ID CYB_HUMAN Reviewed; 380 AA. AC P00156; Q34786; Q8HBR6; Q8HNQ0; Q8HNQ1; Q8HNQ9; Q8HNR4; Q8HNR7; Q8W7V8; AC Q8WCV9; Q8WCY2; Q8WCY7; Q8WCY8; Q9B1A6; Q9B1B6; Q9B1B8; Q9B1D4; Q9B1X6; AC Q9B2V0; Q9B2V8; Q9B2W0; Q9B2W3; Q9B2W8; Q9B2X1; Q9B2X7; Q9B2X9; Q9B2Y3; AC Q9B2Z0; Q9B2Z4; Q9T6H6; Q9T9Y0; Q9TEH4; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 2. DT 27-MAR-2024, entry version 231. DE RecName: Full=Cytochrome b; DE AltName: Full=Complex III subunit 3; DE AltName: Full=Complex III subunit III; DE AltName: Full=Cytochrome b-c1 complex subunit 3; DE AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome b subunit; GN Name=MT-CYB; Synonyms=COB, CYTB, MTCYB; OS Homo sapiens (Human). OG Mitochondrion. 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 [LARGE SCALE GENOMIC DNA]. RC TISSUE=Placenta; RX PubMed=7219534; DOI=10.1038/290457a0; RA Anderson S., Bankier A.T., Barrell B.G., de Bruijn M.H.L., Coulson A.R., RA Drouin J., Eperon I.C., Nierlich D.P., Roe B.A., Sanger F., Schreier P.H., RA Smith A.J.H., Staden R., Young I.G.; RT "Sequence and organization of the human mitochondrial genome."; RL Nature 290:457-465(1981). RN [2] RP SEQUENCE REVISION TO 7. RX PubMed=10508508; DOI=10.1038/13779; RA Andrews R.M., Kubacka I., Chinnery P.F., Lightowlers R.N., Turnbull D.M., RA Howell N.; RT "Reanalysis and revision of the Cambridge reference sequence for human RT mitochondrial DNA."; RL Nat. Genet. 23:147-147(1999). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-7 AND HIS-255. RC TISSUE=Heart; RX PubMed=7623448; DOI=10.1007/bf00711378; RA Marin-Garcia J., Ananthakrishnan R., Gonzalvo A., Goldenthal M.J.; RT "Novel mutations in mitochondrial cytochrome b in fatal post partum RT cardiomyopathy."; RL J. Inherit. Metab. Dis. 18:77-78(1995). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-7; THR-191; ALA-194 AND RP THR-229. RC TISSUE=Placenta; RX PubMed=7530363; DOI=10.1073/pnas.92.2.532; RA Horai S., Hayasaka K., Kondo R., Tsugane K., Takahata N.; RT "Recent African origin of modern humans revealed by complete sequences of RT hominoid mitochondrial DNAs."; RL Proc. Natl. Acad. Sci. U.S.A. 92:532-536(1995). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-378, AND VARIANTS ILE-7; SER-8; RP LEU-18; VAL-39; THR-78; THR-122; ALA-123; THR-153; ALA-194; THR-229; RP ILE-236; THR-306; THR-329; VAL-334; MET-353; MET-356 AND ILE-368. RX PubMed=11130070; DOI=10.1038/35047064; RA Ingman M., Kaessmann H., Paeaebo S., Gyllensten U.; RT "Mitochondrial genome variation and the origin of modern humans."; RL Nature 408:708-713(2000). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-378, AND VARIANTS ILE-7; SER-8; RP LEU-18; THR-122; VAL-164; 189-ILE-ALA-190 DELINS VAL-THR; ALA-194; THR-229; RP ILE-236; THR-330; ALA-360 AND ILE-368. RX PubMed=11553319; DOI=10.1186/1471-2156-2-13; RA Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; RT "Major genomic mitochondrial lineages delineate early human expansions."; RL BMC Genet. 2:13-13(2001). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-378, AND VARIANTS ILE-7; THR-39; RP VAL-78; THR-191; ALA-194 AND ASP-260. RX PubMed=12022039; DOI=10.1086/341358; RA Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., RA Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., RA Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; RT "Mitochondrial genome diversity of native Americans supports a single early RT entry of founder populations into America."; RL Am. J. Hum. Genet. 71:187-192(2002). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 269-380. RC TISSUE=Lymphoblast; RX PubMed=6100559; RA Spurr N.K., Bodmer W.F.; RT "Serendipitous cloning of a mitochondrial cDNA and its polymorphism."; RL Mol. Biol. Med. 2:239-249(1984). RN [9] RP DISEASE. RX PubMed=11047755; DOI=10.1086/316900; RA Keightley J.A., Anitori R., Burton M.D., Quan F., Buist N.R.M., RA Kennaway N.G.; RT "Mitochondrial encephalomyopathy and complex III deficiency associated with RT a stop-codon mutation in the cytochrome b gene."; RL Am. J. Hum. Genet. 