QCR1_EUGGR
ID QCR1_EUGGR Reviewed; 494 AA.
AC P43264;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Ubiquinol-cytochrome-c reductase complex core protein I, mitochondrial;
DE Flags: Precursor;
OS Euglena gracilis.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC Euglenales; Euglenaceae; Euglena.
OX NCBI_TaxID=3039;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SM-ZK;
RX PubMed=8188644; DOI=10.1093/oxfordjournals.jbchem.a124312;
RA Cui J.-Y., Mukai K., Saeki K., Matsubara H.;
RT "Molecular cloning and nucleotide sequences of cDNAs encoding subunits I,
RT II, and IX of Euglena gracilis mitochondrial complex III.";
RL J. Biochem. 115:98-107(1994).
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. {ECO:0000250|UniProtKB:P07256}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 10 subunits. The complex is composed of 3 respiratory
CC subunits cytochrome b, cytochrome c1 and Rieske protein, 2 core protein
CC subunits, and additional low-molecular weight protein subunits. The
CC complex exists as an obligatory dimer and forms supercomplexes (SCs) in
CC the inner mitochondrial membrane with cytochrome c oxidase (complex IV,
CC CIV). {ECO:0000250|UniProtKB:P07256}.
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 -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC1/QCR1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA04079.2; Type=Miscellaneous discrepancy; Note=Incorrect translation table.; Evidence={ECO:0000305};
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DR EMBL; D16671; BAA04079.2; ALT_SEQ; mRNA.
DR PIR; JX0300; JX0300.
DR AlphaFoldDB; P43264; -.
DR SMR; P43264; -.
DR DrugCentral; P43264; -.
DR MEROPS; M16.003; -.
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:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Electron transport; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Mitochondrion; Mitochondrion inner membrane; Protease; Respiratory chain;
KW Transit peptide; Transport; Zinc.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..494
FT /note="Ubiquinol-cytochrome-c reductase complex core
FT protein I, mitochondrial"
FT /id="PRO_0000026789"
FT ACT_SITE 73
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
SQ SEQUENCE 494 AA; 54934 MW; 494D4C9AF74BDB9C CRC64;
MTTPSLSSIL RHTRPIFKET LRAARPTLQN ALPNGFRIAS ESKDGDTCTV GVWIDAGSRW
ETEKNNGVAH FLEHMNFKGT GKRSRQDIEF GMEKMGAHLN AYTSREHTCY YVKCFKKDVP
EAVDILADIL LNSKRTEQDL DAERQTIVQE KEDVEARIDE VLMDHLHSAA FEGSGLGLSI
LGPLENIQKS ITKGMIDDFV KTHYTGPRMA LVGSGAVDHG QLCDLASKYF GALPTGQPKP
SGFTRFLGGD KRETNQLNPL THVAVAFQTP GISHPDAIKI KVLEQLLGSY SRDKGEAAYS
CFARAIVMDF YDPKVGQFFR PNKAGHNPIH SLNAFWAPYS DVGLLGFYAI AEPGKSYGHE
WENILHYAMR ELIRVSRNIS EEEFERAKNQ LKLQTMLQLD GTTNIADDIG RQVLSFGARV
PLASFFEQLD AISREDLIRV GPRVLLRQGP RGGGDWRHGQ RARVRRPAGG DLLRGPLSCP
LCTPLPRQSV VCMA
