ID CYB_GENJO Reviewed; 379 AA. AC Q6XBW5; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 07-SEP-2016, entry version 56. 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 Genetta johnstoni (Johnston's genet). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Viverridae; OC Viverrinae; Genetta. OX NCBI_TaxID=205594; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Gaubert P., Fernandes C.A., Bruford M.W., Veron G.; RT "Genets (Carnivora, Viverridae) in Africa: an evolutionary synthesis RT based on cytochrome b sequences and morphological characters."; RL Biol. J. Linn. Soc. Lond. 81:589-610(2004). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Gaubert P., Tranier M., Delmas A.-S., Colyn M., Veron G.; RT "First molecular evidence for reassessing phylogenetic affinities RT between genets (Genetta) and the enigmatic genet-like taxa RT Osbornictis, Poiana and Prionodon (Carnivora, Viverridae)."; RL Zool. Scr. 33:117-129(2004). CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase CC complex (complex III or cytochrome b-c1 complex), which is a CC respiratory chain that generates an electrochemical potential CC coupled to ATP synthesis. {ECO:0000250}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; CC Note=Binds 2 heme groups non-covalently. {ECO:0000250}; CC -!- SUBUNIT: The bc1 complex contains 11 subunits: 3 respiratory CC subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core CC proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight CC proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, CC UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; CC Multi-pass membrane protein {ECO:0000250}. CC -!- MISCELLANEOUS: Heme 1 (or BL or b562) is low-potential and absorbs CC at about 562 nm, and heme 2 (or BH or b566) is high-potential and CC absorbs at about 566 nm. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the cytochrome b family. CC {ECO:0000255|PROSITE-ProRule:PRU00967, ECO:0000255|PROSITE- CC ProRule:PRU00968}. 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; AY241892; AAP73012.1; -; Genomic_DNA. DR EMBL; AF511051; AAQ08027.1; -; Genomic_DNA. DR ProteinModelPortal; Q6XBW5; -. DR SMR; Q6XBW5; 1-379. DR HOVERGEN; HBG017694; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045275; C:respiratory chain complex III; IEA:InterPro. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro. DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:InterPro. DR CDD; cd00284; Cytochrome_b_N; 1. DR Gene3D; 1.20.810.10; -; 1. DR InterPro; IPR005798; Cyt_b/b6_C. DR InterPro; IPR005797; Cyt_b/b6_N. DR InterPro; IPR027387; Cytb/b6-like. DR InterPro; IPR030689; Cytochrome_b. DR InterPro; IPR016174; Di-haem_cyt_TM. DR Pfam; PF00032; Cytochrom_B_C; 1. DR Pfam; PF00033; Cytochrome_B; 1. DR PIRSF; PIRSF038885; COB; 1. DR SUPFAM; SSF81342; SSF81342; 1. DR SUPFAM; SSF81648; SSF81648; 1. DR PROSITE; PS51003; CYTB_CTER; 1. DR PROSITE; PS51002; CYTB_NTER; 1. PE 3: Inferred from homology; KW Electron transport; Heme; Iron; Membrane; Metal-binding; KW Mitochondrion; Mitochondrion inner membrane; Respiratory chain; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 379 Cytochrome b. FT /FTId=PRO_0000254693. FT TRANSMEM 33 53 Helical. {ECO:0000255}. FT TRANSMEM 76 96 Helical. {ECO:0000255}. FT TRANSMEM 115 135 Helical. {ECO:0000255}. FT TRANSMEM 150 170 Helical. {ECO:0000255}. FT TRANSMEM 179 199 Helical. {ECO:0000255}. FT TRANSMEM 229 249 Helical. {ECO:0000255}. FT TRANSMEM 288 308 Helical. {ECO:0000255}. FT TRANSMEM 323 343 Helical. {ECO:0000255}. FT TRANSMEM 346 366 Helical. {ECO:0000255}. FT METAL 83 83 Iron 1 (heme b562 axial ligand). FT METAL 97 97 Iron 2 (heme b566 axial ligand). FT METAL 182 182 Iron 1 (heme b562 axial ligand). FT METAL 196 196 Iron 2 (heme b566 axial ligand). SQ SEQUENCE 379 AA; 42713 MW; E836C5FE03D94932 CRC64; MTDIRKSHPL AKIINESFID LPAPSNISAW WNFGSLLGVC LIIQILTGLF LAMHYTSDTM TAFSSVTHIC RDVNYGWIIR YMHANGASMF FICLFMHAGR GVYYGSYTFT ETWNIGILLM FTVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTNL VEWIWGGFSV DKATLTRLFA FHFILPFIIS ALAAVHLLFL HETGSNNPSG MMSDSDKIPF HPYYTIKDIL GILLLILVLM LLVLFSPDLL GDPDNYIPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALVLSILI LAIIPFLHTS KQRSMMFRPL SQCLFWLLVA DLLTLTWIGG QPVEHPFITI GQLASILYFS IFLILMPVSG IIENRLLKW //