A9RAG1 · COX2_DEBHA
- ProteinCytochrome c oxidase subunit 2
- GeneCOX2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids246 (go to sequence)
- Protein existenceInferred from homology
- 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] + O2 + 8 H+(in) = 4 Fe(III)-[cytochrome c] + 2 H2O + 4 H+(out)This reaction proceeds in the forward direction.
4 RHEA-COMP:10350 + CHEBI:15379 + 8 H+ (in)CHEBI:15378= 4 RHEA-COMP:14399 + 2 CHEBI:15377 + 4 H+ (out)CHEBI:15378
Cofactor
Note: Binds a dinuclear copper A center per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 175 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 210 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 210 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 212 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 212 | Mg2+ (UniProtKB | ChEBI); ligand shared with subunit 1 | ||||
Sequence: E | ||||||
Binding site | 214 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 214 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 218 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 221 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: M |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial inner membrane | |
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
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Debaryomycetaceae > Debaryomyces
Accessions
- Primary accessionA9RAG1
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion inner membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 31-51 | Helical | ||||
Sequence: HMMYYLALMLGLVSYMLYVMM | ||||||
Transmembrane | 72-92 | Helical | ||||
Sequence: IMWTMFPAVMLLLMAFPSFML |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 39 | in strain: CBS 789 and CLIB 381 | ||||
Sequence: M → V | ||||||
Natural variant | 46 | in strain: CLIB 660 | ||||
Sequence: M → L | ||||||
Natural variant | 51 | in strain: CBS 789 and CLIB 381 | ||||
Sequence: M → I | ||||||
Natural variant | 106 | in strain: CBS 789 and CLIB 381 | ||||
Sequence: V → I | ||||||
Natural variant | 179 | in strain: CBS 789 and CLIB 381 | ||||
Sequence: M → I |
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.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000355032 | 1-246 | Cytochrome c oxidase subunit 2 | |||
Sequence: MIWTDVPTPWGMRFQDAATPNAEGMHELYDHMMYYLALMLGLVSYMLYVMMKDYKNNTFAYKYIKHGQTLEIMWTMFPAVMLLLMAFPSFMLLYLCDEVLTPAMTVKVVGLQWYWKYEYSDFVSETGETVEYESYVMPEDMLEEGQLRLLDTDTSMVVPVDTHVRFMVTANDVLHCFTMPSLGIKVDACPGRLNQVSALMQRTGVYYGQCSELCGVNHGLMPIKTECVPIGDFVEWLGEQENVYVA |
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
Sequence
- Sequence statusComplete
- Length246
- Mass (Da)28,359
- Last updated2008-02-05 v1
- Checksum8F8982C0B23935B4
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 223 | in Ref. 2; ABU80664/ABU80663 and 3; CAQ51421/CAQ51422/CAQ51423/CAQ51424/CAQ51428/CAQ51429 | ||||
Sequence: I → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |