QCR1_BOVIN
ID QCR1_BOVIN Reviewed; 480 AA.
AC P31800;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 167.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=1712295; DOI=10.1111/j.1432-1033.1991.tb16099.x;
RA Gencic S., Schaegger H., von Jagow G.;
RT "Core I protein of bovine ubiquinol-cytochrome-c reductase; an additional
RT member of the mitochondrial-protein-processing family. Cloning of bovine
RT core I and core II cDNAs and primary structure of the proteins.";
RL Eur. J. Biochem. 199:123-131(1991).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RX PubMed=8592474; DOI=10.1016/0076-6879(95)60132-5;
RA Schaegger H., Brandt U., Gencic S., von Jagow G.;
RT "Ubiquinol-cytochrome-c reductase from human and bovine mitochondria.";
RL Methods Enzymol. 260:82-96(1995).
RN [3]
RP PROTEIN SEQUENCE OF 35-52.
RX PubMed=2848575; DOI=10.1021/bi00418a053;
RA Gonzalez-Halphen D., Lindorfer M.A., Capaldi R.M.;
RT "Subunit arrangement in beef heart complex III.";
RL Biochemistry 27:7021-7031(1988).
RN [4]
RP FUNCTION.
RX PubMed=9694818; DOI=10.1074/jbc.273.33.20752;
RA Deng K., Zhang L., Kachurin A.M., Yu L., Xia D., Kim H., Deisenhofer J.,
RA Yu C.A.;
RT "Activation of a matrix processing peptidase from the crystalline
RT cytochrome bc1 complex of bovine heart mitochondria.";
RL J. Biol. Chem. 273:20752-20757(1998).
RN [5]
RP FUNCTION.
RX PubMed=11073949; DOI=10.1074/jbc.m007128200;
RA Deng K., Shenoy S.K., Tso S.C., Yu L., Yu C.A.;
RT "Reconstitution of mitochondrial processing peptidase from the core
RT proteins (subunits I and II) of bovine heart mitochondrial cytochrome bc(1)
RT complex.";
RL J. Biol. Chem. 276:6499-6505(2001).
RN [6]
RP FUNCTION.
RX PubMed=29243944; DOI=10.1080/15384101.2017.1417707;
RA Fernandez-Vizarra E., Zeviani M.;
RT "Mitochondrial complex III Rieske Fe-S protein processing and assembly.";
RL Cell Cycle 17:681-687(2018).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=9204897; DOI=10.1126/science.277.5322.60;
RA Xia D., Yu C.A., Kim H., Xia J.Z., Kachurin A.M., Zhang L., Yu L.,
RA Deisenhofer J.;
RT "Crystal structure of the cytochrome bc1 complex from bovine heart
RT mitochondria.";
RL Science 277:60-66(1997).
RN [8]
RP ERRATUM OF PUBMED:9204897.
RA Xia D., Yu C.A., Kim H., Xia J.Z., Kachurin A.M., Zhang L., Yu L.,
RA Deisenhofer J.;
RL Science 278:2037-2037(1997).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=9651245; DOI=10.1126/science.281.5373.64;
RA Iwata S., Lee J.W., Okada K., Lee J.K., Iwata M., Rasmussen B., Link T.A.,
RA Ramaswamy S., Jap B.K.;
RT "Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1
RT complex.";
RL Science 281:64-71(1998).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RX PubMed=12269811; DOI=10.1021/bi026252p;
RA Gao X., Wen X., Yu C., Esser L., Tsao S., Quinn B., Zhang L., Yu L.,
RA Xia D.;
RT "The crystal structure of mitochondrial cytochrome bc1 in complex with
RT famoxadone: the role of aromatic-aromatic interaction in inhibition.";
RL Biochemistry 41:11692-11702(2002).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS).
RX PubMed=15312779; DOI=10.1016/j.jmb.2004.05.065;
RA Esser L., Quinn B., Li Y.F., Zhang M., Elberry M., Yu L., Yu C.A., Xia D.;
RT "Crystallographic studies of quinol oxidation site inhibitors: a modified
RT classification of inhibitors for the cytochrome bc(1) complex.";
RL J. Mol. Biol. 341:281-302(2004).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=16024040; DOI=10.1016/j.jmb.2005.05.053;
RA Huang L.S., Cobessi D., Tung E.Y., Berry E.A.;
RT "Binding of the respiratory chain inhibitor antimycin to the mitochondrial
RT bc1 complex: a new crystal structure reveals an altered intramolecular
RT hydrogen-bonding pattern.";
RL J. Mol. Biol. 351:573-597(2005).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS).
RX PubMed=16924113; DOI=10.1073/pnas.0601149103;
RA Esser L., Gong X., Yang S., Yu L., Yu C.A., Xia D.;
RT "Surface-modulated motion switch: capture and release of iron-sulfur
RT protein in the cytochrome bc1 complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13045-13050(2006).