67:1400-1410(2000). RN [10] 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 [11] RP VARIANTS ILE-7 AND PRO-87. RX PubMed=1757091; DOI=10.1007/bf00206061; RA Marzuki S., Noer A.S., Lertrit P., Thyagarajan D., Kapsa R., RA Utthanaphol P., Byrne E.; RT "Normal variants of human mitochondrial DNA and translation products: the RT building of a reference data base."; RL Hum. Genet. 88:139-145(1991). RN [12] RP VARIANTS LHON ASN-171 AND MET-356. RX PubMed=1732158; DOI=10.1093/genetics/130.1.163; RA Brown M.D., Voljavec A.S., Lott M.T., Torroni A., Yang C.C., Wallace D.C.; RT "Mitochondrial DNA complex I and III mutations associated with Leber's RT hereditary optic neuropathy."; RL Genetics 130:163-173(1992). RN [13] RP VARIANT EXERCISE INTOLERANCE ASP-290. RX PubMed=8910895; DOI=10.1006/mcpr.1996.0053; RA Dumoulin R., Sagnol I., Ferlin T., Bozon D., Stepien G., Mousson B.; RT "A novel gly290asp mitochondrial cytochrome b mutation linked to a complex RT III deficiency in progressive exercise intolerance."; RL Mol. Cell. Probes 10:389-391(1996). RN [14] RP VARIANT MM GLU-339. RX PubMed=9818877; DOI=10.1212/wnl.51.5.1444; RA Andreu A.L., Bruno C., Shanske S., Shtilbans A., Hirano M., Krishna S., RA Hayward L., Systrom D.S., Brown R.H. Jr., Dimauro S.; RT "Missense mutation in the mtDNA cytochrome b gene in a patient with RT myopathy."; RL Neurology 51:1444-1447(1998). RN [15] RP VARIANTS COLORECTAL CANCER HIS-80 AND LEU-276. RX PubMed=9806551; DOI=10.1038/3108; RA Polyak K., Li Y., Zhu H., Lengauer C., Willson J.K.V., Markowitz S.D., RA Trush M.A., Kinzler K.W., Vogelstein B.; RT "Somatic mutations of the mitochondrial genome in human colorectal RT tumours."; RL Nat. Genet. 20:291-293(1998). RN [16] RP VARIANT HCM GLU-166, AND VARIANTS ILE-7; SER-8; LEU-18; ALA-194; ILE-236 RP AND THR-316. 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 [17] RP VARIANTS MM SER-34 AND 251-GLY--LEU-258 DEL. RX PubMed=10502593; DOI=10.1056/nejm199909303411404; RA Andreu A.L., Hanna M.G., Reichmann H., Bruno C., Penn A.S., Tanji K., RA Pallotti F., Iwata S., Bonilla E., Lach B., Morgan-Hughes J., DiMauro S.; RT "Exercise intolerance due to mutations in the cytochrome b gene of RT mitochondrial DNA."; RL N. Engl. J. Med. 341:1037-1044(1999). RN [18] RP VARIANT CMIH ASP-251. RX PubMed=10960495; DOI=10.1203/00006450-200009000-00008; RA Andreu A.L., Checcarelli N., Iwata S., Shanske S., DiMauro S.; RT "A missense mutation in the mitochondrial cytochrome b gene in a revisited RT case with histiocytoid cardiomyopathy."; RL Pediatr. Res. 48:311-314(2000). RN [19] RP VARIANT MULTISYSTEM DISORDER CYS-278. RX PubMed=11601507; DOI=10.1002/ana.1224; RA Wibrand F., Ravn K., Schwartz M., Rosenberg T., Horn N., Vissing J.; RT "Multisystem disorder associated with a missense mutation in the RT mitochondrial cytochrome b gene."; RL Ann. Neurol. 50:540-543(2001). RN [20] RP VARIANT EXERCISE INTOLERANCE PRO-151. RX PubMed=11464242; DOI=10.1038/sj.ejhg.5200678; RA Legros F., Chatzoglou E., Frachon P., de Baulny H.O., Laforet P., RA Jardel C., Godinot C., Lombes A.; RT "Functional characterization of novel mutations in the human cytochrome b RT gene."; RL Eur. J. Hum. Genet. 9:510-518(2001). RN [21] RP VARIANT EXERCICE INTOLERANCE PRO-35. RX PubMed=11891837; DOI=10.1002/ana.10151; RA Schuelke M., Krude H., Finckh B., Mayatepek E., Janssen A., Schmelz M., RA Trefz F., Trijbels F., Smeitink J.; RT "Septo-optic dysplasia associated with a new mitochondrial cytochrome b RT mutation."; RL Ann. Neurol. 