P11948 · COX2_MACFA

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 site161Cu cation A1 (UniProtKB | ChEBI)
Binding site196Cu cation A1 (UniProtKB | ChEBI)
Binding site196Cu cation A2 (UniProtKB | ChEBI)
Binding site198Cu cation A2 (UniProtKB | ChEBI)
Binding site198Mg2+ (UniProtKB | ChEBI); ligand shared with MT-CO1
Binding site200Cu cation A1 (UniProtKB | ChEBI)
Binding site200Cu cation A2 (UniProtKB | ChEBI)
Binding site204Cu cation A2 (UniProtKB | ChEBI)
Binding site207Cu cation A1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrial inner membrane
Cellular Componentmitochondrion
Cellular Componentrespiratory chain complex IV
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
      MT-CO2
    • Synonyms
      COII, COX2, COXII, MTCO2

Encoded on

  • Mitochondrion

Organism names

Accessions

  • Primary accession
    P11948

Proteomes

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-14Mitochondrial intermembrane
Transmembrane15-45Helical; Name=I
Topological domain46-59Mitochondrial matrix
Transmembrane60-87Helical; Name=II
Topological domain88-227Mitochondrial intermembrane

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001836261-227Cytochrome c oxidase subunit 2

Interaction

Subunit

Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of 14 subunits. The complex is composed of a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in the mitochondrial DNA, and 11 supernumerary subunits COX4I, COX5A, COX5B, COX6A, COX6B, COX6C, COX7A, COX7B, COX7C, COX8 and NDUFA4, which are encoded in the nuclear genome. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), resulting in different assemblies (supercomplex SCI1III2IV1 and megacomplex MCI2III2IV2) (By similarity).
Found in a complex with TMEM177, COA6, COX18, COX20, SCO1 and SCO2. Interacts with TMEM177 in a COX20-dependent manner. Interacts with COX20. Interacts with COX16 (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    227
  • Mass (Da)
    25,488
  • Last updated
    1989-10-01 v1
  • Checksum
    922DDA858D32E4C4
MAHPVQLSLQDATSPIMEELITFHDHAFMAMSLISFLVLYALALTLTTKLTNTNITDAQEMETIWTILPAVILILIALPSLRVLYLTDEVNDPSLTIKSIGHQWYWTYEYTDYGGLIFNSYMLPPLFLKPGDLRLLEVDNRVVLPIEAPVRMMITSQDVLHSWTIPTLGLKTDAVPGRLNQTVFTATRPGVYYGQCSEICGANHSFMPIVADLIPLKIFEMGPVFTL

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict43-44in Ref. 2; AAA31890
Sequence conflict95in Ref. 2; AAA31890
Sequence conflict129in Ref. 2; AAA31890
Sequence conflict149in Ref. 2; AAA31890
Sequence conflict212in Ref. 2; AAA31890

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
J02825
EMBL· GenBank· DDBJ
AAA31889.1
EMBL· GenBank· DDBJ
mRNA
M58008
EMBL· GenBank· DDBJ
AAA31890.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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