# SCO2

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Protein-coding gene in the species Homo sapiens

For sCO2, the phase of carbon dioxide, see [supercritical carbon dioxide](/source/Supercritical_carbon_dioxide).

SCO2 Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2RLI Identifiers Aliases SCO2, CEMCOX1, MYP6, SCO1L, SCO2 cytochrome c oxidase assembly protein, cytochrome c oxidase assembly protein, PD-ECGF, TP, Gliostatin, TYMP, ECGF1, TdRPase, SCO cytochrome c oxidase assembly protein 2, synthesis of cytochrome C oxidase 2, MC4DN2 External IDs OMIM: 604272; MGI: 3818630; HomoloGene: 68444; GeneCards: SCO2; OMA:SCO2 - orthologs Gene location (Human) Chr. Chromosome 22 (human)[1] Band 22q13.33 Start 50,523,568 bp[1] End 50,526,461 bp[1] Gene location (Mouse) Chr. Chromosome 15 (mouse)[2] Band 15|15 E3 Start 89,255,840 bp[2] End 89,258,049 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right uterine tube granulocyte mucosa of transverse colon monocyte gingival epithelium gonad palpebral conjunctiva periodontal fiber right lobe of liver epithelium of bronchus Top expressed in yolk sac blastocyst embryo duodenum colon proximal tubule right kidney muscle of thigh jejunum morula More reference expression data BioGPS n/a Gene ontology Molecular function protein binding copper ion binding metal ion binding protein-disulfide reductase activity Cellular component myofibril mitochondrial matrix mitochondrial inner membrane mitochondrion integral component of mitochondrial inner membrane membrane integral component of membrane Biological process cellular copper ion homeostasis copper ion transport eye development respiratory chain complex IV assembly cell redox homeostasis mitochondrial cytochrome c oxidase assembly Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 9997 100126824 Ensembl ENSG00000284194 ENSMUSG00000091780 UniProt O43819 Q8VCL2 RefSeq (mRNA) NM_005138 NM_001169109 NM_001169110 NM_001169111 NM_001111288 RefSeq (protein) NP_001162580 NP_001162581 NP_001162582 NP_005129 NP_001104758 Location (UCSC) Chr 22: 50.52 – 50.53 Mb Chr 15: 89.26 – 89.26 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**SCO2 cytochrome c oxidase assembly** (also known as **SCO2 homolog, mitochondrial** and **SCO cytochrome oxidase deficient homolog 2**) is a [protein](/source/Protein) that in humans is encoded by the *SCO2* [gene](/source/Gene).[5][6][7] The encoded protein is one of the [cytochrome c oxidase (COX)](/source/Cytochrome_c_oxidase)(Complex IV) assembly factors. Human [COX](/source/Cytochrome_c_oxidase) is a multimeric [protein complex](/source/Protein_complex) that requires several assembly factors. [Cytochrome c oxidase (COX)](/source/Cytochrome_c_oxidase) [catalyzes](/source/Catalysis) the transfer of electrons from [cytochrome c](/source/Cytochrome_c) to [molecular oxygen](/source/Molecular_oxygen), which helps to maintain the [proton gradient](/source/Proton_gradient) across the [inner mitochondrial membrane](/source/Inner_mitochondrial_membrane) that is necessary for aerobic [ATP](/source/Adenosine_triphosphate) production. The encoded protein is a [metallochaperone](/source/Chaperone_(protein)) that is involved in the biogenesis of [cytochrome c oxidase subunit II](/source/Cytochrome_c_oxidase_subunit_II). Mutations in this gene are associated with fatal infantile encephalocardiomyopathy and [myopia](/source/Myopia) 6.[7]

## Structure

The *SCO2* gene is located on the [q arm](/source/Locus_(genetics)) of [chromosome 22](/source/Chromosome_22) at position 13.33 and it spans 2,871 base pairs.[7] The *SCO2* gene produces a 15.1 kDa protein composed of 136 [amino acids](/source/Amino_acids).[8][9] The protein contains an [N-terminal](/source/N-terminal) mitochondrial targeting presequence of 41 [amino acids](/source/Amino_acids), and shares identity with the [yeast](/source/Yeast) protein in regions between [glycine](/source/Glycine)-102 and [glycine](/source/Glycine)-242 in human SCO2.[10] SCO2 is a subunit of the enzyme [Mammalian cytochrome c oxidase (COX)](/source/Cytochrome_c_oxidase)(Complex IV).[7]

