QCR9_HUMAN
ID QCR9_HUMAN Reviewed; 63 AA.
AC Q9UDW1; B5MCM5; Q9T2V6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Cytochrome b-c1 complex subunit 9;
DE AltName: Full=Complex III subunit 9;
DE AltName: Full=Complex III subunit X;
DE AltName: Full=Cytochrome c1 non-heme 7 kDa protein;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex 7.2 kDa protein;
GN Name=UQCR10; Synonyms=UCRC; ORFNames=HSPC119;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Nakamura Y.;
RT "Isolation and characterization of a human cDNA homologous to the bovine
RT ubiquinol-cytochrome c reductase 7.2kDa protein.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow, and Urinary bladder;
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 [5]
RP PROTEIN SEQUENCE OF 2-16.
RC TISSUE=Heart, and Liver;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS).
RX PubMed=28844695; DOI=10.1016/j.cell.2017.07.050;
RA Guo R., Zong S., Wu M., Gu J., Yang M.;
RT "Architecture of human mitochondrial respiratory megacomplex I2III2IV2.";
RL Cell 170:1247-1257(2017).
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:P22289}.
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:28844695). Interacts with STMP1 (By
CC similarity). {ECO:0000250|UniProtKB:P00130,
CC ECO:0000250|UniProtKB:Q8R1I1, ECO:0000269|PubMed:28844695}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P22289}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P22289}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UDW1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UDW1-2; Sequence=VSP_041429;
CC -!- SIMILARITY: Belongs to the UQCR10/QCR9 family. {ECO:0000305}.
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DR EMBL; AB028598; BAB20672.1; -; mRNA.
DR EMBL; AF161468; AAF29083.1; -; mRNA.
DR EMBL; AC004882; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005402; AAH05402.1; -; mRNA.
DR EMBL; BC015971; AAH15971.1; -; mRNA.
DR CCDS; CCDS46680.1; -. [Q9UDW1-1]
DR CCDS; CCDS46681.1; -. [Q9UDW1-2]
DR RefSeq; NP_001003684.1; NM_001003684.1. [Q9UDW1-2]
DR RefSeq; NP_037519.2; NM_013387.3. [Q9UDW1-1]
DR PDB; 5XTE; EM; 3.40 A; D/Q=2-63.
DR PDB; 5XTH; EM; 3.90 A; AD/AQ=2-63.
DR PDB; 5XTI; EM; 17.40 A; AD/AQ=2-63.
DR PDBsum; 5XTE; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; Q9UDW1; -.
DR SMR; Q9UDW1; -.
DR BioGRID; 118920; 62.
DR ComplexPortal; CPX-560; Mitochondrial respiratory chain complex III.
DR IntAct; Q9UDW1; 14.
DR MINT; Q9UDW1; -.
DR STRING; 9606.ENSP00000332887; -.
DR ChEMBL; CHEMBL2388; -.
DR DrugBank; DB07763; (5S)-3-ANILINO-5-(2,4-DIFLUOROPHENYL)-5-METHYL-1,3-OXAZOLIDINE-2,4-DIONE.
DR DrugBank; DB07778; (S)-famoxadone.
DR DrugBank; DB04141; 2-Hexyloxy-6-Hydroxymethyl-Tetrahydro-Pyran-3,4,5-Triol.
DR DrugBank; DB08453; 2-Nonyl-4-quinolinol 1-oxide.
DR DrugBank; DB07636; 5-Heptyl-6-hydroxy-1,3-benzothiazole-4,7-dione.
DR DrugBank; DB04799; 6-Hydroxy-5-undecyl-4,7-benzothiazoledione.
DR DrugBank; DB07401; Azoxystrobin.
DR DrugBank; DB08330; METHYL (2Z)-3-METHOXY-2-{2-[(E)-2-PHENYLVINYL]PHENYL}ACRYLATE.
DR DrugBank; DB08690; Ubiquinone Q2.
DR GlyGen; Q9UDW1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UDW1; -.
DR SwissPalm; Q9UDW1; -.
DR BioMuta; UQCR10; -.
DR DMDM; 9297078; -.
DR EPD; Q9UDW1; -.
DR jPOST; Q9UDW1; -.
