SCO1

From Wikipedia, the free encyclopedia

SCO cytochrome oxidase deficient homolog 1 (yeast)

PDB rendering based on 1wp0.

Available structures: 1wp0, 2ggt, 2gqk, 2gql, 2gqm, 2gt5, 2gt6, 2gvp, 2hrf, 2hrn

Identifiers

Symbol(s)

SCO1; SCOD1

External IDs

OMIM: 603644 MGI: 106362 HomoloGene: 3374

Gene ontology
Molecular Function:	• copper ion binding • metal ion binding
Cellular Component:	• mitochondrion
Biological Process:	• electron transport • protein folding • cytochrome c oxidase complex assembly

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_004589 (mRNA)
NP_004580 (protein)

XM_901619 (mRNA)
XP_906712 (protein)

Location

Chr 17: 10.52 - 10.54 Mb

Chr 11: 66.87 - 66.88 Mb

Pubmed search

[1]

[2]

SCO cytochrome oxidase deficient homolog 1 (yeast), also known as SCO1, is a human gene.^[1]

Mammalian cytochrome c oxidase (COX) catalyzes the transfer of reducing equivalents from cytochrome c to molecular oxygen and pumps protons across the inner mitochondrial membrane. In yeast, 2 related COX assembly genes, SCO1 and SCO2 (synthesis of cytochrome c oxidase), enable subunits 1 and 2 to be incorporated into the holoprotein. This gene is the human homolog to the yeast SCO1 gene.^[1]

[edit] References

^ ^a ^b Entrez Gene: SCO1 SCO cytochrome oxidase deficient homolog 1 (yeast).

[edit] Further reading

Shoubridge EA (2001). "Cytochrome c oxidase deficiency.". Am. J. Med. Genet. 106 (1): 46–52. doi:10.1002/ajmg.1378. PMID 11579424.
Schulze M, Rödel G (1989). "Accumulation of the cytochrome c oxidase subunits I and II in yeast requires a mitochondrial membrane-associated protein, encoded by the nuclear SCO1 gene.". Mol. Gen. Genet. 216 (1): 37–43. PMID 2543907.
Schulze M, Rödel G (1988). "SCO1, a yeast nuclear gene essential for accumulation of mitochondrial cytochrome c oxidase subunit II.". Mol. Gen. Genet. 211 (3): 492–8. PMID 2835635.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353–8. PMID 9110174.
Petruzzella V, Tiranti V, Fernandez P, et al. (1999). "Identification and characterization of human cDNAs specific to BCS1, PET112, SCO1, COX15, and COX11, five genes involved in the formation and function of the mitochondrial respiratory chain.". Genomics 54 (3): 494–504. doi:10.1006/geno.1998.5580. PMID 9878253.
Paret C, Ostermann K, Krause-Buchholz U, et al. (1999). "Human members of the SCO1 gene family: complementation analysis in yeast and intracellular localization.". FEBS Lett. 447 (1): 65–70. PMID 10218584.
Papadopoulou LC, Sue CM, Davidson MM, et al. (1999). "Fatal infantile cardioencephalomyopathy with COX deficiency and mutations in SCO2, a COX assembly gene.". Nat. Genet. 23 (3): 333–7. doi:10.1038/15513. PMID 10545952.
Valnot I, Osmond S, Gigarel N, et al. (2000). "Mutations of the SCO1 gene in mitochondrial cytochrome c oxidase deficiency with neonatal-onset hepatic failure and encephalopathy.". Am. J. Hum. Genet. 67 (5): 1104–9. PMID 11013136.
Horvath R, Lochmüller H, Stucka R, et al. (2000). "Characterization of human SCO1 and COX17 genes in mitochondrial cytochrome-c-oxidase deficiency.". Biochem. Biophys. Res. Commun. 276 (2): 530–3. doi:10.1006/bbrc.2000.3495. PMID 11027508.
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.
Leary SC, Kaufman BA, Pellecchia G, et al. (2005). "Human SCO1 and SCO2 have independent, cooperative functions in copper delivery to cytochrome c oxidase.". Hum. Mol. Genet. 13 (17): 1839–48. doi:10.1093/hmg/ddh197. PMID 15229189.
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. PMID 15489334.
Williams JC, Sue C, Banting GS, et al. (2005). "Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein.". J. Biol. Chem. 280 (15): 15202–11. doi:10.1074/jbc.M410705200. PMID 15659396.
Horng YC, Leary SC, Cobine PA, et al. (2005). "Human Sco1 and Sco2 function as copper-binding proteins.". J. Biol. Chem. 280 (40): 34113–22. doi:10.1074/jbc.M506801200. PMID 16091356.
Cobine PA, Pierrel F, Leary SC, et al. (2006). "The P174L mutation in human Sco1 severely compromises Cox17-dependent metallation but does not impair copper binding.". J. Biol. Chem. 281 (18): 12270–6. doi:10.1074/jbc.M600496200. PMID 16520371.
Banci L, Bertini I, Calderone V, et al. (2006). "A hint for the function of human Sco1 from different structures.". Proc. Natl. Acad. Sci. U.S.A. 103 (23): 8595–600. doi:10.1073/pnas.0601375103. PMID 16735468.
Leary SC, Cobine PA, Kaufman BA, et al. (2007). "The human cytochrome c oxidase assembly factors SCO1 and SCO2 have regulatory roles in the maintenance of cellular copper homeostasis.". Cell Metab. 5 (1): 9–20. doi:10.1016/j.cmet.2006.12.001. PMID 17189203.