Q37545 · COX2_LUMTE

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 subunit 1
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 Componentrespirasome
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
      COII

Encoded on

  • Mitochondrion

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Spiralia > Lophotrochozoa > Annelida > Clitellata > Oligochaeta > Crassiclitellata > Lumbricina > Lumbricidae > Lumbricinae > Lumbricus

Accessions

  • Primary accession
    Q37545

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-26Mitochondrial intermembrane
Transmembrane27-47Helical
Topological domain48-60Mitochondrial matrix
Transmembrane61-81Helical
Topological domain82-228Mitochondrial intermembrane

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001836231-228Cytochrome 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).

Structure

Family & Domains

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    228
  • Mass (Da)
    25,659
  • Last updated
    1996-11-01 v1
  • Checksum
    A1CE3834F3BD80D3
MPNWGQVMFQDAASSVMLQLVSFHDHALLVLTLVLTVVGYALLALMLNKQVNRYIMEAQTVETIWTILPALILLVLALPSLRILYITDEVSQPSITVKTIGHQWYWSYEYTDFLNVEMDSYMLPTSDLLPGDYRLLEVDNRMVVPMQLEIRMLITAADVIHSWTVPALGVKVDAVPGRLNQIGFTTTQPGVFYGQCSEICGANHSFMPIAVEAINTKSFMSWVSNFKP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U24570
EMBL· GenBank· DDBJ
AAC46865.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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