QCR2_MOUSE
ID QCR2_MOUSE Reviewed; 453 AA.
AC Q9DB77; Q8BK11; Q9CVK7;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 178.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Pancreas, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP PROTEIN SEQUENCE OF 24-60; 71-85; 117-147; 163-196; 200-241; 301-315;
RP 360-375 AND 436-453, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP SUBUNIT.
RX PubMed=19026783; DOI=10.1016/j.molcel.2008.10.021;
RA Acin-Perez R., Fernandez-Silva P., Peleato M.L., Perez-Martos A.,
RA Enriquez J.A.;
RT "Respiratory active mitochondrial supercomplexes.";
RL Mol. Cell 32:529-539(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66; LYS-199 AND LYS-250, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [7]
RP SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=30666338; DOI=10.1007/s00018-019-03007-6;
RA Shan W., Li J., Xu W., Li H., Zuo Z.;
RT "Critical role of UQCRC1 in embryo survival, brain ischemic tolerance and
RT normal cognition in mice.";
RL Cell. Mol. Life Sci. 76:1381-1396(2019).
RN [8]
RP INTERACTION WITH RAB5IF.
RX PubMed=31536960; DOI=10.1016/j.isci.2019.08.057;
RA Moutaoufik M.T., Malty R., Amin S., Zhang Q., Phanse S., Gagarinova A.,
RA Zilocchi M., Hoell L., Minic Z., Gagarinova M., Aoki H., Stockwell J.,
RA Jessulat M., Goebels F., Broderick K., Scott N.E., Vlasblom J., Musso G.,
RA Prasad B., Lamantea E., Garavaglia B., Rajput A., Murayama K., Okazaki Y.,
RA Foster L.J., Bader G.D., Cayabyab F.S., Babu M.;
RT "Rewiring of the Human Mitochondrial Interactome during Neuronal
RT Reprogramming Reveals Regulators of the Respirasome and Neurogenesis.";
RL IScience 19:1114-1132(2019).
RN [9]
RP INTERACTION WITH STMP1.
RX PubMed=35101990; DOI=10.1073/pnas.2120476119;
RA Makarewich C.A., Munir A.Z., Bezprozvannaya S., Gibson A.M., Young Kim S.,
RA Martin-Sandoval M.S., Mathews T.P., Szweda L.I., Bassel-Duby R.,
RA Olson E.N.;
RT "The cardiac-enriched microprotein mitolamban regulates mitochondrial
RT respiratory complex assembly and function in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 119:0-0(2022).
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). {ECO:0000250|UniProtKB:P07257,
CC ECO:0000250|UniProtKB:P23004}.
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)) (PubMed:19026783, PubMed:30666338). Interacts with
CC RAB5IF (PubMed:31536960). Interacts with STMP1 (PubMed:35101990).
CC {ECO:0000250|UniProtKB:P23004, ECO:0000269|PubMed:19026783,
CC ECO:0000269|PubMed:30666338, ECO:0000269|PubMed:31536960,
CC ECO:0000269|PubMed:35101990}.
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 -!- TISSUE SPECIFICITY: Expressed in neurons and astrocytes of the cerebral
CC cortex and hippocampus (at protein level).
CC {ECO:0000269|PubMed:30666338}.
CC -!- PTM: Acetylation of Lys-159 and Lys-250 is observed in liver
CC mitochondria from fasted mice but not from fed mice.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC2/QCR2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK005151; BAB23845.1; -; mRNA.
DR EMBL; AK007669; BAB25176.1; -; mRNA.
DR EMBL; AK077583; BAC36876.1; -; mRNA.
DR EMBL; AK088103; BAC40146.1; -; mRNA.
DR EMBL; BC003423; AAH03423.1; -; mRNA.
DR CCDS; CCDS21795.1; -.
DR PIR; PC7073; PC7073.
DR RefSeq; NP_080175.1; NM_025899.2.
DR PDB; 7O37; EM; 3.20 A; B/M=15-453.
DR PDB; 7O3C; EM; 3.30 A; B/M=15-453.
DR PDB; 7O3E; EM; 3.60 A; B/M=15-453.
DR PDB; 7O3H; EM; 2.60 A; B/M=15-453.
DR PDBsum; 7O37; -.
DR PDBsum; 7O3C; -.
DR PDBsum; 7O3E; -.
DR PDBsum; 7O3H; -.
DR AlphaFoldDB; Q9DB77; -.
DR SMR; Q9DB77; -.