## Function

The *SCO2* gene encodes for a [protein](/source/Protein) essential for the assembly and function of [Mammalian cytochrome c oxidase (COX)](/source/Cytochrome_c_oxidase)(Complex IV) of the [mitochondrial respiratory chain](/source/Mitochondrial_respiratory_chain). SCO2 acts as a [metallochaperone](/source/Chaperone_(protein)) involved in the [biogenesis](/source/Biogenesis) of [cytochrome c oxidase subunit II](/source/Cytochrome_c_oxidase_subunit_II), an essential subunit of [Complex IV](/source/Cytochrome_c_oxidase) which transfers the electrons from [cytochrome c](/source/Cytochrome_c) to the bimetallic center of the [catalytic subunit 1](/source/Cytochrome_c_oxidase_subunit_I) via its binuclear copper A center.[11] The biogenesis involves the transport of copper to the Cu(A) site on the [cytochrome c oxidase subunit II](/source/Cytochrome_c_oxidase_subunit_II) leading to the proper synthesis and maturation of the subunit. In addition, SCO2 acts as a [thiol](/source/Thiol)-[disulfide](/source/Disulfide) [oxidoreductase](/source/Oxidoreductase) to regulate the redox state of the [cysteines](/source/Cystein) in [SCO1](/source/SCO1) during maturation of the [cytochrome c oxidase subunit II](/source/Cytochrome_c_oxidase_subunit_II). The maturation and synthesis of [cytochrome c oxidase subunit II](/source/Cytochrome_c_oxidase_subunit_II) is required for the function of [Mammalian cytochrome c oxidase (COX)](/source/Cytochrome_c_oxidase)(Complex IV).[12][13][Complex IV](/source/Cytochrome_c_oxidase), a multimeric [protein complex](/source/Protein_complex) that requires several assembly factors, [catalyzes](/source/Catalysis) the transfer of reducing equivalents from [cytochrome c](/source/Cytochrome_c) to molecular [oxygen](/source/Oxygen) and pumps [protons](/source/Protons) across the [inner mitochondrial membrane](/source/Inner_mitochondrial_membrane).[7]

## Clinical significance

Mutations in *SCO2* that alter the regulation of [copper](/source/Copper) and [oxygen](/source/Oxygen) have been found to be associated with fatal infantile Cardioencephalomyopathy due to cytochrome c oxidase deficiency 1 (CEMCOX1), [Myopia 6](/source/Myopia) (MYP6), and [Leigh syndrome](/source/Leigh_syndrome) (LS).[14][12] CEMCOX1 is characterized by disorders characterized by [hypotonia](/source/Hypotonia), [developmental delay](/source/Developmental_disability), [hypertrophic cardiomyopathy](/source/Hypertrophic_cardiomyopathy), [lactic acidosis](/source/Lactic_acidosis), [gliosis](/source/Gliosis), neuronal loss in [basal ganglia](/source/Basal_ganglia), [brainstem](/source/Brainstem) and [spinal cord](/source/Spinal_cord), and [cytochrome c oxidase](/source/Cytochrome_c_oxidase) deficiency. [Myopia 6](/source/Myopia) is characterized by a [refractive](/source/Refraction) error of the eye, in which parallel rays from a distant object come to focus in front of the [retina](/source/Retina), vision being better for near objects than for far. Lastly, [leigh syndrome](/source/Leigh_syndrome) is an early-onset progressive [neurodegenerative disorder](/source/Neurodegeneration) characterized by the presence of focal, bilateral [lesions](/source/Lesion) in one or more areas of the [central nervous system](/source/Central_nervous_system) including the [brainstem](/source/Brainstem), [thalamus](/source/Thalamus), [basal ganglia](/source/Basal_ganglia), [cerebellum](/source/Cerebellum) and [spinal cord](/source/Spinal_cord). Clinical manifestations may include [psychomotor retardation](/source/Psychomotor_retardation), [hypotonia](/source/Hypotonia), [ataxia](/source/Ataxia), weakness, [vision loss](/source/Vision_loss), [eye movement](/source/Eye_movement) abnormalities, [seizures](/source/Seizures), and [dysphagia](/source/Dysphagia).[12] A pathogenic mutation of G1541A in a patient has shown strong evidence in neonatal [hypotonia](/source/Hypotonia) with an SMA 1 phenotype, and has been found to result in less [COX](/source/Cytochrome_c_oxidase) deficiencies.[15] A mutation of 1602T>G has been found to result in rapidly progressive disease [phenotypes](/source/Phenotypes).[16] Other pathogenic mutations have included a [missense mutation](/source/Missense_mutation) of E140K, a [nonsense mutation](/source/Nonsense_mutation) Q53X, and a 1541G > A mutation which resulted in a severe protein instability.[17][18][19]

