ID QCR1_HUMAN Reviewed; 480 AA. AC P31930; B2R7R8; Q96DD2; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2006, sequence version 3. DT 27-MAR-2024, entry version 220. DE RecName: Full=Cytochrome b-c1 complex subunit 1, mitochondrial; DE AltName: Full=Complex III subunit 1; DE AltName: Full=Core protein I; DE AltName: Full=Ubiquinol-cytochrome-c reductase complex core protein 1; DE Flags: Precursor; GN Name=UQCRC1; 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], AND VARIANT SER-301. RC TISSUE=Placenta; RX PubMed=8407948; DOI=10.1016/s0021-9258(19)36900-5; RA Hoffman G.G., Lee S., Christiano A.M., Chung-Honet L.C., Cheng W., RA Katchman S., Uitto J., Greenspan D.S.; RT "Complete coding sequence, intron/exon organization, and chromosomal RT location of the gene for the core I protein of human ubiquinol-cytochrome c RT reductase."; RL J. Biol. Chem. 268:21113-21119(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Fibroblast; RX PubMed=8069229; RA Islam M.M., Tanaka M., Suzuki H., Torii K., Hattori N., Ozawa T.; RT "A complete cDNA sequence for core I protein subunit of human ubiquinol- RT cytochrome c reductase."; RL Biochem. Mol. Biol. Int. 32:797-805(1994). RN [3] RP ERRATUM OF PUBMED:8069229. RX PubMed=7951059; RA Islam M.M., Tanaka M., Suzuki H., Torii K., Hattori N., Ozawa T.; RL Biochem. Mol. Biol. Int. 33:410-410(1994). RN [4] RP ERRATUM OF PUBMED:8069229. RX PubMed=7981668; RA Islam M.M., Tanaka M., Suzuki H., Torii K., Hattori N., Ozawa T.; RL Biochem. Mol. Biol. Int. 33:815-815(1994). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Subthalamic nucleus; 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 [6] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Bone marrow; 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 [8] RP PROTEIN SEQUENCE OF 35-45. RC TISSUE=Liver; RX PubMed=8313870; DOI=10.1002/elps.11501401181; RA Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C., RA Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F.; RT "Human liver protein map: update 1993."; RL Electrophoresis 14:1216-1222(1993). RN [9] RP PROTEIN SEQUENCE OF 86-99; 214-225; 229-248; 397-415; 424-442; 448-470 AND RP 473-479, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [10] RP PROTEIN SEQUENCE OF 143-165; 181-209 AND 397-415. RC TISSUE=Adipocyte; RX PubMed=15242332; DOI=10.1042/bj20040647; RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.; RT "Vectorial proteomics reveal targeting, phosphorylation and specific RT fragmentation of polymerase I and transcript release factor (PTRF) at the RT surface of caveolae in human adipocytes."; RL Biochem. J. 383:237-248(2004). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-111, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [12] 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 [13] 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 [14] RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER SER-34, AND RP IDENTIFICATION 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 [15] RP FUNCTION. RX PubMed=29243944; DOI=10.1080/15384101.2017.1417707; RA Fernandez-Vizarra E., Zeviani M.; RT "Mitochondrial complex III Rieske Fe-S protein processing and assembly."; RL Cell Cycle 17:681-687(2018). RN [16] RP INTERACTION WITH UQCC6. RX PubMed=32161263; DOI=10.1038/s41467-020-14999-2; RA Zhang S., Reljic B., Liang C., Kerouanton B., Francisco J.C., Peh J.H., RA Mary C., Jagannathan N.S., Olexiouk V., Tang C., Fidelito G., Nama S., RA Cheng R.K., Wee C.L., Wang L.C., Duek Roggli P., Sampath P., Lane L., RA Petretto E., Sobota R.M., Jesuthasan S., Tucker-Kellogg L., Reversade B., RA Menschaert G., Sun L., Stroud D.A., Ho L.; RT "Mitochondrial peptide BRAWNIN is essential for vertebrate respiratory RT complex III assembly."; RL Nat. Commun. 