RN [14]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.10 ANGSTROMS), AND SUBUNIT.
RX PubMed=27830641; DOI=10.7554/elife.21290;
RA Sousa J.S., Mills D.J., Vonck J., Kuehlbrandt W.;
RT "Functional asymmetry and electron flow in the bovine respirasome.";
RL Elife 5:0-0(2016).
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 (PubMed:9694818,
CC PubMed:11073949). May be involved in the in situ processing of UQCRFS1
CC into the mature Rieske protein and its mitochondrial targeting sequence
CC (MTS)/subunit 9 when incorporated into complex III (Probable). Seems to
CC play an important role in the maintenance of proper mitochondrial
CC function in nigral dopaminergic neurons (By similarity).
CC {ECO:0000250|UniProtKB:P07256, ECO:0000250|UniProtKB:P31930,
CC ECO:0000269|PubMed:11073949, ECO:0000269|PubMed:9694818,
CC ECO:0000305|PubMed:29243944}.
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 (PubMed:9651245). 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)) (PubMed:27830641). Interacts with BRAWNIN (By
CC similarity). Interacts with STMP1 (By similarity).
CC {ECO:0000250|UniProtKB:P31930, ECO:0000250|UniProtKB:Q9CZ13,
CC ECO:0000269|PubMed:27830641, ECO:0000269|PubMed:9651245}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X59692; CAA42213.1; -; mRNA.
DR PIR; S16220; ZPBOC1.
DR RefSeq; NP_777054.1; NM_174629.2.
DR PDB; 1BCC; X-ray; 3.16 A; A=35-480.
DR PDB; 1BE3; X-ray; 3.00 A; A=35-480.
DR PDB; 1BGY; X-ray; 3.00 A; A/M=35-480.
DR PDB; 1L0L; X-ray; 2.35 A; A=35-480.
DR PDB; 1L0N; X-ray; 2.60 A; A=35-480.
DR PDB; 1NTK; X-ray; 2.60 A; A=35-480.
DR PDB; 1NTM; X-ray; 2.40 A; A=35-480.
DR PDB; 1NTZ; X-ray; 2.60 A; A=35-480.
DR PDB; 1NU1; X-ray; 3.20 A; A=35-480.
DR PDB; 1PP9; X-ray; 2.10 A; A/N=35-480.
DR PDB; 1PPJ; X-ray; 2.10 A; A/N=35-480.
DR PDB; 1QCR; X-ray; 2.70 A; A=35-480.
DR PDB; 1SQB; X-ray; 2.69 A; A=1-480.
DR PDB; 1SQP; X-ray; 2.70 A; A=1-480.
DR PDB; 1SQQ; X-ray; 3.00 A; A=35-480.
DR PDB; 1SQV; X-ray; 2.85 A; A=35-480.
DR PDB; 1SQX; X-ray; 2.60 A; A=35-480.
DR PDB; 2A06; X-ray; 2.10 A; A/N=35-480.
DR PDB; 2BCC; X-ray; 3.50 A; A=35-480.
DR PDB; 2FYU; X-ray; 2.26 A; A=35-480.
DR PDB; 2YBB; EM; 19.00 A; A/a=35-480.
DR PDB; 3BCC; X-ray; 3.70 A; A=35-480.
DR PDB; 4D6T; X-ray; 3.57 A; A/N=1-480.
DR PDB; 4D6U; X-ray; 4.09 A; A=1-480.
DR PDB; 5GPN; EM; 5.40 A; A/M=35-480.
DR PDB; 5KLV; X-ray; 2.65 A; A=35-480.
DR PDB; 5LUF; EM; 9.10 A; c/l=35-480.
DR PDB; 5NMI; X-ray; 3.50 A; A/N=36-479.
DR PDB; 5OKD; X-ray; 3.10 A; A=1-480.
DR PDB; 6FO0; EM; 4.10 A; A/N=1-480.
DR PDB; 6FO2; EM; 4.40 A; A/N=1-480.
DR PDB; 6FO6; EM; 4.10 A; A/N=1-480.
DR PDB; 6HAW; X-ray; 3.45 A; A=36-479.
DR PDB; 6NHG; X-ray; 2.80 A; A=35-480.
DR PDB; 6XVF; X-ray; 3.50 A; A=36-480.
DR PDB; 6ZFS; X-ray; 3.50 A; A=36-479.
DR PDB; 6ZFT; X-ray; 3.30 A; A=37-480.
DR PDB; 6ZFU; X-ray; 3.50 A; A=36-479.
DR PDBsum; 1BCC; -.
DR PDBsum; 1BE3; -.
DR PDBsum; 1BGY; -.
