P11948 · COX2_MACFA
- ProteinCytochrome c oxidase subunit 2
- GeneMT-CO2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids227 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
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
- 4 Fe(II)-[cytochrome c] + 8 H+(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H+(out) + 2 H2OThis reaction proceeds in the forward direction.
4 RHEA-COMP:10350 + 8 H+ (in)CHEBI:15378+ CHEBI:15379 = 4 RHEA-COMP:14399 + 4 H+ (out)CHEBI:15378+ 2 CHEBI:15377
Cofactor
Note: Binds a dinuclear copper A center per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 161 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 196 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 196 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 198 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 198 | Mg2+ (UniProtKB | ChEBI); ligand shared with MT-CO1 | ||||
Sequence: E | ||||||
Binding site | 200 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 200 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 204 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 207 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: M |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial inner membrane | |
Cellular Component | mitochondrion | |
Cellular Component | respiratory chain complex IV | |
Molecular Function | copper ion binding | |
Molecular Function | cytochrome-c oxidase activity | |
Biological Process | ATP synthesis coupled electron transport |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytochrome c oxidase subunit 2
- EC number
- Alternative names
Gene names
Encoded on
- Mitochondrion
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Cercopithecidae > Cercopithecinae > Macaca
Accessions
- Primary accessionP11948
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion inner membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-14 | Mitochondrial intermembrane | ||||
Sequence: MAHPVQLSLQDATS | ||||||
Transmembrane | 15-45 | Helical; Name=I | ||||
Sequence: PIMEELITFHDHAFMAMSLISFLVLYALALT | ||||||
Topological domain | 46-59 | Mitochondrial matrix | ||||
Sequence: LTTKLTNTNITDAQ | ||||||
Transmembrane | 60-87 | Helical; Name=II | ||||
Sequence: EMETIWTILPAVILILIALPSLRVLYLT | ||||||
Topological domain | 88-227 | Mitochondrial intermembrane | ||||
Sequence: DEVNDPSLTIKSIGHQWYWTYEYTDYGGLIFNSYMLPPLFLKPGDLRLLEVDNRVVLPIEAPVRMMITSQDVLHSWTIPTLGLKTDAVPGRLNQTVFTATRPGVYYGQCSEICGANHSFMPIVADLIPLKIFEMGPVFTL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000183626 | 1-227 | Cytochrome c oxidase subunit 2 | |||
Sequence: MAHPVQLSLQDATSPIMEELITFHDHAFMAMSLISFLVLYALALTLTTKLTNTNITDAQEMETIWTILPAVILILIALPSLRVLYLTDEVNDPSLTIKSIGHQWYWTYEYTDYGGLIFNSYMLPPLFLKPGDLRLLEVDNRVVLPIEAPVRMMITSQDVLHSWTIPTLGLKTDAVPGRLNQTVFTATRPGVYYGQCSEICGANHSFMPIVADLIPLKIFEMGPVFTL |
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).
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
Sequence
- Sequence statusComplete
- Length227
- Mass (Da)25,488
- Last updated1989-10-01 v1
- Checksum922DDA858D32E4C4
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 43-44 | in Ref. 2; AAA31890 | ||||
Sequence: AL → LS | ||||||
Sequence conflict | 95 | in Ref. 2; AAA31890 | ||||
Sequence: L → F | ||||||
Sequence conflict | 129 | in Ref. 2; AAA31890 | ||||
Sequence: K → N | ||||||
Sequence conflict | 149 | in Ref. 2; AAA31890 | ||||
Sequence: P → S | ||||||
Sequence conflict | 212 | in Ref. 2; AAA31890 | ||||
Sequence: D → E |
Keywords
- Technical term