P48170 · COX1_ONCMY
- ProteinCytochrome c oxidase subunit 1
- Genemt-co1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids516 (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
Protein has several cofactor binding sites:
Note: Binds 2 heme A groups non-covalently per subunit.
Note: Binds a copper B center.
Pathway
Energy metabolism; oxidative phosphorylation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 40 | Na+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 45 | Na+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 61 | Fe (UniProtKB | ChEBI) of Fe(II)-heme a (UniProtKB | ChEBI); low-spin; axial binding residue | ||||
Sequence: H | ||||||
Binding site | 240 | Cu cation B (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 244 | O2 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 290 | Cu cation B (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 291 | Cu cation B (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 368 | Mg2+ (UniProtKB | ChEBI); ligand shared with MT-CO2 | ||||
Sequence: H | ||||||
Binding site | 369 | Mg2+ (UniProtKB | ChEBI); ligand shared with MT-CO2 | ||||
Sequence: D | ||||||
Binding site | 376 | Fe (UniProtKB | ChEBI) of heme a3 (UniProtKB | ChEBI); high-spin; axial binding residue | ||||
Sequence: H | ||||||
Binding site | 378 | Fe (UniProtKB | ChEBI) of Fe(II)-heme a (UniProtKB | ChEBI); low-spin; axial binding residue | ||||
Sequence: H | ||||||
Binding site | 441 | Na+ (UniProtKB | ChEBI) | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial respiratory chain complex IV | |
Cellular Component | respiratory chain complex IV | |
Molecular Function | cytochrome-c oxidase activity | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Biological Process | electron transport coupled proton 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 1
- EC number
- Alternative names
Gene names
Encoded on
- Mitochondrion
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Protacanthopterygii > Salmoniformes > Salmonidae > Salmoninae > Oncorhynchus
Accessions
- Primary accessionP48170
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 | 1-11 | Mitochondrial matrix | ||||
Sequence: MAITRWFFSTN | ||||||
Transmembrane | 12-40 | Helical; Name=I | ||||
Sequence: HKDIGTLYLVFGAWAGMVGTALSLLIRAE | ||||||
Topological domain | 41-50 | Mitochondrial intermembrane | ||||
Sequence: LSQPGALLGD | ||||||
Transmembrane | 51-86 | Helical; Name=II | ||||
Sequence: DQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLM | ||||||
Topological domain | 87-94 | Mitochondrial matrix | ||||
Sequence: IGAPDMAF | ||||||
Transmembrane | 95-117 | Helical; Name=III | ||||
Sequence: PRMNNMSFWLLPPSFLLLLSSSG | ||||||
Topological domain | 118-140 | Mitochondrial intermembrane | ||||
Sequence: VEAGAGTGWTVYPPLAGNLAHAG | ||||||
Transmembrane | 141-170 | Helical; Name=IV | ||||
Sequence: ASVDLTIFSLHLAGISSILGAINFITTIIN | ||||||
Topological domain | 171-182 | Mitochondrial matrix | ||||
Sequence: MKPPAISQYQTP | ||||||
Transmembrane | 183-212 | Helical; Name=V | ||||
Sequence: LFVWAVLVTAVLLLLSLPVLAAGITMLLTD | ||||||
Topological domain | 213-227 | Mitochondrial intermembrane | ||||
Sequence: RNLNTTFFDPAGGGD | ||||||
Transmembrane | 228-261 | Helical; Name=VI | ||||
Sequence: PILYQHLFWFFSHPEVYILILPGFGMISHIVAYY | ||||||
Topological domain | 262-269 | Mitochondrial matrix | ||||
Sequence: SGKKEPFG | ||||||
Transmembrane | 270-286 | Helical; Name=VII | ||||
Sequence: YMGMVWAMMAIGLLGFI | ||||||
Topological domain | 287-298 | Mitochondrial intermembrane | ||||
Sequence: VWAHHMFTVGMD | ||||||
Transmembrane | 299-327 | Helical; Name=VIII | ||||
Sequence: VDTRAYFTSATMIIAIPTGVKVFSWLATL | ||||||
Topological domain | 328-335 | Mitochondrial matrix | ||||
Sequence: HGGSIKWE | ||||||
Transmembrane | 336-357 | Helical; Name=IX | ||||
Sequence: TPLLWALGFIFLFTVGGLTGIV | ||||||
Topological domain | 358-370 | Mitochondrial intermembrane | ||||
Sequence: LANSSLDIVLHDT | ||||||
Transmembrane | 371-400 | Helical; Name=X | ||||
Sequence: YYVVAHFHYVLSMGAVFAIMGAFVHWFPLF | ||||||
Topological domain | 401-406 | Mitochondrial matrix | ||||
Sequence: TGYTLH | ||||||
Transmembrane | 407-433 | Helical; Name=XI | ||||
Sequence: STWTKIHFGIMFIGVNLTFFPQHFLGL | ||||||
Topological domain | 434-446 | Mitochondrial intermembrane | ||||
Sequence: AGMPRRYSDYPDA | ||||||
Transmembrane | 447-478 | Helical; Name=XII | ||||
Sequence: YTLWNTVSSIGSLVSLVAVIMFLFILWEAFAA | ||||||
Topological domain | 479-516 | Mitochondrial matrix | ||||
Sequence: KREVASIELTSTNVEWLHGCPPPYHTFEEPAFVQVQAN |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000183370 | 1-516 | Cytochrome c oxidase subunit 1 | |||
Sequence: MAITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPPAISQYQTPLFVWAVLVTAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFSHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGAFVHWFPLFTGYTLHSTWTKIHFGIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLVSLVAVIMFLFILWEAFAAKREVASIELTSTNVEWLHGCPPPYHTFEEPAFVQVQAN | ||||||
Cross-link | 240↔244 | 1'-histidyl-3'-tyrosine (His-Tyr) | ||||
Sequence: HPEVY |
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).
As a newly synthesized protein, rapidly incorporates into a multi-subunit assembly intermediate in the inner membrane, called MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase) complex, whose core components are COA3/MITRAC12 and COX14. Within the MITRAC complex, interacts with COA3 and with SMIM20/MITRAC7; the interaction with SMIM20 stabilizes the newly synthesized MT-CO1 and prevents its premature turnover. Interacts with TMEM177 in a COX20-dependent manner (By similarity).
As a newly synthesized protein, rapidly incorporates into a multi-subunit assembly intermediate in the inner membrane, called MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase) complex, whose core components are COA3/MITRAC12 and COX14. Within the MITRAC complex, interacts with COA3 and with SMIM20/MITRAC7; the interaction with SMIM20 stabilizes the newly synthesized MT-CO1 and prevents its premature turnover. Interacts with TMEM177 in a COX20-dependent manner (By similarity).
Structure
Sequence
- Sequence statusComplete
- Length516
- Mass (Da)56,879
- Last updated1996-02-01 v1
- Checksum721051B0C09EBCA4
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L29771 EMBL· GenBank· DDBJ | AAB03349.1 EMBL· GenBank· DDBJ | Genomic DNA |