11:1312-1312(2020). RN [17] RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), AND SUBUNIT. 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). RN [18] RP VARIANT SER-301. RX PubMed=10453733; DOI=10.1007/s004390050988; RA Valnot I., Kassis J., Chretien D., de Lonlay P., Parfait B., Munnich A., RA Kachaner J., Rustin P., Roetig A.; RT "A mitochondrial cytochrome b mutation but no mutations of nuclearly RT encoded subunits in ubiquinol cytochrome c reductase (complex III) RT deficiency."; RL Hum. Genet. 104:460-466(1999). RN [19] RP INVOLVEMENT IN PKNPY, VARIANTS PKNPY LEU-311 AND SER-314, FUNCTION, AND RP TISSUE SPECIFICITY. RX PubMed=33141179; DOI=10.1093/brain/awaa279; RA Lin C.H., Tsai P.I., Lin H.Y., Hattori N., Funayama M., Jeon B., Sato K., RA Abe K., Mukai Y., Takahashi Y., Li Y., Nishioka K., Yoshino H., Daida K., RA Chen M.L., Cheng J., Huang C.Y., Tzeng S.R., Wu Y.S., Lai H.J., Tsai H.H., RA Yen R.F., Lee N.C., Lo W.C., Hung Y.C., Chan C.C., Ke Y.C., Chao C.C., RA Hsieh S.T., Farrer M., Wu R.M.; RT "Mitochondrial UQCRC1 mutations cause autosomal dominant parkinsonism with RT polyneuropathy."; RL Brain 143:3352-3373(2020). 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 (By similarity). CC May be involved in the in situ processing of UQCRFS1 into the mature CC Rieske protein and its mitochondrial targeting sequence (MTS)/subunit 9 CC when incorporated into complex III (Probable). Seems to play an CC important role in the maintenance of proper mitochondrial function in CC nigral dopaminergic neurons (PubMed:33141179). CC {ECO:0000250|UniProtKB:P07256, ECO:0000250|UniProtKB:P31800, CC ECO:0000269|PubMed:33141179, ECO:0000305|PubMed:29243944}. 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 UQCC6 CC (PubMed:32161263). Interacts with STMP1 (By similarity). CC {ECO:0000250|UniProtKB:P31800, ECO:0000250|UniProtKB:Q9CZ13, CC ECO:0000269|PubMed:28844695, ECO:0000269|PubMed:32161263}. CC -!- INTERACTION: CC P31930; P52566: ARHGDIB; NbExp=3; IntAct=EBI-1052596, EBI-2806617; CC P31930; Q14457: BECN1; NbExp=3; IntAct=EBI-1052596, EBI-949378; CC P31930; Q9UFG5: C19orf25; NbExp=3; IntAct=EBI-1052596, EBI-741214; CC P31930; Q8WU43: C2orf15; NbExp=3; IntAct=EBI-1052596, EBI-12904676; CC P31930; A0A024R9H7: CCDC26; NbExp=3; IntAct=EBI-1052596, EBI-10271580; CC P31930; Q8IV13: CCNJL; NbExp=3; IntAct=EBI-1052596, EBI-21668062; CC P31930; Q9Y6G5: COMMD10; NbExp=3; IntAct=EBI-1052596, EBI-1550310; CC P31930; P26641: EEF1G; NbExp=3; IntAct=EBI-1052596, EBI-351467; CC P31930; Q9UI10: EIF2B4; NbExp=3; IntAct=EBI-1052596, EBI-2340132; CC P31930; Q06547-2: GABPB1; NbExp=3; IntAct=EBI-1052596, EBI-618189; CC P31930; Q9HC44: GPBP1L1; NbExp=3; IntAct=EBI-1052596, EBI-746674; CC P31930; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-1052596, EBI-743960; CC P31930; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-1052596, EBI-11985629; CC