DR PDBsum; 1L0L; -.
DR PDBsum; 1L0N; -.
DR PDBsum; 1NTK; -.
DR PDBsum; 1NTM; -.
DR PDBsum; 1NTZ; -.
DR PDBsum; 1NU1; -.
DR PDBsum; 1PP9; -.
DR PDBsum; 1PPJ; -.
DR PDBsum; 1QCR; -.
DR PDBsum; 1SQB; -.
DR PDBsum; 1SQP; -.
DR PDBsum; 1SQQ; -.
DR PDBsum; 1SQV; -.
DR PDBsum; 1SQX; -.
DR PDBsum; 2A06; -.
DR PDBsum; 2BCC; -.
DR PDBsum; 2FYU; -.
DR PDBsum; 2YBB; -.
DR PDBsum; 3BCC; -.
DR PDBsum; 4D6T; -.
DR PDBsum; 4D6U; -.
DR PDBsum; 5GPN; -.
DR PDBsum; 5KLV; -.
DR PDBsum; 5LUF; -.
DR PDBsum; 5NMI; -.
DR PDBsum; 5OKD; -.
DR PDBsum; 6FO0; -.
DR PDBsum; 6FO2; -.
DR PDBsum; 6FO6; -.
DR PDBsum; 6HAW; -.
DR PDBsum; 6NHG; -.
DR PDBsum; 6XVF; -.
DR PDBsum; 6ZFS; -.
DR PDBsum; 6ZFT; -.
DR PDBsum; 6ZFU; -.
DR AlphaFoldDB; P31800; -.
DR SMR; P31800; -.
DR CORUM; P31800; -.
DR DIP; DIP-1105N; -.
DR IntAct; P31800; 3.
DR STRING; 9913.ENSBTAP00000025422; -.
DR MEROPS; M16.973; -.
DR MEROPS; M16.981; -.
DR PaxDb; P31800; -.
DR PeptideAtlas; P31800; -.
DR PRIDE; P31800; -.
DR GeneID; 282393; -.
DR KEGG; bta:282393; -.
DR CTD; 7384; -.
DR eggNOG; KOG0960; Eukaryota.
DR InParanoid; P31800; -.
DR OrthoDB; 638125at2759; -.
DR BRENDA; 7.1.1.8; 908.
DR EvolutionaryTrace; P31800; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:AgBase.
DR GO; GO:0005739; C:mitochondrion; ISS:AgBase.
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 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 3D-structure; Acetylation; Direct protein sequencing; Electron transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Respiratory chain; Transit peptide; Transport.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2848575"
FT CHAIN 35..480
FT /note="Cytochrome b-c1 complex subunit 1, mitochondrial"
FT /id="PRO_0000026785"
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:0000250|UniProtKB:Q68FY0"
FT MOD_RES 248
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZ13"
FT HELIX 38..42
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1L0N"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1PP9"
FT TURN 84..88
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2BCC"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:1PP9"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 140..153
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 158..175
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 179..191
FT /evidence="ECO:0007829|PDB:1PP9"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 205..210
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 239..250
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:2FYU"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:1NTM"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 282..293
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 301..311
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 327..335
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 339..347
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 352..360
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:1NTM"
FT HELIX 365..382
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 385..402
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 406..419
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:5KLV"
FT HELIX 426..434
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 438..448
FT /evidence="ECO:0007829|PDB:1PP9"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 455..461
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:5OKD"
FT HELIX 468..473
FT /evidence="ECO:0007829|PDB:1PP9"
SQ SEQUENCE 480 AA; 52736 MW; 4E54DD28C1905392 CRC64;
MAASAVCRAA GAGTRVLLRT RRSPALLRSS DLRGTATYAQ ALQSVPETQV SQLDNGLRVA
SEQSSQPTCT VGVWIDAGSR YESEKNNGAG YFVEHLAFKG TKNRPGNALE KEVESMGAHL
NAYSTREHTA YYIKALSKDL PKAVELLADI VQNCSLEDSQ IEKERDVILQ ELQENDTSMR
DVVFNYLHAT AFQGTPLAQS VEGPSENVRK LSRADLTEYL SRHYKAPRMV LAAAGGLEHR
QLLDLAQKHF SGLSGTYDED AVPTLSPCRF TGSQICHRED GLPLAHVAIA VEGPGWAHPD
NVALQVANAI IGHYDCTYGG GAHLSSPLAS IAATNKLCQS FQTFNICYAD TGLLGAHFVC
DHMSIDDMMF VLQGQWMRLC TSATESEVLR GKNLLRNALV SHLDGTTPVC EDIGRSLLTY
GRRIPLAEWE SRIAEVDARV VREVCSKYFY DQCPAVAGFG PIEQLPDYNR IRSGMFWLRF
