QCR2_BOVIN
ID QCR2_BOVIN Reviewed; 453 AA.
AC P23004; Q3ZCG7; Q5E9C7;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Cytochrome b-c1 complex subunit 2, mitochondrial;
DE AltName: Full=Complex III subunit 2;
DE AltName: Full=Core protein II;
DE AltName: Full=Ubiquinol-cytochrome-c reductase complex core protein 2;
DE Flags: Precursor;
GN Name=UQCRC2;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 15-46.
RX PubMed=2841307; DOI=10.1007/bf00769634;
RA Capaldi R.A., Gonzalez-Halphen D., Zhang Y.-Z., Yanamura W.;
RT "Complexity and tissue specificity of the mitochondrial respiratory
RT chain.";
RL J. Bioenerg. Biomembr. 20:291-311(1988).
RN [5]
RP PROTEIN SEQUENCE OF 15-43.
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
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).
CC {ECO:0000250|UniProtKB:P07257, ECO:0000269|PubMed:11073949,
CC ECO:0000269|PubMed:9694818, 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 RAB5IF (By
CC similarity). Interacts with STMP1 (By similarity).
CC {ECO:0000250|UniProtKB:P22695, ECO:0000250|UniProtKB:Q9DB77,
CC ECO:0000269|PubMed:27830641, ECO:0000269|PubMed:9651245}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P07257}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P07257}; Matrix side
CC {ECO:0000250|UniProtKB:P07257}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC2/QCR2 subfamily.
CC {ECO:0000305}.
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DR EMBL; X59693; CAA42214.1; -; mRNA.
DR EMBL; BT020993; AAX09010.1; -; mRNA.
DR EMBL; BC102337; AAI02338.1; -; mRNA.
DR PIR; S16221; ZPBOC2.
DR RefSeq; NP_777055.1; NM_174630.2.
DR PDB; 1BCC; X-ray; 3.16 A; B=32-453.
DR PDB; 1BE3; X-ray; 3.00 A; B=15-453.
DR PDB; 1BGY; X-ray; 3.00 A; B/N=15-453.
DR PDB; 1L0L; X-ray; 2.35 A; B=15-453.
DR PDB; 1L0N; X-ray; 2.60 A; B=15-453.
DR PDB; 1NTK; X-ray; 2.60 A; B=15-453.
DR PDB; 1NTM; X-ray; 2.40 A; B=15-453.
DR PDB; 1NTZ; X-ray; 2.60 A; B=15-453.
DR PDB; 1NU1; X-ray; 3.20 A; B=15-453.
DR PDB; 1PP9; X-ray; 2.10 A; B/O=15-453.
DR PDB; 1PPJ; X-ray; 2.10 A; B/O=15-453.
DR PDB; 1QCR; X-ray; 2.70 A; B=31-453.
DR PDB; 1SQB; X-ray; 2.69 A; B=1-453.
DR PDB; 1SQP; X-ray; 2.70 A; B=1-453.
DR PDB; 1SQQ; X-ray; 3.00 A; B=15-453.
DR PDB; 1SQV; X-ray; 2.85 A; B=15-453.
DR PDB; 1SQX; X-ray; 2.60 A; B=15-453.
DR PDB; 2A06; X-ray; 2.10 A; B/O=15-453.
DR PDB; 2BCC; X-ray; 3.50 A; B=32-453.
DR PDB; 2FYU; X-ray; 2.26 A; B=15-453.
DR PDB; 2YBB; EM; 19.00 A; B/b=15-453.
DR PDB; 3BCC; X-ray; 3.70 A; B=32-453.
DR PDB; 4D6T; X-ray; 3.57 A; B/O=1-453.
DR PDB; 4D6U; X-ray; 4.09 A; B/O=1-453.
DR PDB; 5GPN; EM; 5.40 A; B/N=15-453.
DR PDB; 5KLV; X-ray; 2.65 A; B=15-453.
DR PDB; 5LUF; EM; 9.10 A; m/n=15-453.
DR PDB; 5NMI; X-ray; 3.50 A; B/O=31-453.