P31930; Q8N108-16: MIER1; NbExp=3; IntAct=EBI-1052596, EBI-25830642; CC P31930; C9J082: NPHP1; NbExp=3; IntAct=EBI-1052596, EBI-25830675; CC P31930; Q9UHV9: PFDN2; NbExp=3; IntAct=EBI-1052596, EBI-359873; CC P31930; Q00169: PITPNA; NbExp=3; IntAct=EBI-1052596, EBI-1042490; CC P31930; O14744: PRMT5; NbExp=3; IntAct=EBI-1052596, EBI-351098; CC P31930; O95416: SOX14; NbExp=3; IntAct=EBI-1052596, EBI-9087806; CC P31930; Q9BUA3: SPINDOC; NbExp=3; IntAct=EBI-1052596, EBI-1773488; CC P31930; O43704: SULT1B1; NbExp=3; IntAct=EBI-1052596, EBI-10179062; CC P31930; O95947: TBX6; NbExp=3; IntAct=EBI-1052596, EBI-2824328; CC P31930; Q8WTV1: THAP3; NbExp=3; IntAct=EBI-1052596, EBI-17438286; CC P31930; Q9BZM4: ULBP3; NbExp=3; IntAct=EBI-1052596, EBI-1032551; CC P31930; Q6ZMY6-2: WDR88; NbExp=3; IntAct=EBI-1052596, EBI-25857007; CC P31930; Q9UNY5: ZNF232; NbExp=3; IntAct=EBI-1052596, EBI-749023; CC P31930; Q96MN9-2: ZNF488; NbExp=3; IntAct=EBI-1052596, EBI-25831733; CC P31930; Q8N8E2: ZNF513; NbExp=3; IntAct=EBI-1052596, EBI-10279993; CC P31930; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-1052596, EBI-745520; CC P31930; Q9BRT8: ZNG1A; NbExp=3; IntAct=EBI-1052596, EBI-1054417; 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 -!- TISSUE SPECIFICITY: Expressed in brain, including substantia nigra, CC striatum, cortex and cerebellum, and in spinal cord, heart, kidney, CC liver and muscle. {ECO:0000269|PubMed:33141179}. CC -!- DISEASE: Parkinsonism with polyneuropathy (PKNPY) [MIM:619279]: An CC autosomal dominant disorder characterized by late-onset, levodopa- CC responsive parkinsonism with asymmetric tremor, rigidity and CC bradykinesia. Patients also manifest a sensorimotor polyneuropathy with CC variable degrees of distal legs and hands muscle atrophy and weakness, CC and absent deep tendon reflexes. {ECO:0000269|PubMed:33141179}. CC Note=The protein represented in this entry is involved in disease CC pathogenesis. CC -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC1/QCR1 subfamily. CC {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; L16842; AAA20046.1; -; mRNA. DR EMBL; D26485; BAA05495.1; -; mRNA. DR EMBL; AK313090; BAG35915.1; -; mRNA. DR EMBL; CH471055; EAW64898.1; -; Genomic_DNA. DR EMBL; BC009586; AAH09586.1; -; mRNA. DR CCDS; CCDS2774.1; -. DR PIR; A48043; A48043. DR RefSeq; NP_003356.2; NM_003365.2. DR PDB; 5XTE; EM; 3.40 A; L/Y=35-480. DR PDB; 5XTH; EM; 3.90 A; AL/AY=35-480. DR PDB; 5XTI; EM; 17.40 A; AL/AY=35-480. DR PDBsum; 5XTE; -. DR PDBsum; 5XTH; -. DR PDBsum; 5XTI; -. DR AlphaFoldDB; P31930; -. DR SMR; P31930; -. DR BioGRID; 113230; 219. DR ComplexPortal; CPX-560; Mitochondrial respiratory chain complex III. DR IntAct; P31930; 92. DR MINT; P31930; -. DR STRING; 9606.ENSP00000203407; -. 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; 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; DB04741; Myxothiazol. DR DrugBank; DB08690; Ubiquinone Q2. DR MEROPS; M16.973; -. DR MEROPS; M16.981; -. DR GlyGen; P31930; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P31930; -. DR MetOSite; P31930; -. DR PhosphoSitePlus; P31930; -. DR SwissPalm; P31930; -. DR BioMuta; UQCRC1; -. DR DMDM; 92090651; -. DR OGP; P31930; -. DR REPRODUCTION-2DPAGE; IPI00013847; -. DR EPD; P31930; -. DR jPOST; P31930; -. DR MassIVE; P31930; -. DR MaxQB; P31930; -. DR PaxDb; 