatus Golgi membrane COPI vesicle coat endoplasmic reticulum membrane endoplasmic reticulum endoplasmic reticulum-Golgi intermediate compartment
Biological process	retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum protein transport organelle transport along microtubule intracellular protein transport establishment of Golgi localization endoplasmic reticulum to Golgi vesicle-mediated transport vesicle-mediated transport intra-Golgi vesicle-mediated transport protein secretion
Sources:Amigo / QuickGO

Databases

NCBI: entry; OMA: entry

Species

Human

Mouse


22820


54161


ENSG00000181789


ENSMUSG00000030058


Q9Y678


Q9QZE5

RefSeq (mRNA)


NM_016128


NM_017477 NM_201244

RefSeq (protein)


NP_057212


NP_059505 NP_957696

Location (UCSC)

Chr 3: 129.25 – 129.28 Mb

Chr 6: 87.86 – 87.89 Mb

PubMed search

View/Edit Human

View/Edit Mouse

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.

Interactions

COPG has been shown to interact with Dopamine receptor D1, COPZ1 and COPB1.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000181789 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000030058 – 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.
1 2 3 4 Futatsumori M, Kasai K, Takatsu H, Shin HW, Nakayama K (February 2001). "Identification and characterization of novel isoforms of COP I subunits". J Biochem. 128 (5): 793–801. doi:10.1093/oxfordjournals.jbchem.a022817. PMID 11056392.
↑ "Entrez Gene: COPG coatomer protein complex, subunit gamma".
↑ Bermak, Jason C; Li Ming; Bullock Clayton; Weingarten Paul; Zhou Qun-Yong (February 2002). "Interaction of gamma-COP with a transport motif in the D1 receptor C-terminus". Eur. J. Cell Biol. 81 (2). Germany: 77–85. doi:10.1078/0171-9335-00222. ISSN 0171-9335. PMID 11893085.
↑ Faulstich, D; Auerbach S; Orci L; Ravazzola M; Wegchingel S; Lottspeich F; Stenbeck G; Harter C; Wieland F T; Tschochner H (October 1996). "Architecture of coatomer: molecular characterization of delta-COP and protein interactions within the complex" (PDF). J. Cell Biol. 135 (1). UNITED STATES: 53–61. doi:10.1083/jcb.135.1.53. ISSN 0021-9525. PMC 2121028. PMID 8858162.
↑ Lowe, M; Kreis T E (November 1996). "In vivo assembly of coatomer, the COP-I coat precursor". J. Biol. Chem. 271 (48). UNITED STATES: 30725–30. doi:10.1074/jbc.271.48.30725. ISSN 0021-9258. PMID 8940050.

External links

Human COPG1 genome location and COPG1 gene details page in the UCSC Genome Browser.

Further reading

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.
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. Bibcode:1998PNAS...95.2140P. doi:10.1073/pnas.95.5.2140. PMC 19276. PMID 9482852.
Fischer KD, Helms JB, Zhao L, Wieland FT (2000). "Site-specific photocrosslinking to probe interactions of Arf1 with proteins involved in budding of COPI vesicles". Methods. 20 (4): 455–64. doi:10.1006/meth.2000.0958. PMID 10720466.
Eugster A, Frigerio G, Dale M, Duden R (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.
Hu RM, Han ZG, Song HD, et al. (2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 97 (17): 9543–8. Bibcode:2000PNAS...97.9543H. doi:10.1073/pnas.160270997. PMC 16901. PMID 10931946.
Sullivan BM, Harrison-Lavoie KJ, Marshansky V, et al. (2000). "RGS4 and RGS2 bind coatomer and inhibit COPI association with Golgi membranes and intracellular transport". Mol. Biol. Cell. 11 (9): 3155–68. doi:10.1091/mbc.11.9.3155. PMC 14982. PMID 10982407.
Hahn Y, Lee YJ, Yun JH, et al. (2000). "Duplication of genes encoding non-clathrin coat protein gamma-COP in vertebrate, insect and plant evolution". FEBS Lett. 482 (1–2): 31–6. doi:10.1016/S0014-5793(00)02033-0. PMID 11018518. S2CID 36356269.
Paulsson KM, Kleijmeer MJ, Griffith J, et al. (2002). "Association of tapasin and COPI provides a mechanism for the retrograde transport of major histocompatibility complex (MHC) class I molecules from the Golgi complex to the endoplasmic reticulum". J. Biol. Chem. 277 (21): 18266–71. doi:10.1074/jbc.M201388200. PMID 11884415.
Bermak JC, Li M, Bullock C, et al. (2002). "Interaction of gamma-COP with a transport motif in the D1 receptor C-terminus". Eur. J. Cell Biol. 81 (2): 77–85. doi:10.1078/0171-9335-00222. PMID 11893085.
Kanzaki M, Watson RT, Hou JC, et al. (2003). "Small GTP-binding protein TC10 differentially regulates two distinct populations of filamentous actin in 3T3L1 adipocytes". Mol. Biol. Cell. 13 (7): 2334–46. doi:10.1091/mbc.01-10-0490. PMC 117317. PMID 12134073.
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. 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.
Rohde HM, Cheong FY, Konrad G, et al. (2004). "The human phosphatidylinositol phosphatase SAC1 interacts with the coatomer I complex". J. Biol. Chem. 278 (52): 52689–99. doi:10.1074/jbc.M307983200. PMID 14527956.
Watson PJ, Frigerio G, Collins BM, et al. (2004). "Gamma-COP appendage domain - structure and function". Traffic. 5 (2): 79–88. doi:10.1111/j.1600-0854.2004.00158.x. PMID 14690497. S2CID 24249308.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

v t e PDB gallery
1pzd: Structural Identification of a conserved appendage domain in the carboxyl-terminus of the COPI gamma-subunit. 1r4x: Crystal Structure Analys of the Gamma-COPI Appendage domain

Membrane protein: vesicular transport proteins (TC 1F)

Synaptic vesicle

Q-SNARE	SNAP25 SNAP29 Syntaxin STX1A STX1B STX2 STX3 STX4 STX5 STX6 STX7 STX8 STX10 STX11 STX12 STX16 STX17 STX18 STX19 Munc-18: STXBP1 STXBP2 STXBP3 STXBP4 STXBP5 STXBP6
R-SNARE	Synaptobrevin/VAMP: VAMP1 VAMP2 VAMP3

Other

Small GTPase: RAB3A

Coatomer
- COPA
- COPB1
- COPB2
- COPD/Archain
- COPE
- COPG
- COPG2
- COPZ1
- COPZ2

Small GTPase: ARF

Coatomer
- SEC23A/SEC24A
- SEC13/SEC31

Small GTPase: SAR1A

Other/ungrouped

Vesicle formation

Adaptor protein complex 1:	AP1AR AP1B1 AP1G1 AP1G2 AP1M1 AP1M2 AP1S1 AP1S2 AP1S3
Adaptor protein complex 2:	AP2A1 AP2A2 AP2B1 AP2M1 AP2S1
Adaptor protein complex 3:	AP3B1 AP3B2 AP3D1 AP3M1 AP3M2 AP3S1 AP3S2
Adaptor protein complex 4:	AP4B1 AP4E1 AP4M1 AP4S1
LMAN1
LYST
BLOC-1:	DTNBP1 BLOC153
BLOC-2:	HPS3 HPS5 HPS6
BLOC-3:	HPS1 HPS4
Coats:	Retromer TIP47

Dynamin
- DNM1
- DNM2
- DNM3

Other

Sorting nexins

SYNRG

See also vesicular transport protein disorders

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