QCR2_RAT
ID QCR2_RAT Reviewed; 452 AA.
AC P32551; Q5XIR3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 158.
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 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 [MRNA].
RX PubMed=2162168;
RA Hosokawa Y., Suzuki H., Toda H., Nishikimi M., Ozawa T.;
RT "The primary structure of the precursor to core protein II, a putative
RT member of mitochondrial processing protease family, of rat mitochondrial
RT cytochrome bc1 complex deduced from cDNA sequence analysis.";
RL Biochem. Int. 20:731-737(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 42-59; 183-195 AND 231-240, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=19423663; DOI=10.1530/rep-09-0052;
RA Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.;
RT "Identification of novel immunodominant epididymal sperm proteins using
RT combinatorial approach.";
RL Reproduction 138:81-93(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, AND IDENTIFICATION BY
RP 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). {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)) (By similarity). Interacts with RAB5IF (By
CC similarity). Interacts with STMP1 (By similarity).
CC {ECO:0000250|UniProtKB:P22695, ECO:0000250|UniProtKB:P23004,
CC ECO:0000250|UniProtKB:Q9DB77}.
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 the head region and flagellum of
CC epididymal sperm. {ECO:0000269|PubMed:19423663}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC2/QCR2 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC083610; AAH83610.1; -; mRNA.
DR PIR; S29510; S29510.
DR RefSeq; NP_001006971.1; NM_001006970.1.
DR AlphaFoldDB; P32551; -.
DR SMR; P32551; -.
DR BioGRID; 254272; 5.
DR CORUM; P32551; -.
DR IntAct; P32551; 7.
DR MINT; P32551; -.
DR STRING; 10116.ENSRNOP00000021514; -.
DR MEROPS; M16.974; -.
DR CarbonylDB; P32551; -.
DR iPTMnet; P32551; -.
DR PhosphoSitePlus; P32551; -.
DR World-2DPAGE; 0004:P32551; -.
DR jPOST; P32551; -.
DR PaxDb; P32551; -.
DR PRIDE; P32551; -.
DR Ensembl; ENSRNOT00000021514; ENSRNOP00000021514; ENSRNOG00000036742.
DR GeneID; 293448; -.
DR KEGG; rno:293448; -.
DR UCSC; RGD:1359150; rat.
DR CTD; 7385; -.
DR RGD; 1359150; Uqcrc2.
DR eggNOG; KOG2583; Eukaryota.
DR GeneTree; ENSGT00940000154915; -.
DR HOGENOM; CLU_009902_0_0_1; -.
DR InParanoid; P32551; -.
DR OMA; WVGEFFT; -.
DR OrthoDB; 1000258at2759; -.
DR PhylomeDB; P32551; -.
DR TreeFam; TF105033; -.
DR Reactome; R-RNO-611105; Respiratory electron transport.
DR PRO; PR:P32551; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000036742; Expressed in heart and 20 other tissues.
DR Genevisible; P32551; 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:0005751; C:mitochondrial respiratory chain complex IV; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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 Acetylation; Direct protein sequencing; Electron transport; Membrane;
KW 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..452
FT /note="Cytochrome b-c1 complex subunit 2, mitochondrial"
FT /id="PRO_0000026793"
FT MOD_RES 65
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB77"
FT MOD_RES 198
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB77"
FT MOD_RES 249
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB77"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 445
FT /note="H -> N (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 48396 MW; F4FFCA59CEB04270 CRC64;
MKLLSRAGSF SRFYSLKVAP KLKTSAPGGV PLQPQELEFT KLPNGLVIAS LENYAPLSRI
GLFIKAGSRY ENYNYLGTSH LLRLASTLTT KGASSFKITR GIEAVGGKLS VTATRENMAY
TVEGIRDDIE ILMEFLLNVT TAPEFRRWEV AALRSQLKID KAVAFQNPQT RIIENLHDVA
YKNALANPLY CPDYRMGKIT SEELHYFVQN HFTSARMALV GLGVSHSILK EVAEQFLNIR
GGLGLAGAKA KYRGGEIREQ NGDNLVHAAI VAESAAIGNA EANAFSVLQH LLGAGPHIKR
GNNTTSLLSQ SVAKGSQQPF DVSAFNASYS DSGLFGIYTV SQAAAAGDVI NAAYNQVKAV
AQGNLSSADV QAAKNKLKAG YLMSVETSEG FLSEIGSQAL ATGSYMPPPT VLQQIDAVAD
ADVVKAAKKF VSGKKSMTAS GNLGHTPFLD EL