9606-ENSP00000203407; -. DR PeptideAtlas; P31930; -. DR ProteomicsDB; 54803; -. DR Pumba; P31930; -. DR Antibodypedia; 1257; 406 antibodies from 29 providers. DR DNASU; 7384; -. DR Ensembl; ENST00000203407.6; ENSP00000203407.5; ENSG00000010256.11. DR GeneID; 7384; -. DR KEGG; hsa:7384; -. DR MANE-Select; ENST00000203407.6; ENSP00000203407.5; NM_003365.3; NP_003356.2. DR UCSC; uc003cub.2; human. DR AGR; HGNC:12585; -. DR CTD; 7384; -. DR DisGeNET; 7384; -. DR GeneCards; UQCRC1; -. DR HGNC; HGNC:12585; UQCRC1. DR HPA; ENSG00000010256; Tissue enhanced (skeletal muscle, tongue). DR MalaCards; UQCRC1; -. DR MIM; 191328; gene. DR MIM; 619279; phenotype. DR neXtProt; NX_P31930; -. DR OpenTargets; ENSG00000010256; -. DR PharmGKB; PA37216; -. DR VEuPathDB; HostDB:ENSG00000010256; -. DR eggNOG; KOG0960; Eukaryota. DR GeneTree; ENSGT00940000158931; -. DR HOGENOM; CLU_009902_4_0_1; -. DR InParanoid; P31930; -. DR OMA; WSNPDNV; -. DR OrthoDB; 167798at2759; -. DR PhylomeDB; P31930; -. DR TreeFam; TF105032; -. DR BioCyc; MetaCyc:HS00277-MONOMER; -. DR PathwayCommons; P31930; -. DR Reactome; R-HSA-611105; Respiratory electron transport. DR SignaLink; P31930; -. DR SIGNOR; P31930; -. DR BioGRID-ORCS; 7384; 417 hits in 1176 CRISPR screens. DR ChiTaRS; UQCRC1; human. DR GeneWiki; UQCRC1; -. DR GenomeRNAi; 7384; -. DR Pharos; P31930; Tbio. DR PRO; PR:P31930; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P31930; Protein. DR Bgee; ENSG00000010256; Expressed in apex of heart and 210 other cell types or tissues. DR ExpressionAtlas; P31930; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal. DR GO; GO:0005746; C:mitochondrial respirasome; TAS:ProtInc. DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IPI:ComplexPortal. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; TAS:ProtInc. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0009060; P:aerobic respiration; TAS:ProtInc. DR GO; GO:0045333; P:cellular respiration; NAS:ComplexPortal. DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; NAS:ComplexPortal. DR GO; GO:0006119; P:oxidative phosphorylation; TAS:ProtInc. DR GO; GO:0014823; P:response to activity; IEA:Ensembl. DR GO; GO:0043279; P:response to alkaloid; IEA:Ensembl. DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2. DR InterPro; IPR011249; Metalloenz_LuxS/M16. DR InterPro; IPR011765; Pept_M16_N. DR InterPro; IPR007863; Peptidase_M16_C. DR PANTHER; PTHR11851:SF116; CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL; 1. DR PANTHER; PTHR11851; METALLOPROTEASE; 1. DR Pfam; PF00675; Peptidase_M16; 1. DR Pfam; PF05193; Peptidase_M16_C; 1. DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2. DR SWISS-2DPAGE; P31930; -. DR UCD-2DPAGE; P31930; -. DR Genevisible; P31930; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Disease variant; KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane; KW Neuropathy; Parkinsonism; Phosphoprotein; Reference proteome; KW Respiratory chain; Transit peptide; Transport. FT TRANSIT 1..34 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:8313870, FT ECO:0007744|PubMed:25944712" FT CHAIN 35..480 FT /note="Cytochrome b-c1 complex subunit 1, mitochondrial" FT /id="PRO_0000026786" FT MOD_RES 111 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 138 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9CZ13" FT MOD_RES 163 