51:388-392(2002). RN [22] RP VARIANT SER-251. RX PubMed=12905068; DOI=10.1007/s00439-003-0983-8; RA Okura T., Koda M., Ando F., Niino N., Tanaka M., Shimokata H.; RT "Association of the mitochondrial DNA 15497G/A polymorphism with obesity in RT a middle-aged and elderly Japanese population."; RL Hum. Genet. 113:432-436(2003). RN [23] RP VARIANT [LARGE SCALE ANALYSIS] ILE-7, AND IDENTIFICATION BY MASS RP 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). CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase complex CC (complex III or cytochrome b-c1 complex) that is part of the CC mitochondrial respiratory chain. The b-c1 complex mediates electron CC transfer from ubiquinol to cytochrome c. Contributes to the generation CC of a proton gradient across the mitochondrial membrane that is then CC used for ATP synthesis. {ECO:0000250|UniProtKB:P00157}. CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000250|UniProtKB:P00157}; CC Note=Binds 2 heme b groups non-covalently. CC {ECO:0000250|UniProtKB:P00157}; CC -!- SUBUNIT: The cytochrome bc1 complex contains 11 subunits: 3 respiratory CC subunits (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and CC UQCRC2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, CC UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of CC UQCRFS1). This cytochrome bc1 complex then forms a dimer. CC {ECO:0000250|UniProtKB:P00157}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P00157}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P00157}. CC -!- DISEASE: Note=Defects in MT-CYB are a rare cause of mitochondrial CC dysfunction underlying different myopathies. They include mitochondrial CC encephalomyopathy, hypertrophic cardiomyopathy (HCM), and sporadic CC mitochondrial myopathy (MM). In mitochondrial myopathy, exercise CC intolerance is the predominant symptom. Additional features include CC lactic acidosis, muscle weakness and/or myoglobinuria. Defects in MTCYB CC are also found in cases of exercise intolerance accompanied by CC deafness, intellectual disability, retinitis pigmentosa, cataract, CC growth retardation, epilepsy (multisystem disorder). CC {ECO:0000269|PubMed:11047755, ECO:0000269|PubMed:11601507}. CC -!- DISEASE: Cardiomyopathy, infantile histiocytoid (CMIH) [MIM:500000]: A CC heart disease characterized by the presence of pale granular foamy CC histiocyte-like cells within the myocardium. It usually affects CC children younger than 2 years of age, with a clear predominance of CC females over males. Infants present with dysrhythmia or cardiac arrest. CC The clinical course is usually fulminant, sometimes simulating sudden CC infant death syndrome. {ECO:0000269|PubMed:10960495}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Leber hereditary optic neuropathy (LHON) [MIM:535000]: A CC maternally inherited form of Leber hereditary optic neuropathy, a CC mitochondrial disease resulting in bilateral painless loss of central CC vision due to selective degeneration of the retinal ganglion cells and CC their axons. The disorder shows incomplete penetrance and male CC predominance. Cardiac conduction defects and neurological defects have CC also been described in some LHON patients. LHON results from primary CC mitochondrial DNA mutations affecting the respiratory chain complexes. CC {ECO:0000269|PubMed:1732158}. Note=The disease is caused by variants CC affecting distinct genetic loci, including the gene represented in this CC entry. CC -!- MISCELLANEOUS: Heme 1 (or BL or b562) is low-potential and absorbs at CC about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs CC at about 566 nm. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000255|PROSITE- CC ProRule:PRU00967, ECO:0000255|PROSITE-ProRule:PRU00968}. CC -!- CAUTION: The full-length protein contains only eight transmembrane CC helices, not nine as predicted by bioinformatics tools. CC {ECO:0000250|UniProtKB:P00157}. 