ID CYB_ORYGA Reviewed; 379 AA. AC Q955G6; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 14-OCT-2015, entry version 66. 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 Oryx gazella (Gemsbok). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Hippotraginae; Oryx. OX NCBI_TaxID=9958; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11420362; DOI=10.1093/oxfordjournals.molbev.a003908; RA Matthee C.A., Davis S.K.; RT "Molecular insights into the evolution of the family Bovidae: a RT nuclear DNA perspective."; RL Mol. Biol. Evol. 18:1220-1230(2001). 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; AF249973; AAK67831.1; -; Genomic_DNA. DR ProteinModelPortal; Q955G6; -. DR SMR; Q955G6; 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 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; PF13631; Cytochrom_B_N_2; 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_0000061326. FT TRANSMEM 33 53 Helical. {ECO:0000255}. FT TRANSMEM 90 110 Helical. {ECO:0000255}. FT TRANSMEM 115 135 Helical. {ECO:0000255}. FT TRANSMEM 140 158 Helical. {ECO:0000255}. FT TRANSMEM 178 198 Helical. {ECO:0000255}. FT TRANSMEM 229 249 Helical. {ECO:0000255}. FT TRANSMEM 288 308 Helical. {ECO:0000255}. FT TRANSMEM 320 340 Helical. {ECO:0000255}. FT TRANSMEM 348 368 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; 42619 MW; E260538D927277EA CRC64; MTNIRKTHPL MKIVNNAFID LPAPSNISSW WNFGSLLGVC LILQILTGLF LAMHYTSDTT TAFSSVTHIC RDVNYGWIIR YMHANGASMF FICLFMHVGR GLYYGSYTFL ETWNIGVILL FATMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTNL VEWIWGGFSV DKATLTRFFA FHFILPFIIA ALAMVHLLFL HETGSNNPTG ITSDTDKIPF HPYYTIKDIL GALLLILALM LLVLFAPDLL GDPDNYTPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALVLSILI LVLVPTLHTS KQRSMMFRPI SQCVFWILVA DLLTLTWIGG QPVEHPYIII GQLASIMYFL LILVLMPVAS TIENNLLKW //