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CZ13" FT MOD_RES 163 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CZ13" FT MOD_RES 212 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q68FY0" FT MOD_RES 248 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9CZ13" FT VARIANT 215 FT /note="D -> H (in dbSNP:rs17080284)" FT /id="VAR_034581" FT VARIANT 301 FT /note="N -> S (in dbSNP:rs144710790)" FT /evidence="ECO:0000269|PubMed:10453733, FT ECO:0000269|PubMed:8407948" FT /id="VAR_013629" FT VARIANT 311 FT /note="I -> L (in PKNPY)" FT /evidence="ECO:0000269|PubMed:33141179" FT /id="VAR_085428" FT VARIANT 314 FT /note="Y -> S (in PKNPY)" FT /evidence="ECO:0000269|PubMed:33141179" FT /id="VAR_085429" FT HELIX 38..44 FT /evidence="ECO:0007829|PDB:5XTE" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 84..86 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 89..95 FT /evidence="ECO:0007829|PDB:5XTE" FT STRAND 96..99 FT /evidence="ECO:0007829|PDB:5XTE" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 106..116 FT /evidence="ECO:0007829|PDB:5XTE" FT STRAND 121..124 FT /evidence="ECO:0007829|PDB:5XTE" FT STRAND 129..132 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 137..139 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 140..150 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 158..175 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 181..192 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 196..198 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 205..208 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 213..222 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 239..250 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 258..260 FT /evidence="ECO:0007829|PDB:5XTE" FT STRAND 285..294 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 300..311 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 327..332 FT /evidence="ECO:0007829|PDB:5XTE" FT TURN 333..336 FT /evidence="ECO:0007829|PDB:5XTE" FT STRAND 339..347 FT /evidence="ECO:0007829|PDB:5XTE" FT STRAND 349..360 FT /evidence="ECO:0007829|PDB:5XTE" FT TURN 362..364 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 365..380 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 385..401 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 406..419 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 426..434 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 438..448 FT /evidence="ECO:0007829|PDB:5XTE" FT TURN 449..451 FT /evidence="ECO:0007829|PDB:5XTE" FT STRAND 455..461 FT /evidence="ECO:0007829|PDB:5XTE" FT STRAND 463..465 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 468..472 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 473..475 FT /evidence="ECO:0007829|PDB:5XTE" SQ SEQUENCE 480 AA; 52646 MW; E76B082166CAF48F CRC64; MAASVVCRAA TAGAQVLLRA RRSPALLRTP ALRSTATFAQ ALQFVPETQV SLLDNGLRVA SEQSSQPTCT VGVWIDVGSR FETEKNNGAG YFLEHLAFKG TKNRPGSALE KEVESMGAHL NAYSTREHTA YYIKALSKDL PKAVELLGDI VQNCSLEDSQ IEKERDVILR EMQENDASMR DVVFNYLHAT AFQGTPLAQA VEGPSENVRK LSRADLTEYL STHYKAPRMV LAAAGGVEHQ QLLDLAQKHL GGIPWTYAED AVPTLTPCRF TGSEIRHRDD ALPFAHVAIA VEGPGWASPD NVALQVANAI IGHYDCTYGG GVHLSSPLAS GAVANKLCQS FQTFSICYAE TGLLGAHFVC DRMKIDDMMF VLQGQWMRLC TSATESEVAR GKNILRNALV SHLDGTTPVC EDIGRSLLTY GRRIPLAEWE SRIAEVDASV VREICSKYIY DQCPAVAGYG PIEQLPDYNR IRSGMFWLRF //