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; V00662; CAA24038.1; -; Genomic_DNA. DR EMBL; J01415; AAB58955.3; -; Genomic_DNA. DR EMBL; U09500; AAA19775.1; -; Genomic_DNA. DR EMBL; D38112; BAA77674.1; -; Genomic_DNA. DR EMBL; AF346963; AAK17219.1; -; Genomic_DNA. DR EMBL; AF346964; AAK17232.2; -; Genomic_DNA. DR EMBL; AF346965; AAK17245.2; -; Genomic_DNA. DR EMBL; AF346966; AAK17258.1; -; Genomic_DNA. DR EMBL; AF346967; AAK17271.2; -; Genomic_DNA. DR EMBL; AF346968; AAK17284.2; -; Genomic_DNA. DR EMBL; AF346969; AAK17297.2; -; Genomic_DNA. DR EMBL; AF346970; AAK17310.2; -; Genomic_DNA. DR EMBL; AF346971; AAK17323.2; -; Genomic_DNA. DR EMBL; AF346972; AAK17336.2; -; Genomic_DNA. DR EMBL; AF346973; AAK17349.2; -; Genomic_DNA. DR EMBL; AF346974; AAK17362.2; -; Genomic_DNA. DR EMBL; AF346975; AAK17375.2; -; Genomic_DNA. DR EMBL; AF346976; AAK17388.1; -; Genomic_DNA. DR EMBL; AF346977; AAK17401.1; -; Genomic_DNA. DR EMBL; AF346978; AAK17414.1; -; Genomic_DNA. DR EMBL; AF346979; AAK17427.1; -; Genomic_DNA. DR EMBL; AF346980; AAK17440.2; -; Genomic_DNA. DR EMBL; AF346981; AAK17453.2; -; Genomic_DNA. DR EMBL; AF346982; AAK17466.1; -; Genomic_DNA. DR EMBL; AF346983; AAK17479.1; -; Genomic_DNA. DR EMBL; AF346984; AAK17492.2; -; Genomic_DNA. DR EMBL; AF346985; AAK17505.2; -; Genomic_DNA. DR EMBL; AF346986; AAK17518.2; -; Genomic_DNA. DR EMBL; AF346987; AAK17531.2; -; Genomic_DNA. DR EMBL; AF346988; AAK17544.1; -; Genomic_DNA. DR EMBL; AF346989; AAK17557.2; -; Genomic_DNA. DR EMBL; AF346990; AAK17570.1; -; Genomic_DNA. DR EMBL; AF346991; AAK17583.2; -; Genomic_DNA. DR EMBL; AF346992; AAK17596.2; -; Genomic_DNA. DR EMBL; AF346993; AAK17609.2; -; Genomic_DNA. DR EMBL; AF346994; AAK17622.2; -; Genomic_DNA. DR EMBL; AF346995; AAK17635.2; -; Genomic_DNA. DR EMBL; AF346996; AAK17648.2; -; Genomic_DNA. DR EMBL; AF346997; AAK17661.2; -; Genomic_DNA. DR EMBL; AF346998; AAK17674.2; -; Genomic_DNA. DR EMBL; AF346999; AAK17687.2; -; Genomic_DNA. DR EMBL; AF347000; AAK17700.1; -; Genomic_DNA. DR EMBL; AF347001; AAK17713.2; -; Genomic_DNA. DR EMBL; AF347002; AAK17726.2; -; Genomic_DNA. DR EMBL; AF347003; AAK17739.2; -; Genomic_DNA. DR EMBL; AF347004; AAK17752.2; -; Genomic_DNA. DR EMBL; AF347005; AAK17765.2; -; Genomic_DNA. DR EMBL; AF347006; AAK17778.2; -; Genomic_DNA. DR EMBL; AF347007; AAK17791.2; -; Genomic_DNA. DR EMBL; AF347008; AAK17804.2; -; Genomic_DNA. DR EMBL; AF347009; AAK17817.2; -; Genomic_DNA. DR EMBL; AF347010; AAK17830.2; -; Genomic_DNA. DR EMBL; AF347011; AAK17843.2; -; Genomic_DNA. DR EMBL; AF347012; AAK17856.2; -; Genomic_DNA. DR EMBL; AF347013; AAK17869.2; -; Genomic_DNA. DR EMBL; AF347014; AAK17882.2; -; Genomic_DNA. DR EMBL; AF347015; AAK17895.2; -; Genomic_DNA. DR EMBL; AF381981; AAL54394.1; -; Genomic_DNA. DR EMBL; AF381982; AAL54409.1; -; Genomic_DNA. DR EMBL; AF381983; AAL54422.1; -; Genomic_DNA. DR EMBL; AF381984; AAL54435.1; -; Genomic_DNA. DR EMBL; AF381985; AAL54448.1; -; Genomic_DNA. DR EMBL; AF381986; AAL54461.1; -; Genomic_DNA. DR EMBL; AF381987; AAL54474.1; -; Genomic_DNA. DR EMBL; AF381988; AAL54487.1; -; Genomic_DNA. DR EMBL; AF381989; AAL54500.1; -; Genomic_DNA. DR EMBL; AF381990; AAL54513.1; -; Genomic_DNA. DR EMBL; AF381991; AAL54526.1; -; Genomic_DNA. DR EMBL; AF381992; AAL54539.1; -; Genomic_DNA. DR EMBL; AF381993; AAL54552.1; -; Genomic_DNA. DR EMBL; AF381994; AAL54565.1; -; Genomic_DNA. DR EMBL; AF381995; AAL54578.1; -; Genomic_DNA. DR EMBL; AF381996; AAL54591.1; -; Genomic_DNA. DR EMBL; AF381997; AAL54604.1; -; Genomic_DNA. DR EMBL; AF381998; AAL54617.1; -; Genomic_DNA. DR EMBL; AF381999; AAL54630.1; -; Genomic_DNA. DR EMBL; AF382000; AAL54643.1; -; Genomic_DNA. DR EMBL; AF382001; AAL54656.1; -; Genomic_DNA. DR EMBL; AF382002; AAL54669.1; -; Genomic_DNA. DR EMBL; AF382003; AAL54682.1; -; Genomic_DNA. DR