QCR1_MESAU
ID QCR1_MESAU Reviewed; 114 AA.
AC P86201;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Cytochrome b-c1 complex subunit 1, mitochondrial {ECO:0000250|UniProtKB:P31930};
DE AltName: Full=Complex III subunit 1 {ECO:0000250|UniProtKB:P31930};
DE AltName: Full=Core protein I {ECO:0000250|UniProtKB:P31930};
DE AltName: Full=Ubiquinol-cytochrome-c reductase complex core protein 1 {ECO:0000250|UniProtKB:P31930};
DE Flags: Fragments;
GN Name=UQCRC1 {ECO:0000250|UniProtKB:P31930};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
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:0000255}.
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DR AlphaFoldDB; P86201; -.
DR SMR; P86201; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR Pfam; PF00675; Peptidase_M16; 1.
DR SUPFAM; SSF63411; SSF63411; 1.
PE 1: Evidence at protein level;
KW Acetylation; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transport.
FT CHAIN <1..114
FT /note="Cytochrome b-c1 complex subunit 1, mitochondrial"
FT /id="PRO_0000394400"
FT MOD_RES 31
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31930"
FT NON_CONS 31..32
FT /evidence="ECO:0000305"
FT NON_CONS 52..53
FT /evidence="ECO:0000305"
FT NON_CONS 71..72
FT /evidence="ECO:0000305"
FT NON_CONS 81..82
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 114 AA; 12970 MW; 09B98A0E560A4D48 CRC64;
YETEKNNGAG YFLEHLAFKG TKNRPGNALE KHLSSVSRVY EEDAVPGLTP CRNALVSHLD
GTTPVCEDIG RRIPLAEWES RYFYDQCPAV AGYGPIEQLP DYNRIRSGMF WLRF