## Interactions

In addition to co-complex interactions, SCO2 has been found to interact with [COA6](/source/COA6), [THEM177](https://en.wikipedia.org/w/index.php?title=THEM177&action=edit&redlink=1) in a [COX20](/source/COX20)-dependent manner, [COX20](/source/COX20), [COX16](https://en.wikipedia.org/w/index.php?title=COX16&action=edit&redlink=1), [SCO1](/source/SCO1), and others.[12][20]

## References

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## Further reading

- Jaksch M, Ogilvie I, Yao J, Kortenhaus G, Bresser HG, Gerbitz KD, Shoubridge EA (March 2000). ["Mutations in SCO2 are associated with a distinct form of hypertrophic cardiomyopathy and cytochrome c oxidase deficiency"](https://doi.org/10.1093%2Fhmg%2F9.5.795). *Human Molecular Genetics*. **9** (5): 795–801. [doi](/source/Doi_(identifier)):[10.1093/hmg/9.5.795](https://doi.org/10.1093%2Fhmg%2F9.5.795). [PMID](/source/PMID_(identifier)) [10749987](https://pubmed.ncbi.nlm.nih.gov/10749987).

- Jaksch M, Horvath R, Horn N, Auer DP, Macmillan C, Peters J, Gerbitz KD, Kraegeloh-Mann I, Muntau A, Karcagi V, Kalmanchey R, Lochmuller H, Shoubridge EA, Freisinger P (October 2001). "Homozygosity (E140K) in SCO2 causes delayed infantile onset of cardiomyopathy and neuropathy". *Neurology*. **57** (8): 1440–6. [doi](/source/Doi_(identifier)):[10.1212/wnl.57.8.1440](https://doi.org/10.1212%2Fwnl.57.8.1440). [PMID](/source/PMID_(identifier)) [11673586](https://pubmed.ncbi.nlm.nih.gov/11673586). [S2CID](/source/S2CID_(identifier)) [24920023](https://api.semanticscholar.org/CorpusID:24920023).

- Jaksch M, Paret C, Stucka R, Horn N, Müller-Höcker J, Horvath R, Trepesch N, Stecker G, Freisinger P, Thirion C, Müller J, Lunkwitz R, Rödel G, Shoubridge EA, Lochmüller H (December 2001). ["Cytochrome c oxidase deficiency due to mutations in SCO2, encoding a mitochondrial copper-binding protein, is rescued by copper in human myoblasts"](https://doi.org/10.1093%2Fhmg%2F10.26.3025). *Human Molecular Genetics*. **10** (26): 3025–35. [doi](/source/Doi_(identifier)):[10.1093/hmg/10.26.3025](https://doi.org/10.1093%2Fhmg%2F10.26.3025). [PMID](/source/PMID_(identifier)) [11751685](https://pubmed.ncbi.nlm.nih.gov/11751685).

- Salviati L, Hernandez-Rosa E, Walker WF, Sacconi S, DiMauro S, Schon EA, Davidson MM (April 2002). ["Copper supplementation restores cytochrome c oxidase activity in cultured cells from patients with SCO2 mutations"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1222481). *The Biochemical Journal*. **363** (Pt 2): 321–7. [doi](/source/Doi_(identifier)):[10.1042/0264-6021:3630321](https://doi.org/10.1042%2F0264-6021%3A3630321). [PMC](/source/PMC_(identifier)) [1222481](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1222481). [PMID](/source/PMID_(identifier)) [11931660](https://pubmed.ncbi.nlm.nih.gov/11931660).

- Collins JE, Goward ME, Cole CG, Smink LJ, Huckle EJ, Knowles S, Bye JM, Beare DM, Dunham I (January 2003). ["Reevaluating human gene annotation: a second-generation analysis of chromosome 22"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC430954). *Genome Research*. **13** (1): 27–36. [doi](/source/Doi_(identifier)):[10.1101/gr.695703](https://doi.org/10.1101%2Fgr.695703). [PMC](/source/PMC_(identifier)) [430954](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC430954). [PMID](/source/PMID_(identifier)) [12529303](https://pubmed.ncbi.nlm.nih.gov/12529303).

