P24894 · COX2_CAEEL
- ProteinCytochrome c oxidase subunit 2
- Genectc-2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids231 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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 | 164 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 199 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 199 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 201 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 201 | Mg2+ (UniProtKB | ChEBI); ligand shared with subunit 1 | ||||
Sequence: E | ||||||
Binding site | 203 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 203 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 207 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 210 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: M |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial inner membrane | |
Cellular Component | respirasome | |
Molecular Function | copper ion binding | |
Molecular Function | cytochrome-c oxidase activity | |
Biological Process | ATP synthesis coupled electron transport | |
Biological Process | mitochondrial electron transport, cytochrome c to oxygen |
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
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionP24894
Proteomes
Organism-specific databases
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 | 1-30 | Mitochondrial intermembrane | ||||
Sequence: MNNFFQGYNLLFQHSLFASYMDWFHSFNCS | ||||||
Transmembrane | 31-52 | Helical | ||||
Sequence: LLLGVLVFVTLLFGYLIFGTFY | ||||||
Topological domain | 53-69 | Mitochondrial matrix | ||||
Sequence: FKSKKIEYQFGELLCSI | ||||||
Transmembrane | 70-89 | Helical | ||||
Sequence: FPTIILLMQMVPSLSLLYYY | ||||||
Topological domain | 90-231 | Mitochondrial intermembrane | ||||
Sequence: GLMNLDSNLTVKVTGHQWYWSYEYSDIPGLEFDSYMKSLDQLSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDAMSGILSTFSYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSWCFGTME |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 132 | in strain: PB303 | ||||
Sequence: S → N | ||||||
Natural variant | 143 | in strain: CB4857 | ||||
Sequence: N → I | ||||||
Natural variant | 186 | in strain: AB2, CB4852, CB4853, CB4855, CB4858 and PB306 | ||||
Sequence: S → N | ||||||
Natural variant | 216 | in strain: AB1 and KR314 | ||||
Sequence: V → M |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 4 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_0000183526 | 1-231 | Cytochrome c oxidase subunit 2 | |||
Sequence: MNNFFQGYNLLFQHSLFASYMDWFHSFNCSLLLGVLVFVTLLFGYLIFGTFYFKSKKIEYQFGELLCSIFPTIILLMQMVPSLSLLYYYGLMNLDSNLTVKVTGHQWYWSYEYSDIPGLEFDSYMKSLDQLSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDAMSGILSTFSYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSWCFGTME |
Proteomic databases
Expression
Gene expression databases
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
- Length231
- Mass (Da)26,549
- Last updated1995-11-01 v2
- ChecksumFCD8D458D1B0DDAA
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY171193 EMBL· GenBank· DDBJ | AAO16253.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY171194 EMBL· GenBank· DDBJ | AAO16257.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY171195 EMBL· GenBank· DDBJ | AAO16261.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY171196 EMBL· GenBank· DDBJ | AAO16265.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY171197 EMBL· GenBank· DDBJ | AAO16269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY171198 EMBL· GenBank· DDBJ | AAO16273.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY171199 EMBL· GenBank· DDBJ | AAO16277.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY171200 EMBL· GenBank· DDBJ | AAO16281.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY171201 EMBL· GenBank· DDBJ | AAO16285.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY171202 EMBL· GenBank· DDBJ | AAO16289.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY171203 EMBL· GenBank· DDBJ | AAO16293.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY171204 EMBL· GenBank· DDBJ | AAO16297.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY171205 EMBL· GenBank· DDBJ | AAO16301.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY171206 EMBL· GenBank· DDBJ | AAO16305.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY171207 EMBL· GenBank· DDBJ | AAO16309.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X54252 EMBL· GenBank· DDBJ | CAA38160.1 EMBL· GenBank· DDBJ | Genomic DNA |