EMBL; AF382004; AAL54695.1; -; Genomic_DNA. DR EMBL; AF382005; AAL54708.1; -; Genomic_DNA. DR EMBL; AF382006; AAL54721.1; -; Genomic_DNA. DR EMBL; AF382007; AAL54734.1; -; Genomic_DNA. DR EMBL; AF382008; AAL54747.1; -; Genomic_DNA. DR EMBL; AF382009; AAL54760.1; -; Genomic_DNA. DR EMBL; AF382010; AAL54773.1; -; Genomic_DNA. DR EMBL; AF382011; AAL54786.1; -; Genomic_DNA. DR EMBL; AF382012; AAL54799.1; -; Genomic_DNA. DR EMBL; AF382013; AAL54812.1; -; Genomic_DNA. DR EMBL; AF465942; AAN14559.1; -; Genomic_DNA. DR EMBL; AF465945; AAN14592.1; -; Genomic_DNA. DR EMBL; AF465946; AAN14603.1; -; Genomic_DNA. DR EMBL; AF465947; AAN14614.1; -; Genomic_DNA. DR EMBL; AF465948; AAN14625.1; -; Genomic_DNA. DR EMBL; AF465949; AAN14636.1; -; Genomic_DNA. DR EMBL; AF465953; AAN14680.1; -; Genomic_DNA. DR EMBL; AF465956; AAN14713.1; -; Genomic_DNA. DR EMBL; AF465968; AAN14845.1; -; Genomic_DNA. DR EMBL; AF465971; AAN14878.1; -; Genomic_DNA. DR EMBL; AF465972; AAN14889.1; -; Genomic_DNA. DR EMBL; AF465973; AAN14900.1; -; Genomic_DNA. DR EMBL; AF465974; AAN14911.1; -; Genomic_DNA. DR EMBL; AF465975; AAN14922.1; -; Genomic_DNA. DR EMBL; AF465977; AAN14944.1; -; Genomic_DNA. DR EMBL; M28016; AAA31851.1; -; mRNA. DR PIR; A00151; CBHU. DR RefSeq; YP_003024038.1; NC_012920.1. DR PDB; 5XTE; EM; 3.40 A; J/V=2-379. DR PDB; 5XTH; EM; 3.90 A; AJ/AV=2-379. DR PDB; 5XTI; EM; 17.40 A; AJ/AV=2-379. DR PDBsum; 5XTE; -. DR PDBsum; 5XTH; -. DR PDBsum; 5XTI; -. DR AlphaFoldDB; P00156; -. DR SMR; P00156; -. DR BioGRID; 110619; 22. DR ComplexPortal; CPX-560; Mitochondrial respiratory chain complex III. DR IntAct; P00156; 10. DR MINT; P00156; -. DR STRING; 9606.ENSP00000354554; -. DR BindingDB; P00156; -. 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 iPTMnet; P00156; -. DR PhosphoSitePlus; P00156; -. DR SwissPalm; P00156; -. DR BioMuta; MT-CYB; -. DR DMDM; 408360043; -. DR EPD; P00156; -. DR jPOST; P00156; -. DR MassIVE; P00156; -. DR PaxDb; 9606-ENSP00000354554; -. DR PeptideAtlas; P00156; -. DR ProteomicsDB; 51225; -. DR Pumba; P00156; -. DR TopDownProteomics; P00156; -. DR Antibodypedia; 35365; 240 antibodies from 28 providers. DR DNASU; 4519; -. DR Ensembl; ENST00000361789.2; ENSP00000354554.2; ENSG00000198727.2. DR GeneID; 4519; -. DR KEGG; hsa:4519; -. DR AGR; HGNC:7427; -. DR CTD; 4519; -. DR DisGeNET; 4519; -. DR GeneCards; MT-CYB; -. DR GeneReviews; MT-CYB; -. DR HGNC; HGNC:7427; MT-CYB. DR HPA; ENSG00000198727; Tissue enhanced (heart). DR MalaCards; MT-CYB; -. DR MIM; 500000; phenotype. DR MIM; 516020; gene. DR MIM; 535000; phenotype. DR neXtProt; NX_P00156; -. DR OpenTargets; ENSG00000198727; -. DR Orphanet; 137675; Histiocytoid cardiomyopathy. DR Orphanet; 1460; Isolated complex III deficiency. DR Orphanet; 104; Leber hereditary optic neuropathy. DR PharmGKB; PA31234; -. DR VEuPathDB; HostDB:ENSG00000198727; -. DR eggNOG; KOG4663; Eukaryota. DR GeneTree; ENSGT00390000017948; -. DR HOGENOM; CLU_031114_3_0_1; -. DR InParanoid; P00156; -. DR OMA; NISAWWN; -. DR PhylomeDB; P00156; -. DR TreeFam; TF353088; -. DR BioCyc; MetaCyc:HS00029-MONOMER; -. DR PathwayCommons; P00156; -. DR Reactome; R-HSA-611105; Respiratory electron transport. DR SignaLink; P00156; -. DR SIGNOR; P00156; -. DR BioGRID-ORCS; 4519; 0 hits in 2 CRISPR screens. DR ChiTaRS; CYTB; human. DR GeneWiki; MT-CYB; -. DR GenomeRNAi; 4519; -. DR Pharos; P00156; Tbio. DR PRO; PR:P00156; -. DR Proteomes; UP000005640; Mitochondrion. DR RNAct; P00156; Protein. DR Bgee; ENSG00000198727; Expressed in apex of heart and 95 other cell types or tissues. DR ExpressionAtlas; P00156; baseline and differential. 