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COX7C

Chr 5q14.3

cytochrome c oxidase subunit 7C

MANE:
ENST00000247655.4

Annotations refreshed 9 hours ago.

Predicted protein structure

Clinical relevance (Genomics England PanelApp)

Moderate Evidence (Amber)

  • Mitochondrial disorder with complex IV deficiency

    Unknown
  • Possible mitochondrial disorder - nuclear genes

    Unknown
  • Likely inborn error of metabolism

    Unknown
  • Mitochondrial disorders

Disease associations (Open Targets)

  • neurodegenerative disease

    0.56
  • Alzheimer disease

    0.42
  • Parkinson disease

    0.37
  • multiple sclerosis

    0.37
  • lysosomal storage disease

    0.37
  • autoimmune disorder of central nervous system

    0.37
  • Vertigo

    0.29
  • smoking initiation

    0.27
  • gestational diabetes

    0.25
  • anemia (phenotype)

    0.25

Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.

Protein function (UniProt)

Cytochrome c oxidase subunit 7C, mitochondrial

Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix

Data sources: HGNC (CC BY 4.0), AlphaFold (CC BY 4.0, Jumper et al. Nature 2021), Genomics England PanelApp (CC BY 4.0), ClinGen, Open Targets (CC0), UniProt.

Not for sole clinical decision-making. Always verify against primary sources.