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 24-JAN-2024, entry version 180. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 52. 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; 9606-ENSP00000467262; -. DR PeptideAtlas; O14957; -. DR ProteomicsDB; 48334; -. DR Pumba; O14957; -. DR TopDownProteomics; O14957; -. DR Antibodypedia; 42255; 77 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 AGR; HGNC:30862; -. DR CTD; 10975; -. DR DisGeNET; 10975; -. DR GeneCards; UQCR11; -. DR HGNC; HGNC:30862; UQCR11. DR HPA; ENSG00000127540; Tissue enhanced (heart muscle, skeletal muscle). 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; LAKNWMP; -. DR OrthoDB; 5340959at2759; -. DR PhylomeDB; O14957; -. DR TreeFam; TF105034; -. DR BioCyc; MetaCyc:HS05111-MONOMER; -. DR PathwayCommons; O14957; -. DR Reactome; R-HSA-611105; Respiratory electron transport. DR SignaLink; O14957; -. DR SIGNOR; O14957; -. DR BioGRID-ORCS; 10975; 71 hits in 1151 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 148 other cell types or tissues. 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; NAS: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; NAS:ComplexPortal. DR Gene3D; 1.20.5.220; -; 1. DR InterPro; IPR029027; Single_a-helix_sf. DR InterPro; IPR015089; UQCR. DR PANTHER; PTHR15420:SF2; CYTOCHROME B-C1 COMPLEX SUBUNIT 10; 1. DR PANTHER; PTHR15420; UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 6.4 KD PROTEIN; 1. DR Pfam; PF08997; UCR_6-4kD; 1. DR SUPFAM; SSF81518; Subunit XI (6.4 kDa protein) of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1. DR Genevisible; O14957; HS. 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 //