- Sacconi S, Salviati L, Sue CM, Shanske S, Davidson MM, Bonilla E, Naini AB, De Vivo DC, DiMauro S (February 2003). "Mutation screening in patients with isolated cytochrome c oxidase deficiency". *Pediatric Research*. **53** (2): 224–30. [doi](/source/Doi_(identifier)):[10.1203/01.PDR.0000048100.91730.6A](https://doi.org/10.1203%2F01.PDR.0000048100.91730.6A). [hdl](/source/Hdl_(identifier)):[11577/1368344](https://hdl.handle.net/11577%2F1368344). [PMID](/source/PMID_(identifier)) [12538779](https://pubmed.ncbi.nlm.nih.gov/12538779). [S2CID](/source/S2CID_(identifier)) [12496207](https://api.semanticscholar.org/CorpusID:12496207).

- Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW (June 2004). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". *Nature Biotechnology*. **22** (6): 707–16. [doi](/source/Doi_(identifier)):[10.1038/nbt971](https://doi.org/10.1038%2Fnbt971). [PMID](/source/PMID_(identifier)) [15146197](https://pubmed.ncbi.nlm.nih.gov/15146197). [S2CID](/source/S2CID_(identifier)) [27764390](https://api.semanticscholar.org/CorpusID:27764390).

- Leary SC, Kaufman BA, Pellecchia G, Guercin GH, Mattman A, Jaksch M, Shoubridge EA (September 2004). ["Human SCO1 and SCO2 have independent, cooperative functions in copper delivery to cytochrome c oxidase"](https://doi.org/10.1093%2Fhmg%2Fddh197). *Human Molecular Genetics*. **13** (17): 1839–48. [doi](/source/Doi_(identifier)):[10.1093/hmg/ddh197](https://doi.org/10.1093%2Fhmg%2Fddh197). [PMID](/source/PMID_(identifier)) [15229189](https://pubmed.ncbi.nlm.nih.gov/15229189).

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- Stiburek L, Vesela K, Hansikova H, Pecina P, Tesarova M, Cerna L, Houstek J, Zeman J (December 2005). ["Tissue-specific cytochrome c oxidase assembly defects due to mutations in SCO2 and SURF1"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1316303). *The Biochemical Journal*. **392** (Pt 3): 625–32. [doi](/source/Doi_(identifier)):[10.1042/BJ20050807](https://doi.org/10.1042%2FBJ20050807). [PMC](/source/PMC_(identifier)) [1316303](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1316303). [PMID](/source/PMID_(identifier)) [16083427](https://pubmed.ncbi.nlm.nih.gov/16083427).

- Matoba S, Kang JG, Patino WD, Wragg A, Boehm M, Gavrilova O, Hurley PJ, Bunz F, Hwang PM (June 2006). "p53 regulates mitochondrial respiration". *Science*. **312** (5780): 1650–3. [Bibcode](/source/Bibcode_(identifier)):[2006Sci...312.1650M](https://ui.adsabs.harvard.edu/abs/2006Sci...312.1650M). [doi](/source/Doi_(identifier)):[10.1126/science.1126863](https://doi.org/10.1126%2Fscience.1126863). [PMID](/source/PMID_(identifier)) [16728594](https://pubmed.ncbi.nlm.nih.gov/16728594). [S2CID](/source/S2CID_(identifier)) [36668814](https://api.semanticscholar.org/CorpusID:36668814).

- Leary SC, Cobine PA, Kaufman BA, Guercin GH, Mattman A, Palaty J, Lockitch G, Winge DR, Rustin P, Horvath R, Shoubridge EA (January 2007). ["The human cytochrome c oxidase assembly factors SCO1 and SCO2 have regulatory roles in the maintenance of cellular copper homeostasis"](https://doi.org/10.1016%2Fj.cmet.2006.12.001). *Cell Metabolism*. **5** (1): 9–20. [doi](/source/Doi_(identifier)):[10.1016/j.cmet.2006.12.001](https://doi.org/10.1016%2Fj.cmet.2006.12.001). [PMID](/source/PMID_(identifier)) [17189203](https://pubmed.ncbi.nlm.nih.gov/17189203).

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## External links

- [*SCO2*](https://genome.ucsc.edu/cgi-bin/hgTracks?db=hg38&singleSearch=knownCanonical&position=SCO2) human gene location in the [UCSC Genome Browser](/source/UCSC_Genome_Browser).

- [*SCO2*](https://genome.ucsc.edu/cgi-bin/hgGene?db=hg38&hgg_type=knownGene&hgg_gene=SCO2) human gene details in the [UCSC Genome Browser](/source/UCSC_Genome_Browser).

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Adapted from the Wikipedia article [SCO2](https://en.wikipedia.org/wiki/SCO2) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/SCO2?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.