QCR10_HUMAN
ID QCR10_HUMAN Reviewed; 56 AA.
AC O14957; B2R542; D6W5Z4; Q9UEA3; Q9UPK4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Cytochrome b-c1 complex subunit 10;
DE AltName: Full=Complex III subunit 10;
DE AltName: Full=Complex III subunit XI;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex 6.4 kDa protein;
GN Name=UQCR11; Synonyms=UQCR;
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].
RC TISSUE=Fibroblast;
RX PubMed=9161705; DOI=10.1080/15216549700202191;
RA Islam M.M., Suzuki H., Yoneda M., Tanaka M.;
RT "Primary structure of the smallest (6.4-kDa) subunit of human and bovine
RT ubiquinol-cytochrome c reductase deduced from cDNA sequences.";
RL Biochem. Mol. Biol. Int. 41:1109-1116(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [6]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF 1-52.
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. QCR10 has a role in CIII assembly and RIP1
CC stability. {ECO:0000250|UniProtKB:P37299}.
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). {ECO:0000250|UniProtKB:P07552,
CC ECO:0000269|PubMed:28844695}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P37299}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P37299}.
CC -!- SIMILARITY: Belongs to the UQCR11/QCR10 family. {ECO:0000305}.
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DR EMBL; D55636; BAA21748.1; -; mRNA.
DR EMBL; AK312053; BAG34989.1; -; mRNA.
DR EMBL; AC005321; AAC27374.1; -; Genomic_DNA.
DR EMBL; AC005943; AAC72105.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69474.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69475.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69476.1; -; Genomic_DNA.
DR EMBL; BC000462; AAH00462.1; -; mRNA.
DR EMBL; BC003594; AAH03594.1; -; mRNA.
DR CCDS; CCDS12073.1; -.
DR RefSeq; NP_006821.1; NM_006830.3.
DR PDB; 5XTE; EM; 3.40 A; G/T=2-52.
DR PDB; 5XTH; EM; 3.90 A; AG/AT=2-52.
DR PDB; 5XTI; EM; 17.40 A; AG/AT=2-52.
DR PDBsum; 5XTE; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; O14957; -.
DR SMR; O14957; -.
DR BioGRID; 116172; 51.
DR ComplexPortal; CPX-560; Mitochondrial respiratory chain complex III.
DR IntAct; O14957; 2.
DR STRING; 9606.ENSP00000467262; -.
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; DB08453; 2-Nonyl-4-quinolinol 1-oxide.
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 BioMuta; UQCR11; -.
DR EPD; O14957; -.
DR jPOST; O14957; -.
DR MassIVE; O14957; -.
DR MaxQB; O14957; -.
DR PaxDb; O14957; -.
DR PeptideAtlas; O14957; -.
DR PRIDE; O14957; -.
DR ProteomicsDB; 48334; -.
DR TopDownProteomics; O14957; -.
DR Antibodypedia; 42255; 76 antibodies from 12 providers.
DR DNASU; 10975; -.
DR Ensembl; ENST00000585671.2; ENSP00000466420.1; ENSG00000127540.12.
DR Ensembl; ENST00000589880.1; ENSP00000467555.1; ENSG00000127540.12.
DR Ensembl; ENST00000591899.8; ENSP00000467262.1; ENSG00000127540.12.
DR GeneID; 10975; -.
DR KEGG; hsa:10975; -.
DR MANE-Select; ENST00000591899.8; ENSP00000467262.1; NM_006830.4; NP_006821.1.
DR UCSC; uc002ltm.4; human.
DR CTD; 10975; -.
DR DisGeNET; 10975; -.
DR GeneCards; UQCR11; -.
DR HGNC; HGNC:30862; UQCR11.
DR HPA; ENSG00000127540; Tissue enhanced (skeletal).
DR MIM; 609711; gene.
DR neXtProt; NX_O14957; -.
DR OpenTargets; ENSG00000127540; -.
DR PharmGKB; PA165394505; -.
DR VEuPathDB; HostDB:ENSG00000127540; -.
DR eggNOG; ENOG502S9FZ; Eukaryota.
DR GeneTree; ENSGT00390000018299; -.
DR HOGENOM; CLU_211742_0_0_1; -.
DR InParanoid; O14957; -.
DR OMA; ASMWGAV; -.
DR OrthoDB; 1621371at2759; -.
DR PhylomeDB; O14957; -.
DR TreeFam; TF105034; -.
DR BioCyc; MetaCyc:HS05111-MON; -.
DR PathwayCommons; O14957; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR SignaLink; O14957; -.
DR SIGNOR; O14957; -.
DR BioGRID-ORCS; 10975; 71 hits in 1070 CRISPR screens.
DR ChiTaRS; UQCR11; human.
DR GenomeRNAi; 10975; -.
DR Pharos; O14957; Tbio.
DR PRO; PR:O14957; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O14957; protein.
DR Bgee; ENSG00000127540; Expressed in apex of heart and 146 other tissues.
DR Genevisible; O14957; 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:0009055; F:electron transfer activity; TAS:UniProtKB.
DR GO; GO:0045333; P:cellular respiration; IC:ComplexPortal.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IC:ComplexPortal.
DR InterPro; IPR029027; Single_a-helix_sf.
DR InterPro; IPR015089; UQCR.
DR PANTHER; PTHR15420; PTHR15420; 1.
DR Pfam; PF08997; UCR_6-4kD; 1.
DR SUPFAM; SSF81518; SSF81518; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..56
FT /note="Cytochrome b-c1 complex subunit 10"
FT /id="PRO_0000193560"
FT TOPO_DOM 1..12
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:28844695"
FT TRANSMEM 13..35
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28844695"
FT TOPO_DOM 36..56
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:28844695"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 8..35
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:5XTE"
SQ SEQUENCE 56 AA; 6570 MW; 0AE1CB90A205112C CRC64;
MVTRFLGPRY RELVKNWVPT AYTWGAVGAV GLVWATDWRL ILDWVPYING KFKKDN
