ID Q35091_MONSC Unreviewed; 379 AA. AC Q35091; Q35098; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 87. DE RecName: Full=Cytochrome b {ECO:0000256|RuleBase:RU362117}; DE Flags: Fragment; GN Name=cytb {ECO:0000313|EMBL:ADA84441.1}; OS Monachus schauinslandi (Hawaiian monk seal). OG Mitochondrion {ECO:0000313|EMBL:CAA51008.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Phocidae; OC Monachus. OX NCBI_TaxID=29088 {ECO:0000313|EMBL:CAA51008.1}; RN [1] {ECO:0000313|EMBL:CAA51008.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=8308901; RA Arnason U., Gullberg A.; RT "Comparison between the complete mtDNA sequences of the blue and the RT fin whale, two species that can hybridize in nature."; RL J. Mol. Evol. 37:312-322(1993). RN [2] {ECO:0000313|EMBL:CAJ56961.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16815048; DOI=10.1016/j.ympev.2006.05.022; RA Arnason U., Gullberg A., Janke A., Kullberg M., Lehman N., RA Petrov E.A., Vainola R.; RT "Pinniped phylogeny and a new hypothesis for their origin and RT dispersal."; RL Mol. Phylogenet. Evol. 41:345-354(2006). RN [3] {ECO:0000313|EMBL:ADA84441.1} RP NUCLEOTIDE SEQUENCE. RX AGRICOLA=IND44358483; DOI=10.1111/j.1365-2699.2010.02271.x; RA Fulton T.L., Strobeck C.; RT "Multiple fossil calibrations, nuclear loci and mitochondrial genomes RT provide new insight into biogeography and divergence timing for true RT seals (Phocidae, Pinnipedia)."; RL J. Biogeogr. 37:814-829(2010). 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: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; GU174610; ADA84441.1; -; Genomic_DNA. DR EMBL; X72209; CAA51008.1; -; Genomic_DNA. DR EMBL; AM181022; CAJ56961.1; -; Genomic_DNA. DR PIR; S41834; S41834. DR RefSeq; YP_778772.1; NC_008421.1. DR ProteinModelPortal; Q35091; -. DR GeneID; 4356022; -. DR CTD; 4519; -. 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 {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:CAA51008.1}; 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 56 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 77 98 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 319 338 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 350 372 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}. FT NON_TER 379 379 {ECO:0000313|EMBL:CAA51008.1}. SQ SEQUENCE 379 AA; 42634 MW; 0476E9A314464581 CRC64; MTNIRKTHPL AKIINNSLID LPAPSNISMW WNFGSLLGIC LILQILTGLF LAMHYTSDTT TAFSSITHIC RDVNYGWIIR YMHANGASMF FICLYMHVGR GLYYGSYTFT ETWNIGIILL LTVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTDL VQWIWGGFSV DKATLTRFFA FHFIMPFMVL ALAAVHLLFL HETGSNNPSG IPSNSDKIPF HPYYTIKDIL GALLLILILM LLVLFSPDLL GDPDNYIPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALVLSILI LAIIPLLHTS KQRGMTFRPM SQCLFWLLAA DLITLTWIGG QPVEYPYTTI GQLASILYFT IPLVLMPITS IIENNILKW //