DR MassIVE; Q9UDW1; -.
DR MaxQB; Q9UDW1; -.
DR PaxDb; Q9UDW1; -.
DR PeptideAtlas; Q9UDW1; -.
DR PRIDE; Q9UDW1; -.
DR ProteomicsDB; 84120; -. [Q9UDW1-1]
DR ProteomicsDB; 84121; -. [Q9UDW1-2]
DR TopDownProteomics; Q9UDW1-1; -. [Q9UDW1-1]
DR TopDownProteomics; Q9UDW1-2; -. [Q9UDW1-2]
DR Antibodypedia; 24577; 91 antibodies from 22 providers.
DR DNASU; 29796; -.
DR Ensembl; ENST00000330029.6; ENSP00000332887.6; ENSG00000184076.13. [Q9UDW1-1]
DR Ensembl; ENST00000401406.3; ENSP00000384962.3; ENSG00000184076.13. [Q9UDW1-2]
DR GeneID; 29796; -.
DR KEGG; hsa:29796; -.
DR MANE-Select; ENST00000330029.6; ENSP00000332887.6; NM_013387.4; NP_037519.2.
DR UCSC; uc003agp.2; human. [Q9UDW1-1]
DR CTD; 29796; -.
DR DisGeNET; 29796; -.
DR GeneCards; UQCR10; -.
DR HGNC; HGNC:30863; UQCR10.
DR HPA; ENSG00000184076; Tissue enhanced (skeletal).
DR MIM; 610843; gene.
DR neXtProt; NX_Q9UDW1; -.
DR OpenTargets; ENSG00000184076; -.
DR PharmGKB; PA165378374; -.
DR VEuPathDB; HostDB:ENSG00000184076; -.
DR eggNOG; KOG3494; Eukaryota.
DR GeneTree; ENSGT00390000014052; -.
DR HOGENOM; CLU_171977_2_0_1; -.
DR InParanoid; Q9UDW1; -.
DR OMA; DIKHRYI; -.
DR OrthoDB; 1624769at2759; -.
DR PhylomeDB; Q9UDW1; -.
DR TreeFam; TF324385; -.
DR BioCyc; MetaCyc:HS15855-MON; -.
DR PathwayCommons; Q9UDW1; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR SignaLink; Q9UDW1; -.
DR SIGNOR; Q9UDW1; -.
DR BioGRID-ORCS; 29796; 208 hits in 1075 CRISPR screens.
DR ChiTaRS; UQCR10; human.
DR GeneWiki; UCRC; -.
DR GenomeRNAi; 29796; -.
DR Pharos; Q9UDW1; Tbio.
DR PRO; PR:Q9UDW1; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9UDW1; protein.
DR Bgee; ENSG00000184076; Expressed in body of tongue and 209 other tissues.
DR Genevisible; Q9UDW1; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IPI:ComplexPortal.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; NAS:UniProtKB.
DR GO; GO:0045333; P:cellular respiration; IC:ComplexPortal.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR Gene3D; 1.20.5.260; -; 1.
DR InterPro; IPR008027; QCR9.
DR InterPro; IPR036656; QCR9_sf.
DR PANTHER; PTHR12980; PTHR12980; 1.
DR Pfam; PF05365; UCR_UQCRX_QCR9; 1.
DR SUPFAM; SSF81514; SSF81514; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8592474,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..63
FT /note="Cytochrome b-c1 complex subunit 9"
FT /id="PRO_0000193553"
FT TOPO_DOM 2..21
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:28844695"
FT TRANSMEM 22..47
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28844695"
FT TOPO_DOM 48..63
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:28844695"
FT VAR_SEQ 51..63
FT /note="KLWKHIKHKYENK -> VRACAIPDLGPA (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041429"
FT VARIANT 47
FT /note="I -> V (in dbSNP:rs14115)"
FT /id="VAR_052444"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:5XTE"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 18..47
FT /evidence="ECO:0007829|PDB:5XTE"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:5XTE"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:5XTE"
SQ SEQUENCE 63 AA; 7308 MW; 12CCBC666F54E464 CRC64;
MAAATLTSKL YSLLFRRTST FALTIIVGVM FFERAFDQGA DAIYDHINEG KLWKHIKHKY
ENK
