QCR1_HUMAN
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 03-AUG-2022, entry version 211.
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:7951059.
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 BRAWNIN.
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 BRAWNIN
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; Q9BRT8: CBWD1; NbExp=3; IntAct=EBI-1052596, EBI-1054417;
CC P31930; Q8TAB7: 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 -!- 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}.
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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; 190.
DR ComplexPortal; CPX-560; Mitochondrial respiratory chain complex III.
DR IntAct; P31930; 89.
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 SWISS-2DPAGE; P31930; -.
DR UCD-2DPAGE; P31930; -.
DR EPD; P31930; -.
DR jPOST; P31930; -.
DR MassIVE; P31930; -.
DR MaxQB; P31930; -.
DR PaxDb; P31930; -.
DR PeptideAtlas; P31930; -.
DR PRIDE; P31930; -.
DR ProteomicsDB; 54803; -.
DR Antibodypedia; 1257; 374 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 CTD; 7384; -.
DR DisGeNET; 7384; -.
DR GeneCards; UQCRC1; -.
DR HGNC; HGNC:12585; UQCRC1.
DR HPA; ENSG00000010256; Tissue enhanced (skeletal muscle, tongue).
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; 638125at2759; -.
DR PhylomeDB; P31930; -.
DR TreeFam; TF105032; -.
DR BioCyc; MetaCyc:HS00277-MON; -.
DR PathwayCommons; P31930; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR SignaLink; P31930; -.
DR SIGNOR; P31930; -.
DR BioGRID-ORCS; 7384; 381 hits in 1090 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 208 other tissues.
DR ExpressionAtlas; P31930; baseline and differential.
DR Genevisible; P31930; HS.
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; IC:ComplexPortal.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IC: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 InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
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
