Search Results

Overview

Uniprot IDQ9DB77
Protein NameCytochrome b-c1 complex subunit 2, mitochondrial
Gene NameUqcrc2
OrganismMus musculus

Kla Sites from experimental identification

Position Flanking peptide
109 GIEAVGGKLSVTATR
162 RSQLKIDKAVAFQNS
199 CPDYRMGKITSEELH
250 GLGLAGAKAKYRGGE
375 SADVQAAKNKLKAGY
92 LASSLTTKGASSFKI

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 (PubMed:34616041, PubMed:38575788). 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 (PubMed:34616041, PubMed:38575788). 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 (PubMed:34616041, PubMed:38575788). 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 (By similarity). 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 (By similarity)

Protein Sequence

10 MKLLSRAGSF 20 SRFYSLKVAP 30 KVKTSAAPGG 40 VPLQPQDLEF 50 TKLPNGLVIA 60 SLENYAPLSR 70 IGLFVKAGSR 80 YEDSNNLGTS 90 HLLRLASSLT 100 TKGASSFKIT 110 RGIEAVGGKL 120 SVTATRENMA 130 YTVEGIRSDI 140 EILMEFLLNV 150 TTAPEFRRWE 160 VAALRSQLKI 170 DKAVAFQNSQ 180 TRIIENLHDV 190 AYKNALANPL 200 YCPDYRMGKI 210 TSEELHYFVQ 220 NHFTSARMAL 230 VGLGVSHSVL 240 KQVAEQFLNM 250 RGGLGLAGAK 260 AKYRGGEIRE 270 QNGDNLVHAA 280 IVAESAAIGN 290 AEANAFSVLQ 300 HLLGAGPHIK 310 RGNNTTSLLS 320 QSVAKGSHQP 330 FDVSAFNASY 340 SDSGLFGIYT 350 ISQAAAAGEV 360 INAAYNQVKA 370 VAQGNLSSAD 380 VQAAKNKLKA 390 GYLMSVETSE 400 GFLSEIGSQA 410 LAAGSYMPPS 420 TVLQQIDSVA 430 DADVVKAAKK 440 FVSGKKSMAA 450 SGNLGHTPFL DEL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005743 mitochondrial inner membrane
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0043209 myelin sheath
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0045275 respiratory chain complex III
Molecular Function GO:0046872 metal ion binding
Molecular Function GO:0004222 metalloendopeptidase activity
Molecular Function GO:0044877 protein-containing complex binding
Biological Process GO:0045333 cellular respiration
Biological Process GO:0006122 mitochondrial electron transport, ubiquinol to cytochrome c
Biological Process GO:0006508 proteolysis
Biological Process GO:0009410 response to xenobiotic stimulus

Reference

[1] Chang J, Wu W, Qian P, Lu Z, He X et al.. Multi-omics study on the effect of moderate-intensity exercise on protein lactylation in mouse muscle tissue.. Front Cell Dev Biol 12:1472338. 2024. PMID: 39935788.

[2] Zhuo W, Zhang M, Tan J, Gao Y, Wang Y et al.. Lysine lactylation analysis of proteins in the heart of the Kawasaki disease mouse model.. Front Cell Dev Biol 13:1550220. 2025. PMID: 40114965.

[3] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.