| 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. The 2 core subunits UQCRC1/QCR1 and UQCRC2/QCR2 are homologous to the 2 mitochondrial-processing peptidase (MPP) subunits beta-MPP and alpha-MPP respectively, and they seem to have preserved their MPP processing properties. May be involved in the in situ processing of UQCRFS1 into the mature Rieske protein and its mitochondrial targeting sequence (MTS)/subunit 9 when incorporated into complex III (Probable). |
| Protein Name | Cytochrome B-C1 Complex Subunit 2 - MitochondrialComplex Iii Subunit 2Core Protein IiUbiquinol-Cytochrome-C Reductase Complex Core Protein 2 |
| Database Links | Reactome: R-HSA-611105Reactome: R-HSA-9837999Reactome: R-HSA-9865881 |
| Cellular Localisation | Mitochondrion Inner MembranePeripheral Membrane ProteinMatrix Side |
| Alternative Protein Names | Cytochrome B-C1 Complex Subunit 2 - Mitochondrial proteinComplex Iii Subunit 2 proteinCore Protein Ii proteinUbiquinol-Cytochrome-C Reductase Complex Core Protein 2 proteinUQCRC2 protein |
Information sourced from Uniprot.org
