A9RAG1 · COX2_DEBHA

Function

function

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.

Catalytic activity

Cofactor

Cu cation (UniProtKB | Rhea| CHEBI:23378 )

Note: Binds a dinuclear copper A center per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site175Cu cation A1 (UniProtKB | ChEBI)
Binding site210Cu cation A1 (UniProtKB | ChEBI)
Binding site210Cu cation A2 (UniProtKB | ChEBI)
Binding site212Cu cation A2 (UniProtKB | ChEBI)
Binding site212Mg2+ (UniProtKB | ChEBI); ligand shared with subunit 1
Binding site214Cu cation A1 (UniProtKB | ChEBI)
Binding site214Cu cation A2 (UniProtKB | ChEBI)
Binding site218Cu cation A2 (UniProtKB | ChEBI)
Binding site221Cu cation A1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrial inner membrane
Molecular Functioncopper ion binding
Molecular Functioncytochrome-c oxidase activity
Biological ProcessATP synthesis coupled electron transport

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cytochrome c oxidase subunit 2
  • EC number
  • Alternative names
    • Cytochrome c oxidase polypeptide II

Gene names

    • Name
      COX2

Encoded on

  • Mitochondrion

Organism names

Accessions

  • Primary accession
    A9RAG1
  • Secondary accessions
    • B0LCE8
    • B0LCE9
    • B4F4K1
    • B4F4K2
    • B4F4K4

Proteomes

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane31-51Helical
Transmembrane72-92Helical

Keywords

Phenotypes & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant39in strain: CBS 789 and CLIB 381
Natural variant46in strain: CLIB 660
Natural variant51in strain: CBS 789 and CLIB 381
Natural variant106in strain: CBS 789 and CLIB 381
Natural variant179in strain: CBS 789 and CLIB 381

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 5 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003550321-246Cytochrome c oxidase subunit 2

Interaction

Subunit

Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of a catalytic core of 3 subunits and several supernumerary subunits. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII).

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    246
  • Mass (Da)
    28,359
  • Last updated
    2008-02-05 v1
  • Checksum
    8F8982C0B23935B4
MIWTDVPTPWGMRFQDAATPNAEGMHELYDHMMYYLALMLGLVSYMLYVMMKDYKNNTFAYKYIKHGQTLEIMWTMFPAVMLLLMAFPSFMLLYLCDEVLTPAMTVKVVGLQWYWKYEYSDFVSETGETVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRFMVTANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWLGEQENVYVA

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict223in Ref. 2; ABU80664/ABU80663 and 3; CAQ51421/CAQ51422/CAQ51423/CAQ51424/CAQ51428/CAQ51429

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ508940
EMBL· GenBank· DDBJ
ABF58062.1
EMBL· GenBank· DDBJ
Genomic DNA
EF599377
EMBL· GenBank· DDBJ
ABU80663.1
EMBL· GenBank· DDBJ
Genomic DNA
EF599378
EMBL· GenBank· DDBJ
ABU80664.1
EMBL· GenBank· DDBJ
Genomic DNA
AM991984
EMBL· GenBank· DDBJ
CAQ51421.1
EMBL· GenBank· DDBJ
Genomic DNA
AM991986
EMBL· GenBank· DDBJ
CAQ51423.1
EMBL· GenBank· DDBJ
Genomic DNA
AM991987
EMBL· GenBank· DDBJ
CAQ51424.1
EMBL· GenBank· DDBJ
Genomic DNA
AM991985
EMBL· GenBank· DDBJ
CAQ51422.1
EMBL· GenBank· DDBJ
Genomic DNA
AM991991
EMBL· GenBank· DDBJ
CAQ51428.1
EMBL· GenBank· DDBJ
Genomic DNA
AM991992
EMBL· GenBank· DDBJ
CAQ51429.1
EMBL· GenBank· DDBJ
Genomic DNA
D55727
EMBL· GenBank· DDBJ
BAA09541.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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