F2QH72 · F2QH72_9NEOP

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 copper A center.

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

Names & Taxonomy

Protein names

  • Recommended name
    Cytochrome c oxidase subunit 2

Gene names

    • Name
      COII

Encoded on

  • Mitochondrion

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Polyneoptera > Grylloblattodea > Grylloblattidae > Galloisiana

Accessions

  • Primary accession
    F2QH72

Subcellular Location

Membrane
; Multi-pass membrane protein
Mitochondrion inner membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane27-51Helical
Transmembrane63-85Helical

Keywords

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).

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-91Cytochrome oxidase subunit II transmembrane region profile
Domain92-225Cytochrome oxidase subunit II copper A binding

Sequence similarities

Belongs to the cytochrome c oxidase subunit 2 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    230
  • Mass (Da)
    26,057
  • Last updated
    2011-05-31 v1
  • Checksum
    A735138684252EDD
MATWANLSLQDSSSPMMEQLIFFHDHALLILTIIVALVTYLMGSLFFNSYINRNLLESQTIEMIWTITPAVILFFIAIPSLRLLYLMDEINNPAITLKTIGHQWYWSYEYSDFSNIEFDSYMIPTTEMELKGFRLLDVDNRITLPINTHIRVIVTAADVLHSWTIPSLGVKVDATPGRLNQMGMLINRPGVYYGQCSEICGANHSFMPIVAEGVTTNTFTSWISSLSEAS

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue230

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FR728657
EMBL· GenBank· DDBJ
CBY17532.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp