ID A0A3G1CWY9_ARCFO Unreviewed; 379 AA. AC A0A3G1CWY9; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 11-DEC-2019, entry version 5. DE RecName: Full=Cytochrome b {ECO:0000256|RuleBase:RU362117}; GN Name=CYTB {ECO:0000313|EMBL:AMM04980.1}; OS Arctocephalus forsteri (New Zealand fur seal) (Arctocephalus australis OS forsteri). OG Mitochondrion {ECO:0000313|EMBL:AMM04980.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Otariidae; Arctocephalus. OX NCBI_TaxID=29084 {ECO:0000313|EMBL:AMM04980.1}; RN [1] {ECO:0000313|EMBL:AMM04980.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NZFS22 {ECO:0000313|EMBL:AMM04980.1}, NZFS23 RC {ECO:0000313|EMBL:AMM04993.1}, and NZFS24 RC {ECO:0000313|EMBL:AMM05006.1}; RX PubMed=27246241; RA Emami-Khoyi A., Hartley D.A., Ross J.G., Murphy E.C., Paterson A.M., RA Cruickshank R.H., Else T.A.; RT "Complete mitochondrial genome of the stoat (Mustela erminea) and New RT Zealand fur seal (Arctocephalus forsteri) and their significance for RT mammalian phylogeny."; RL Mitochondrial DNA A DNA MappSeq Anal 27:4597-4599(2016). 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; KT693354; AMM04980.1; -; Genomic_DNA. DR EMBL; KT693355; AMM04993.1; -; Genomic_DNA. DR EMBL; KT693356; AMM05006.1; -; Genomic_DNA. 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:AMM04980.1}; 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..308 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 320..340 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 346..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" SQ SEQUENCE 379 AA; 42575 MW; 417510B308CB36C6 CRC64; MTNIRKMHPL AKIINNSLID LPAPSNISAW WNFGSLLAVC LALQILTGLF LAMHYTSDTT TAFSSVTHIC RDVNYGWIIR YMHANGASMF FICLYMHVGR GLYYGSYTLM ETWNIGIILL FTIMATAFMG YVLPWGQMSF WGATVITNLL SAVPYVGTNL VEWIWGGFSV DKATLTRFFA FHFILPFVVS ALVMVHLLFL HETGSNNPSG VSSDSDKIPF HPYYTIKDIL GALLLILILM LLVMFSPDLL GDPDNYIPAN PLSTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALLLSILI LAIIPLLHTS KQRGMMFRPI SQFLFWLLVA DLLTLTWIGG QPVEHPFIAI GQLASILYFT ILLILMPIAG IIENHILKW //