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:0005739; C:mitochondrion; HDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; NAS:UniProtKB. DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl. DR GO; GO:0045333; P:cellular respiration; NAS:ComplexPortal. DR GO; GO:0015990; P:electron transport coupled proton transport; IEA:Ensembl. DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central. DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl. DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl. DR GO; GO:0033590; P:response to cobalamin; IEA:Ensembl. DR GO; GO:0046688; P:response to copper ion; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0033762; P:response to glucagon; IEA:Ensembl. DR GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0046689; P:response to mercury ion; IEA:Ensembl. DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR CDD; cd00290; cytochrome_b_C; 1. DR CDD; cd00284; Cytochrome_b_N; 1. DR InterPro; IPR005798; Cyt_b/b6_C. DR InterPro; IPR036150; Cyt_b/b6_C_sf. DR InterPro; IPR005797; Cyt_b/b6_N. DR InterPro; IPR027387; Cytb/b6-like_sf. DR InterPro; IPR030689; Cytochrome_b. DR InterPro; IPR048260; Cytochrome_b_C_euk/bac. DR InterPro; IPR048259; Cytochrome_b_N_euk/bac. DR InterPro; IPR016174; Di-haem_cyt_TM. DR PANTHER; PTHR19271; CYTOCHROME B; 1. DR PANTHER; PTHR19271:SF16; CYTOCHROME B; 1. DR Pfam; PF00032; Cytochrom_B_C; 1. DR Pfam; PF00033; Cytochrome_B; 1. DR PIRSF; PIRSF038885; COB; 1. DR SUPFAM; SSF81648; a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1. DR SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 1. DR PROSITE; PS51003; CYTB_CTER; 1. DR PROSITE; PS51002; CYTB_NTER; 1. PE 1: Evidence at protein level; KW 3D-structure; Cardiomyopathy; Cataract; Deafness; Disease variant; KW Electron transport; Heme; Iron; Leber hereditary optic neuropathy; KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; KW Primary mitochondrial disease; Reference proteome; Respiratory chain; KW Transmembrane; Transmembrane helix; Transport; Ubiquinone. FT CHAIN 1..380 FT /note="Cytochrome b" FT /id="PRO_0000061045" FT TRANSMEM 33..53 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00157" FT TRANSMEM 77..98 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00157" FT TRANSMEM 113..133 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00157" FT TRANSMEM 178..198 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00157" FT TRANSMEM 226..246 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00157" FT TRANSMEM 288..308 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00157" FT TRANSMEM 320..340 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00157" FT TRANSMEM 347..367 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00157" FT BINDING 83 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="b562" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P00157" FT BINDING 97 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="b566" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P00157" FT BINDING 182 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="b562" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P00157" FT BINDING 196 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="b566" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P00157" FT BINDING 201 FT /ligand="a ubiquinone" FT /ligand_id="ChEBI:CHEBI:16389" FT /evidence="ECO:0000250|UniProtKB:P00157" FT VARIANT 7 FT /note="T -> I (in dbSNP:rs193302980)" FT /evidence="ECO:0000269|PubMed:10453733, FT ECO:0000269|PubMed:11130070, ECO:0000269|PubMed:11553319, FT ECO:0000269|PubMed:12022039, ECO:0000269|PubMed:1757091, FT ECO:0000269|PubMed:7530363, ECO:0000269|PubMed:7623448, FT ECO:0007744|PubMed:21269460" FT /id="VAR_008585" FT VARIANT 8 FT /note="N -> S (in dbSNP:rs28357679)" FT /evidence="ECO:0000269|PubMed:10453733, FT ECO:0000269|PubMed:11130070, ECO:0000269|PubMed:11553319" FT /id="VAR_013643" FT VARIANT 18 FT /note="F -> L (in dbSNP:rs28357681)" FT /evidence="ECO:0000269|PubMed:10453733, FT ECO:0000269|PubMed:11130070, ECO:0000269|PubMed:11553319" FT /id="VAR_013644" FT VARIANT 34 FT /note="G -> S (in mitochondrial myopathy; sporadic; FT dbSNP:rs207459998)" FT /evidence="ECO:0000269|PubMed:10502593" FT /id="VAR_013645" FT VARIANT 35 FT /note="S -> P (in exercice intolerance; with cardiomyopathy FT and septo-optic dysplasia; dbSNP:rs207460004)" FT /evidence="ECO:0000269|PubMed:11891837" FT /id="VAR_033058" FT VARIANT 39 FT /note="A -> T (in dbSNP:rs2853505)" FT /evidence="ECO:0000269|PubMed:12022039" FT /id="VAR_015571" FT VARIANT 39 FT /note="A -> V (in dbSNP:rs1603224933)" FT /evidence="ECO:0000269|PubMed:11130070" FT /id="VAR_013646" FT VARIANT 78 FT /note="I -> T (in dbSNP:rs200786872)" FT /evidence="ECO:0000269|PubMed:11130070" FT /id="VAR_013647" FT VARIANT 78 FT /note="I -> V (in dbSNP:rs199997767)" FT /evidence="ECO:0000269|PubMed:12022039" FT /id="VAR_015572" FT VARIANT 80 FT /note="R -> H (in colorectal cancer; dbSNP:rs207459995)" FT /evidence="ECO:0000269|PubMed:9806551" FT /id="VAR_008388" FT VARIANT 87 FT /note="A -> P (in dbSNP:rs1603225017)" FT /evidence="ECO:0000269|PubMed:1757091" FT /id="VAR_008586" FT VARIANT 122 FT /note="A -> T (in dbSNP:rs28357685)" FT /evidence="ECO:0000269|PubMed:11130070, FT ECO:0000269|PubMed:11553319" FT /id="VAR_013648" FT VARIANT 123 FT /note="T -> A (in dbSNP:rs1603225089)" FT /evidence="ECO:0000269|PubMed:11130070" FT /id="VAR_013649" FT VARIANT 151 FT /note="S -> P (in exercise intolerance; dbSNP:rs207460001)" FT /evidence="ECO:0000269|PubMed:11464242" FT /id="VAR_013650" FT VARIANT 153 FT /note="I -> T (in dbSNP:rs28357687)" FT /evidence="ECO:0000269|PubMed:11130070" FT /id="VAR_013651" FT VARIANT 164 FT /note="I -> V (in dbSNP:rs386829239)" FT /evidence="ECO:0000269|PubMed:11553319" FT /id="VAR_013652" FT VARIANT 166 FT /note="G -> E (in hyperthrophic cardiomyopathy; FT dbSNP:rs1603225167)" FT /evidence="ECO:0000269|PubMed:10453733" FT /id="VAR_013653" FT VARIANT 171 FT /note="D -> N (in LHON; uncertain significance; secondary FT mutation; dbSNP:rs41518645)" FT /evidence="ECO:0000269|PubMed:1732158" FT /id="VAR_002197" FT VARIANT 189..190 FT /note="IA -> VT" FT /evidence="ECO:0000269|PubMed:11553319" FT /id="VAR_013654" FT VARIANT 191 FT /note="A -> T (in dbSNP:rs2853507)" FT /evidence="ECO:0000269|PubMed:12022039, FT ECO:0000269|PubMed:7530363" FT /id="VAR_011339" FT VARIANT 194 FT /note="T -> A (in dbSNP:rs2853508)" FT /evidence="ECO:0000269|PubMed:10453733, FT ECO:0000269|PubMed:11130070, ECO:0000269|PubMed:11553319, FT ECO:0000269|PubMed:12022039, ECO:0000269|PubMed:7530363" FT /id="VAR_011340" FT VARIANT 229 FT /note="A -> T (in dbSNP:rs193302993)" FT /evidence="ECO:0000269|PubMed:11130070, FT ECO:0000269|PubMed:11553319, ECO:0000269|PubMed:7530363" FT /id="VAR_011341" FT VARIANT 236 FT /note="L -> I (in dbSNP:rs193302994)" FT /evidence="ECO:0000269|PubMed:10453733, FT ECO:0000269|PubMed:11130070, ECO:0000269|PubMed:11553319" FT /id="VAR_013655" FT VARIANT 251..258 FT /note="Missing (in mitochondrial myopathy; sporadic)" FT /evidence="ECO:0000269|PubMed:10502593" FT /id="VAR_013657" FT VARIANT 251 FT /note="G -> D (in CMIH; dbSNP:rs207460003)" FT /evidence="ECO:0000269|PubMed:10960495" FT /id="VAR_013656" FT VARIANT 251 FT /note="G -> S (risk factor for obesity; dbSNP:rs199951903)" FT /evidence="ECO:0000269|PubMed:12905068" FT /id="VAR_033059" FT VARIANT 255 FT /note="N -> H (found in a patient with fatal post-partum FT cardiomyopathy; uncertain significance)" FT /evidence="ECO:0000269|PubMed:7623448" FT /id="VAR_013658" FT VARIANT 260 FT /note="N -> D (in dbSNP:rs1603225331)" FT /evidence="ECO:0000269|PubMed:12022039" FT /id="VAR_015573" FT VARIANT 276 FT /note="F -> L (in colorectal cancer; dbSNP:rs207459996)" FT /evidence="ECO:0000269|PubMed:9806551" FT /id="VAR_008389" FT VARIANT 278 FT /note="Y -> C (in multisystem