ID Q35091_NEOSC Unreviewed; 379 AA. AC Q35091; Q35098; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-NOV-1996, sequence version 1. DT 11-DEC-2019, entry version 105. DE RecName: Full=Cytochrome b {ECO:0000256|RuleBase:RU362117}; DE Flags: Fragment; GN Name=cytb {ECO:0000313|EMBL:ADA84441.1}; GN Synonyms=CYTB {ECO:0000313|RefSeq:YP_778772.1}; OS Neomonachus schauinslandi (Hawaiian monk seal) (Monachus schauinslandi). OG Mitochondrion {ECO:0000313|EMBL:CAA51008.1, OG ECO:0000313|RefSeq:YP_778772.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Phocidae; Neomonachus. 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 fin RT whale, two species that can hybridize in nature."; RL J. Mol. Evol. 37:312-322(1993). RN [2] {ECO:0000313|EMBL:CAJ56961.1, ECO:0000313|RefSeq:YP_778772.1} 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., Petrov E.A., RA Vainola R.; RT "Pinniped phylogeny and a new hypothesis for their origin and dispersal."; RL Mol. Phylogenet. Evol. 41:345-354(2006). RN [3] {ECO:0000313|RefSeq:YP_778772.1} RP NUCLEOTIDE SEQUENCE. RG NCBI Genome Project; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [4] {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 seals RT (Phocidae, Pinnipedia)."; RL J. Biogeogr. 37:814-829(2010). RN [5] {ECO:0000313|RefSeq:YP_778772.1} RP IDENTIFICATION. RG RefSeq; RL Submitted (JUN-2018) to UniProtKB. 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:0000256|RuleBase:RU362117}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|PIRSR:PIRSR038885-2, CC ECO:0000256|RuleBase:RU362117}; CC Note=Binds 2 heme groups non-covalently. CC {ECO:0000256|PIRSR:PIRSR038885-2, 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 GeneID; 4356022; -. DR CTD; 4519; -. DR OrthoDB; 1125966at2759; -. DR Proteomes; UP000248481; Genome assembly. 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:0045275; C:respiratory chain complex III; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. 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; 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|PIRSR:PIRSR038885-2, ECO:0000256|RuleBase:RU362117}; KW Iron {ECO:0000256|PIRSR:PIRSR038885-2, ECO:0000256|RuleBase:RU362117}; KW Membrane {ECO:0000256|RuleBase:RU362117}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR038885-2, KW ECO:0000256|RuleBase:RU362117}; KW Mitochondrion {ECO:0000256|RuleBase:RU362117, ECO:0000313|EMBL:CAA51008.1, KW ECO:0000313|RefSeq:YP_778772.1}; 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 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 77..98 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 113..133 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 140..158 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 178..200 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 229..246 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 288..307 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 319..338 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 350..372 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT DOMAIN 1..209 FT /note="CYTB_NTER" FT /evidence="ECO:0000259|PROSITE:PS51002" FT DOMAIN 210..379 FT /note="CYTB_CTER" FT /evidence="ECO:0000259|PROSITE:PS51003" FT METAL 83 FT /note="Iron 1 (heme b562 axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2" FT METAL 97 FT /note="Iron 2 (heme b566 axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2" FT METAL 182 FT /note="Iron 1 (heme b562 axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2" FT METAL 196 FT /note="Iron 2 (heme b566 axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2" FT BINDING 201 FT /note="Ubiquinone" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-1" FT NON_TER 379 FT /evidence="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 //