DR BioGRID; 211868; 74.
DR ComplexPortal; CPX-563; Mitochondrial respiratory chain complex III.
DR CORUM; Q9DB77; -.
DR IntAct; Q9DB77; 16.
DR MINT; Q9DB77; -.
DR STRING; 10090.ENSMUSP00000033176; -.
DR MEROPS; M16.974; -.
DR iPTMnet; Q9DB77; -.
DR PhosphoSitePlus; Q9DB77; -.
DR SwissPalm; Q9DB77; -.
DR EPD; Q9DB77; -.
DR jPOST; Q9DB77; -.
DR MaxQB; Q9DB77; -.
DR PaxDb; Q9DB77; -.
DR PeptideAtlas; Q9DB77; -.
DR PRIDE; Q9DB77; -.
DR ProteomicsDB; 300330; -.
DR TopDownProteomics; Q9DB77; -.
DR Antibodypedia; 1267; 245 antibodies from 30 providers.
DR DNASU; 67003; -.
DR Ensembl; ENSMUST00000033176; ENSMUSP00000033176; ENSMUSG00000030884.
DR GeneID; 67003; -.
DR KEGG; mmu:67003; -.
DR UCSC; uc009jms.1; mouse.
DR CTD; 7385; -.
DR MGI; MGI:1914253; Uqcrc2.
DR VEuPathDB; HostDB:ENSMUSG00000030884; -.
DR eggNOG; KOG2583; Eukaryota.
DR GeneTree; ENSGT00940000154915; -.
DR HOGENOM; CLU_009902_0_0_1; -.
DR InParanoid; Q9DB77; -.
DR OMA; WVGEFFT; -.
DR OrthoDB; 1000258at2759; -.
DR PhylomeDB; Q9DB77; -.
DR TreeFam; TF105033; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR BioGRID-ORCS; 67003; 24 hits in 74 CRISPR screens.
DR ChiTaRS; Uqcrc2; mouse.
DR PRO; PR:Q9DB77; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9DB77; protein.
DR Bgee; ENSMUSG00000030884; Expressed in paneth cell and 267 other tissues.
DR ExpressionAtlas; Q9DB77; baseline and differential.
DR Genevisible; Q9DB77; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IDA:UniProtKB.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0045333; P:cellular respiration; IC:ComplexPortal.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IC:ComplexPortal.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
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; Phosphoprotein;
KW Reference proteome; Respiratory chain; Transit peptide; Transport.
FT TRANSIT 1..14
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 15..453
FT /note="Cytochrome b-c1 complex subunit 2, mitochondrial"
FT /id="PRO_0000026792"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 250
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32551"
FT CONFLICT 36
FT /note="Q -> L (in Ref. 1; BAB25176)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="Q -> R (in Ref. 1; BAC36876)"
FT /evidence="ECO:0000305"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 57..66
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:7O3C"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:7O3H"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:7O3C"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:7O3H"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 130..142
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 148..165
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:7O3H"
FT TURN 194..199
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 227..237
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 265..275
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:7O37"
FT HELIX 281..293
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 308..314
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 322..330
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 333..344
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 347..362
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 368..386
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 389..402
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 409..417
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 421..433
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 436..442
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:7O37"
SQ SEQUENCE 453 AA; 48235 MW; 24A2BDDDA657867E CRC64;
MKLLSRAGSF SRFYSLKVAP KVKTSAAPGG VPLQPQDLEF TKLPNGLVIA SLENYAPLSR
IGLFVKAGSR YEDSNNLGTS HLLRLASSLT TKGASSFKIT RGIEAVGGKL SVTATRENMA
YTVEGIRSDI EILMEFLLNV TTAPEFRRWE VAALRSQLKI DKAVAFQNSQ TRIIENLHDV
AYKNALANPL YCPDYRMGKI TSEELHYFVQ NHFTSARMAL VGLGVSHSVL KQVAEQFLNM
RGGLGLAGAK AKYRGGEIRE QNGDNLVHAA IVAESAAIGN AEANAFSVLQ HLLGAGPHIK
RGNNTTSLLS QSVAKGSHQP FDVSAFNASY SDSGLFGIYT ISQAAAAGEV INAAYNQVKA
VAQGNLSSAD VQAAKNKLKA GYLMSVETSE GFLSEIGSQA LAAGSYMPPS TVLQQIDSVA
DADVVKAAKK FVSGKKSMAA SGNLGHTPFL DEL
