QCR1_RAT
ID QCR1_RAT Reviewed; 480 AA.
AC Q68FY0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cytochrome b-c1 complex subunit 1, mitochondrial;
DE AltName: Full=Complex III subunit 1;
DE AltName: Full=Core protein I;
DE AltName: Full=Ubiquinol-cytochrome-c reductase complex core protein 1;
DE Flags: Precursor;
GN Name=Uqcrc1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PROTEIN SEQUENCE OF 86-99; 112-126 AND 397-415, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND THR-214, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC multisubunit transmembrane complex that is part of the mitochondrial
CC electron transport chain which drives oxidative phosphorylation. The
CC respiratory chain contains 3 multisubunit complexes succinate
CC dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase
CC (complex IV, CIV), that cooperate to transfer electrons derived from
CC NADH and succinate to molecular oxygen, creating an electrochemical
CC gradient over the inner membrane that drives transmembrane transport
CC and the ATP synthase. The cytochrome b-c1 complex catalyzes electron
CC transfer from ubiquinol to cytochrome c, linking this redox reaction to
CC translocation of protons across the mitochondrial inner membrane, with
CC protons being carried across the membrane as hydrogens on the quinol.
CC In the process called Q cycle, 2 protons are consumed from the matrix,
CC 4 protons are released into the intermembrane space and 2 electrons are
CC passed to cytochrome c (By similarity). The 2 core subunits UQCRC1/QCR1
CC and UQCRC2/QCR2 are homologous to the 2 mitochondrial-processing
CC peptidase (MPP) subunits beta-MPP and alpha-MPP respectively, and they
CC seem to have preserved their MPP processing properties. May be involved
CC in the in situ processing of UQCRFS1 into the mature Rieske protein and
CC its mitochondrial targeting sequence (MTS)/subunit 9 when incorporated
CC into complex III (By similarity). Seems to play an important role in
CC the maintenance of proper mitochondrial function in nigral dopaminergic
CC neurons (By similarity). {ECO:0000250|UniProtKB:P07256,
CC ECO:0000250|UniProtKB:P31800, ECO:0000250|UniProtKB:P31930}.
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 11 subunits. The complex is composed of 3 respiratory
CC subunits cytochrome b, cytochrome c1 and Rieske protein UQCRFS1, 2 core
CC protein subunits UQCRC1/QCR1 and UQCRC2/QCR2, and 6 low-molecular
CC weight protein subunits UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8,
CC UQCR10/QCR9, UQCR11/QCR10 and subunit 9, the cleavage product of Rieske
CC protein UQCRFS1 (By similarity). The complex exists as an obligatory
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC cytochrome c oxidase (complex IV, CIV), resulting in different
CC assemblies (supercomplex SCI(1)III(2)IV(1) and megacomplex
CC MCI(2)III(2)IV(2)) (By similarity). Interacts with BRAWNIN (By
CC similarity). Interacts with STMP1 (By similarity).
CC {ECO:0000250|UniProtKB:P31800, ECO:0000250|UniProtKB:P31930,
CC ECO:0000250|UniProtKB:Q9CZ13}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P07256}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P07256}; Matrix side
CC {ECO:0000250|UniProtKB:P07256}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC1/QCR1 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC078923; AAH78923.1; -; mRNA.
DR RefSeq; NP_001004250.1; NM_001004250.2.
DR AlphaFoldDB; Q68FY0; -.
DR SMR; Q68FY0; -.
DR BioGRID; 256797; 2.
DR CORUM; Q68FY0; -.
DR IntAct; Q68FY0; 2.
DR MINT; Q68FY0; -.
DR STRING; 10116.ENSRNOP00000044696; -.
DR MEROPS; M16.975; -.
DR CarbonylDB; Q68FY0; -.
DR iPTMnet; Q68FY0; -.
DR PhosphoSitePlus; Q68FY0; -.
DR World-2DPAGE; 0004:Q68FY0; -.
DR jPOST; Q68FY0; -.
DR PaxDb; Q68FY0; -.
DR PRIDE; Q68FY0; -.
DR Ensembl; ENSRNOT00000042114; ENSRNOP00000044696; ENSRNOG00000032134.
DR GeneID; 301011; -.
DR KEGG; rno:301011; -.
DR UCSC; RGD:1303314; rat.
DR CTD; 7384; -.
DR RGD; 1303314; Uqcrc1.
DR eggNOG; KOG0960; Eukaryota.
DR GeneTree; ENSGT00940000158931; -.
DR HOGENOM; CLU_009902_4_0_1; -.
DR InParanoid; Q68FY0; -.
DR OMA; WSNPDNV; -.
DR OrthoDB; 638125at2759; -.
DR PhylomeDB; Q68FY0; -.
DR TreeFam; TF105032; -.
DR Reactome; R-RNO-611105; Respiratory electron transport.
DR PRO; PR:Q68FY0; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000032134; Expressed in heart and 19 other tissues.
DR Genevisible; Q68FY0; RN.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0043279; P:response to alkaloid; IEP:RGD.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Electron transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Respiratory chain; Transit peptide; Transport.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 35..480
FT /note="Cytochrome b-c1 complex subunit 1, mitochondrial"
FT /id="PRO_0000271398"
FT MOD_RES 111
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31930"
FT MOD_RES 138
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZ13"
FT MOD_RES 163
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZ13"
FT MOD_RES 163
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZ13"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 480 AA; 52849 MW; 140B7E886BD4D8C0 CRC64;
MAASAVCRAA CSGTQALLRT CRSPALLRLP ALRGTATFVQ ALQSVPETQV SVLDNGLRVA
SEQSSHPTCT VGVWIDVGSR YETEKNNGAG YFLEHLAFKG TKNRPGNALE KEVESIGAHL
NAYSTREHTA YLIKALSKDL PKVVELLADI VQNISLEDSQ IEKERDVILR EMQENDASMQ
NVVFDYLHAT AFQGTPLAQA VEGPSENVRR LSRTDLTDYL SRHYKAPRMV LAAAGGVKHQ
QLLDLAQDHF SSVSQVYEED AVPSITPCRF TGSEIRHRDD ALPLAHVAIA VEGPGWANPD
NVALQVANAI IGHYDCTYGG GVHLSSPLAS VAVANKLCQS FQTFNISYSE TGLLGAHFVC
DAMSIDDMIF FLQGQWMRLC TSATESEVTR GKNILRNALI SHLDGTTPVC EDIGRSLLTY
GRRIPLAEWE SRIEEVDAQM VREVCSKYFY DQCPAVAGYG PIEQLSDYNR IRSGMFWLRF
