P08574 · CY1_HUMAN
- ProteinCytochrome c1, heme protein, mitochondrial
- GeneCYC1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids325 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of 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. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. Cytochrome c1 is a catalytic core subunit containing a c-type heme. It transfers electrons from the [2Fe-2S] iron-sulfur cluster of the Rieske protein to cytochrome c.
Catalytic activity
- a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H+(out)
Cofactor
Note: Binds 1 heme c group covalently per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 121 | heme c (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 124 | heme c (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 125 | Fe (UniProtKB | ChEBI) of heme c (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 244 | Fe (UniProtKB | ChEBI) of heme c (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: M |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | mitochondrial inner membrane | |
Cellular Component | mitochondrial respiratory chain complex III | |
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Molecular Function | ubiquinol-cytochrome-c reductase activity | |
Biological Process | cellular respiration | |
Biological Process | mitochondrial electron transport, ubiquinol to cytochrome c | |
Biological Process | response to glucagon |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytochrome c1, heme protein, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP08574
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion inner membrane ; Single-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 85-281 | Mitochondrial intermembrane | ||||
Sequence: SDLELHPPSYPWSHRGLLSSLDHTSIRRGFQVYKQVCASCHSMDFVAYRHLVGVCYTEDEAKELAAEVEVQDGPNEDGEMFMRPGKLFDYFPKPYPNSEAARAANNGALPPDLSYIVRARHGGEDYVFSLLTGYCEPPTGVSLREGLYFNPYFPGQAIAMAPPIYTDVLEFDDGTPATMSQIAKDVCTFLRWASEPE | ||||||
Transmembrane | 282-315 | Helical | ||||
Sequence: HDHRKRMGLKMLMMMALLVPLVYTIKRHKWSVLK | ||||||
Topological domain | 316-325 | Mitochondrial matrix | ||||
Sequence: SRKLAYRPPK |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Mitochondrial complex III deficiency, nuclear type 6 (MC3DN6)
- Note
- DescriptionAn autosomal recessive disorder caused by mitochondrial dysfunction. It is characterized by onset in early childhood of episodic acute lactic acidosis, ketoacidosis, and insulin-responsive hyperglycemia, usually associated with infection. Laboratory studies show decreased activity of mitochondrial complex III. Psychomotor development is normal.
- See alsoMIM:615453
Natural variants in MC3DN6
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_070847 | 96 | W>C | in MC3DN6; dbSNP:rs587777041 | |
VAR_070848 | 215 | L>F | in MC3DN6; dbSNP:rs587777042 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_025163 | 76 | in dbSNP:rs7820984 | |||
Sequence: M → V | ||||||
Natural variant | VAR_013631 | 89 | ||||
Sequence: L → V | ||||||
Natural variant | VAR_070847 | 96 | in MC3DN6; dbSNP:rs587777041 | |||
Sequence: W → C | ||||||
Natural variant | VAR_070848 | 215 | in MC3DN6; dbSNP:rs587777042 | |||
Sequence: L → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 476 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Transit peptide | 1-84 | UniProt | Mitochondrion | ||||
Sequence: MAAAAASLRGVVLGPRGAGLPGARARGLLCSARPGQLPLRTPQAVALSSKSGLSRGRKVMLSALGMLAAGGAGLAMALHSAVSA | |||||||
Chain | PRO_0000006554 | 85-325 | UniProt | Cytochrome c1, heme protein, mitochondrial | |||
Sequence: SDLELHPPSYPWSHRGLLSSLDHTSIRRGFQVYKQVCASCHSMDFVAYRHLVGVCYTEDEAKELAAEVEVQDGPNEDGEMFMRPGKLFDYFPKPYPNSEAARAANNGALPPDLSYIVRARHGGEDYVFSLLTGYCEPPTGVSLREGLYFNPYFPGQAIAMAPPIYTDVLEFDDGTPATMSQIAKDVCTFLRWASEPEHDHRKRMGLKMLMMMALLVPLVYTIKRHKWSVLKSRKLAYRPPK | |||||||
Modified residue (large scale data) | 103 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 182 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 182 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 11 subunits. The complex is composed of 3 respiratory subunits cytochrome b, cytochrome c1 and Rieske protein UQCRFS1, 2 core protein subunits UQCRC1/QCR1 and UQCRC2/QCR2, and 6 low-molecular weight protein subunits UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and subunit 9, the cleavage product of Rieske protein UQCRFS1 (By similarity).
The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and cytochrome c oxidase (complex IV, CIV), resulting in different assemblies (supercomplex SCI1III2IV1 and megacomplex MCI2III2IV2) (PubMed:28844695).
Interacts with FLVCR2; this interaction occurs in the absence of heme and is disrupted upon heme binding
The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and cytochrome c oxidase (complex IV, CIV), resulting in different assemblies (supercomplex SCI1III2IV1 and megacomplex MCI2III2IV2) (PubMed:28844695).
Interacts with FLVCR2; this interaction occurs in the absence of heme and is disrupted upon heme binding
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P08574 | ANKHD1 Q8IWZ3-3 | 3 | EBI-1224514, EBI-25833200 | |
BINARY | P08574 | HTT P42858 | 7 | EBI-1224514, EBI-466029 | |
BINARY | P08574 | PDCD2 Q16342 | 3 | EBI-1224514, EBI-359462 | |
BINARY | P08574 | UQCRB P14927 | 3 | EBI-1224514, EBI-743128 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 108-209 | Cytochrome c | ||||
Sequence: TSIRRGFQVYKQVCASCHSMDFVAYRHLVGVCYTEDEAKELAAEVEVQDGPNEDGEMFMRPGKLFDYFPKPYPNSEAARAANNGALPPDLSYIVRARHGGED |
Sequence similarities
Belongs to the cytochrome c family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length325
- Mass (Da)35,422
- Last updated2010-11-02 v3
- ChecksumCC8EA2E60E96BBDC
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M16597 EMBL· GenBank· DDBJ | AAA35730.1 EMBL· GenBank· DDBJ | mRNA | ||
J04444 EMBL· GenBank· DDBJ | AAA52135.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CR541674 EMBL· GenBank· DDBJ | CAG46475.1 EMBL· GenBank· DDBJ | mRNA | ||
BT019798 EMBL· GenBank· DDBJ | AAV38601.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ300360 EMBL· GenBank· DDBJ | ABB96244.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC104592 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC001006 EMBL· GenBank· DDBJ | AAH01006.1 EMBL· GenBank· DDBJ | mRNA | ||
BC015616 EMBL· GenBank· DDBJ | AAH15616.1 EMBL· GenBank· DDBJ | mRNA | ||
BC020566 EMBL· GenBank· DDBJ | AAH20566.1 EMBL· GenBank· DDBJ | mRNA | ||
X06994 EMBL· GenBank· DDBJ | CAA30052.1 EMBL· GenBank· DDBJ | mRNA |