COX7C

Protein-coding gene in the species Homo sapiens
COX7C
Identifiers
AliasesCOX7C, cytochrome c oxidase subunit 7C
External IDsOMIM: 603774; MGI: 103226; HomoloGene: 135674; GeneCards: COX7C; OMA:COX7C - orthologs
Gene location (Human)
Chromosome 5 (human)
Chr.Chromosome 5 (human)[1]
Chromosome 5 (human)
Genomic location for COX7C
Genomic location for COX7C
Band5q14.3Start86,617,928 bp[1]
End86,620,962 bp[1]
Gene location (Mouse)
Chromosome 13 (mouse)
Chr.Chromosome 13 (mouse)[2]
Chromosome 13 (mouse)
Genomic location for COX7C
Genomic location for COX7C
Band13|13 C3Start86,192,935 bp[2]
End86,195,023 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right ventricle

  • right auricle

  • left ventricle

  • apex of heart

  • muscle of thigh

  • human kidney

  • prefrontal cortex

  • ganglionic eminence

  • biceps brachii

  • mucosa of transverse colon
Top expressed in
  • quadriceps femoris muscle

  • right kidney

  • yolk sac

  • heart

  • proximal tubule

  • stomach

  • muscle tissue

  • neural tube

  • skeletal muscle tissue

  • jejunum
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • cytochrome-c oxidase activity
Cellular component
  • integral component of membrane
  • mitochondrial inner membrane
  • membrane
  • mitochondrion
  • mitochondrial respiratory chain complex IV
Biological process
  • proton transmembrane transport
  • generation of precursor metabolites and energy
  • mitochondrial electron transport, cytochrome c to oxygen
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

1350

12867

Ensembl

ENSG00000127184

ENSMUSG00000017778

UniProt

P15954

P17665

RefSeq (mRNA)

NM_001867

NM_007749

RefSeq (protein)

NP_001858

NP_031775

Location (UCSC)Chr 5: 86.62 – 86.62 MbChr 13: 86.19 – 86.2 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Cytochrome c oxidase subunit 7C, mitochondrial is an enzyme that in humans is encoded by the COX7C gene.[5][6]

Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. This component is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded subunits may function in the regulation and assembly of the complex. This nuclear gene encodes subunit VIIc, which shares 87% and 85% amino acid sequence identity with mouse and bovine COX VIIc, respectively, and is found in all tissues. A pseudogene COX7CP1 has been found on chromosome 13.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000127184 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000017778 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Hofmann S, Lichtner P, Schuffenhauer S, Gerbitz KD, Meitinger T (Mar 1999). "Assignment of the human genes coding for cytochrome c oxidase subunits Va (COX5A), VIc (COX6C) and VIIc (COX7C) to chromosome bands 15q25, 8q22→q23 and 5q14 and of three pseudogenes (COX5AP1, COX6CP1, COX7CP1) to 14q22, 16p12 and 13q14→q21 by FISH and radiation hybrid mapping". Cytogenet Cell Genet. 83 (3–4): 226–7. doi:10.1159/000015185. PMID 10072584.
  6. ^ a b "Entrez Gene: COX7C cytochrome c oxidase subunit VIIc".

Further reading

  • Lenka N, Vijayasarathy C, Mullick J, Avadhani NG (1998). "Structural organization and transcription regulation of nuclear genes encoding the mammalian cytochrome c oxidase complex". Prog. Nucleic Acid Res. Mol. Biol. Progress in Nucleic Acid Research and Molecular Biology. 61: 309–44. doi:10.1016/S0079-6603(08)60830-2. ISBN 9780125400619. PMID 9752724.
  • Sirchia R, Luparello C (2007). "Mid-region parathyroid hormone-related protein (PTHrP) and gene expression of MDA-MB231 breast cancer cells". Biol. Chem. 388 (5): 457–65. doi:10.1515/BC.2007.059. PMID 17516841. S2CID 2286919.
  • 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.
  • 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.
  • Kaminishi H, Hamatake H, Cho T, et al. (1994). "Activation of blood clotting factors by microbial proteinases". FEMS Microbiol. Lett. 121 (3): 327–32. doi:10.1111/j.1574-6968.1994.tb07121.x. PMID 7926688.
  • Koga Y, Fabrizi GM, Mita S, et al. (1990). "Sequence of a cDNA specifying subunit VIIc of human cytochrome c oxidase". Nucleic Acids Res. 18 (3): 684. doi:10.1093/nar/18.3.684. PMC 333506. PMID 2155413.
  • Van Kuilenburg AB, Van Beeumen JJ, Van der Meer NM, Muijsers AO (1992). "Subunits VIIa,b,c of human cytochrome c oxidase. Identification of both 'heart-type' and 'liver-type' isoforms of subunit VIIa in human heart". Eur. J. Biochem. 203 (1–2): 193–9. doi:10.1111/j.1432-1033.1992.tb19847.x. PMID 1309697.


  • v
  • t
  • e