disorder; dbSNP:rs207460002)" FT /evidence="ECO:0000269|PubMed:11601507" FT /id="VAR_013659" FT VARIANT 290 FT /note="G -> D (in exercise intolerance; dbSNP:rs207459997)" FT /evidence="ECO:0000269|PubMed:8910895" FT /id="VAR_013660" FT VARIANT 306 FT /note="I -> T (in dbSNP:rs369851331)" FT /evidence="ECO:0000269|PubMed:11130070" FT /id="VAR_013661" FT VARIANT 316 FT /note="M -> T (in dbSNP:rs200975632)" FT /evidence="ECO:0000269|PubMed:10453733" FT /id="VAR_013662" FT VARIANT 329 FT /note="A -> T (in dbSNP:rs1556424652)" FT /evidence="ECO:0000269|PubMed:11130070" FT /id="VAR_013663" FT VARIANT 330 FT /note="A -> T (in dbSNP:rs386829259)" FT /evidence="ECO:0000269|PubMed:11553319" FT /id="VAR_013664" FT VARIANT 334 FT /note="I -> V (in dbSNP:rs386829260)" FT /evidence="ECO:0000269|PubMed:11130070" FT /id="VAR_013665" FT VARIANT 339 FT /note="G -> E (in mitochondrial myopathy)" FT /evidence="ECO:0000269|PubMed:9818877" FT /id="VAR_002198" FT VARIANT 353 FT /note="V -> M (in dbSNP:rs1603225508)" FT /evidence="ECO:0000269|PubMed:11130070" FT /id="VAR_013666" FT VARIANT 356 FT /note="V -> M (in LHON; secondary mutation; does not seem FT to directly cause the disease; dbSNP:rs200336777)" FT /evidence="ECO:0000269|PubMed:11130070, FT ECO:0000269|PubMed:1732158" FT /id="VAR_002199" FT VARIANT 360 FT /note="T -> A (in dbSNP:rs28357376)" FT /evidence="ECO:0000269|PubMed:11553319" FT /id="VAR_013667" FT VARIANT 368 FT /note="T -> I (in dbSNP:rs202225494)" FT /evidence="ECO:0000269|PubMed:11130070, FT ECO:0000269|PubMed:11553319" FT /id="VAR_013668" FT HELIX 4..7 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 9..17 FT /evidence="ECO:0007829|PDB:5XTE" FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 29..31 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 32..52 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 61..70 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 76..103 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 106..108 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 110..131 FT /evidence="ECO:0007829|PDB:5XTE" FT TURN 132..134 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 137..148 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 149..152 FT /evidence="ECO:0007829|PDB:5XTE" FT TURN 154..156 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 157..165 FT /evidence="ECO:0007829|PDB:5XTE" FT STRAND 167..170 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 172..200 FT /evidence="ECO:0007829|PDB:5XTE" FT TURN 201..203 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 214..216 FT /evidence="ECO:0007829|PDB:5XTE" FT STRAND 217..219 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 220..244 FT /evidence="ECO:0007829|PDB:5XTE" FT STRAND 249..251 FT /evidence="ECO:0007829|PDB:5XTE" FT STRAND 255..258 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 272..283 FT /evidence="ECO:0007829|PDB:5XTE" FT STRAND 284..286 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 289..303 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 304..307 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 315..317 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 319..339 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 345..363 FT /evidence="ECO:0007829|PDB:5XTE" FT HELIX 365..376 FT /evidence="ECO:0007829|PDB:5XTE" SQ SEQUENCE 380 AA; 42718 MW; 600E520C262E5498 CRC64; MTPMRKTNPL MKLINHSFID LPTPSNISAW WNFGSLLGAC LILQITTGLF LAMHYSPDAS TAFSSIAHIT RDVNYGWIIR YLHANGASMF FICLFLHIGR GLYYGSFLYS ETWNIGIILL LATMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTDL VQWIWGGYSV DSPTLTRFFT FHFILPFIIA ALATLHLLFL HETGSNNPLG ITSHSDKITF HPYYTIKDAL GLLLFLLSLM TLTLFSPDLL GDPDNYTLAN PLNTPPHIKP EWYFLFAYTI LRSVPNKLGG VLALLLSILI LAMIPILHMS KQQSMMFRPL SQSLYWLLAA DLLILTWIGG QPVSYPFTII GQVASVLYFT TILILMPTIS LIENKMLKWA //