DR PDB; 5OKD; X-ray; 3.10 A; B=1-453.
DR PDB; 6FO0; EM; 4.10 A; B/O=1-453.
DR PDB; 6FO2; EM; 4.40 A; B/O=1-453.
DR PDB; 6FO6; EM; 4.10 A; B/O=1-453.
DR PDB; 6HAW; X-ray; 3.45 A; B=36-453.
DR PDB; 6NHG; X-ray; 2.80 A; B=15-453.
DR PDB; 6XVF; X-ray; 3.50 A; B=36-453.
DR PDB; 6ZFS; X-ray; 3.50 A; B=34-453.
DR PDB; 6ZFT; X-ray; 3.30 A; B=34-453.
DR PDB; 6ZFU; X-ray; 3.50 A; B=34-453.
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; P23004; -.
DR SMR; P23004; -.
DR CORUM; P23004; -.
DR DIP; DIP-1106N; -.
DR IntAct; P23004; 2.
DR STRING; 9913.ENSBTAP00000028853; -.
DR MEROPS; M16.974; -.
DR PaxDb; P23004; -.
DR PeptideAtlas; P23004; -.
DR PRIDE; P23004; -.
DR Ensembl; ENSBTAT00000028853; ENSBTAP00000028853; ENSBTAG00000021651.
DR GeneID; 282394; -.
DR KEGG; bta:282394; -.
DR CTD; 7385; -.
DR VEuPathDB; HostDB:ENSBTAG00000021651; -.
DR VGNC; VGNC:36696; UQCRC2.
DR eggNOG; KOG2583; Eukaryota.
DR GeneTree; ENSGT00940000154915; -.
DR HOGENOM; CLU_009902_0_0_1; -.
DR InParanoid; P23004; -.
DR OMA; WVGEFFT; -.
DR OrthoDB; 1000258at2759; -.
DR TreeFam; TF105033; -.
DR EvolutionaryTrace; P23004; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000021651; Expressed in cardiac ventricle and 104 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Electron transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Respiratory chain; Transit peptide; Transport.
FT TRANSIT 1..14
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2841307,
FT ECO:0000269|PubMed:2848575"
FT CHAIN 15..453
FT /note="Cytochrome b-c1 complex subunit 2, mitochondrial"
FT /id="PRO_0000026790"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB77"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB77"
FT MOD_RES 250
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB77"
FT VARIANT 41
FT /note="T -> R"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1BCC"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 57..66
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1PP9"
FT TURN 74..78
FT /evidence="ECO:0007829|PDB:1L0N"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:1PP9"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 130..142
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 148..165
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1PP9"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 227..237
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:1SQB"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 265..274
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:1SQV"
FT HELIX 281..293
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:1SQB"
FT HELIX 308..316
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 321..330
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 333..343
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 347..362
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 368..385
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 389..403
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 409..417
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 421..433
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 436..442
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:1PP9"
SQ SEQUENCE 453 AA; 48149 MW; B7C600DA71CD34CF CRC64;
MKLLTRAGSL SRFYSLKVAP KVKATEAPAG VPPHPQDLEF TRLPNGLVIA SLENYAPASR
IGLFIKAGSR YENSNNLGTS HLLRLASSLT TKGASSFKIT RGIEAVGGKL SVTSTRENMA
YTVECLRDDV DILMEFLLNV TTAPEFRRWE VAALQPQLRI DKAVALQNPQ AHVIENLHAA
AYRNALANSL YCPDYRIGKV TPVELHDYVQ NHFTSARMAL IGLGVSHPVL KQVAEQFLNI
RGGLGLSGAK AKYHGGEIRE QNGDSLVHAA LVAESAAIGS AEANAFSVLQ HVLGAGPHVK
RGSNATSSLY QAVAKGVHQP FDVSAFNASY SDSGLFGFYT ISQAASAGDV IKAAYNQVKT
IAQGNLSNPD VQAAKNKLKA GYLMSVESSE GFLDEVGSQA LAAGSYTPPS TVLQQIDAVA
DADVINAAKK FVSGRKSMAA SGNLGHTPFI DEL
