ID A0A3G4R2E0_OCHKO Unreviewed; 379 AA. AC A0A3G4R2E0; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 08-MAY-2019, entry version 3. DE RecName: Full=Cytochrome b {ECO:0000256|RuleBase:RU362117}; GN Name=CYTB {ECO:0000313|EMBL:AYU56860.1}; OS Ochotona koslowi (Koslov's pika). OG Mitochondrion {ECO:0000313|EMBL:AYU56860.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Ochotonidae; OC Ochotona. OX NCBI_TaxID=130835 {ECO:0000313|EMBL:AYU56860.1}; RN [1] {ECO:0000313|EMBL:AYU56860.1} RP NUCLEOTIDE SEQUENCE. RA He J.Y., Ma G.Y., Xie C.H., Zhang Z.T., Su P.J.; RT "The complete mitochondrial DNA sequence of Ochotona koslowi."; RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase CC complex (complex III or cytochrome b-c1 complex) that is part of CC the mitochondrial respiratory chain. The b-c1 complex mediates CC electron transfer from ubiquinol to cytochrome c. Contributes to CC the generation of a proton gradient across the mitochondrial CC membrane that is then used for ATP synthesis. CC {ECO:0000256|RuleBase:RU362117}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|RuleBase:RU362117}; CC Note=Binds 2 heme groups non-covalently. CC {ECO:0000256|RuleBase:RU362117}; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU362117}. CC -!- SIMILARITY: Belongs to the cytochrome b family. CC {ECO:0000256|RuleBase:RU362117}. 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; MG888668; AYU56860.1; -; Genomic_DNA. DR SMR; A0A3G4R2E0; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR CDD; cd00290; cytochrome_b_C; 1. DR CDD; cd00284; Cytochrome_b_N; 1. DR Gene3D; 1.20.810.10; -; 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; 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 {ECO:0000256|RuleBase:RU362117}; KW Heme {ECO:0000256|RuleBase:RU362117}; KW Iron {ECO:0000256|RuleBase:RU362117}; KW Membrane {ECO:0000256|RuleBase:RU362117}; KW Metal-binding {ECO:0000256|RuleBase:RU362117}; KW Mitochondrion {ECO:0000256|RuleBase:RU362117, KW ECO:0000313|EMBL:AYU56860.1}; KW Respiratory chain {ECO:0000256|RuleBase:RU362117}; KW Transmembrane {ECO:0000256|RuleBase:RU362117}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362117}; KW Transport {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 30 52 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 87 107 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 113 133 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 140 158 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 178 200 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 229 246 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 288 307 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 319 340 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 346 372 Helical. {ECO:0000256|RuleBase:RU362117}. FT DOMAIN 1 209 CYTB_NTER. {ECO:0000259|PROSITE:PS51002}. FT DOMAIN 210 379 CYTB_CTER. {ECO:0000259|PROSITE:PS51003}. SQ SEQUENCE 379 AA; 42716 MW; 42268E04B8C06E10 CRC64; MTNIRKTHPL MKIVNHSFID LPAPSNISAW WNFGSLLGLC LGIQIITGLF LAMHYTSDTL TAFSSVTHIC RDVNYGWIIR YMHANGASMF FICLFLHVGR GIYYGSYTYS ETWNIGILLL FTVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTDL VQWIWGGFSV DKATLTRFFA FHFILPFVIA ALVLVHLLFL HETGSNNPTG IISDADKIPF HPYYTIKDAL GFLLLISLLL SLVLFHPDLL GDPDNYTPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALVLSIAI LAAMPFLHTS KQRSMMFRPM SQTLFWILVA DLLTLTWIGG QPVEHPFIII GQLASFLYFL LILALMPICS LIENKLLKW //