ID Q8HEG9_PLEPL Unreviewed; 380 AA. AC Q8HEG9; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 03-JUL-2019, entry version 75. DE RecName: Full=Cytochrome b {ECO:0000256|RuleBase:RU362117}; DE Flags: Fragment; GN Name=cytb {ECO:0000313|EMBL:AAN87027.1}; OS Pleuronectes platessa (European plaice). OG Mitochondrion {ECO:0000313|EMBL:AAN87027.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Carangaria; Pleuronectiformes; Pleuronectoidei; Pleuronectidae; OC Pleuronectes. OX NCBI_TaxID=8262 {ECO:0000313|EMBL:AAN87027.1}; RN [1] {ECO:0000313|EMBL:AAN87027.1} RP NUCLEOTIDE SEQUENCE. RA Cunha R., Castilho R.; RT "Molecular systematics of Pleuronectiformes based on mitochondrial RT DNA."; RL Submitted (OCT-2002) 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|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; AY164472; AAN87027.1; -; 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, KW ECO:0000313|EMBL:AAN87027.1}; 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 29 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 145 166 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 178 200 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 229 250 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 288 308 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 320 340 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 346 366 Helical. {ECO:0000256|RuleBase:RU362117}. FT DOMAIN 1 209 CYTB_NTER. {ECO:0000259|PROSITE:PS51002}. FT DOMAIN 210 380 CYTB_CTER. {ECO:0000259|PROSITE:PS51003}. FT METAL 83 83 Iron 1 (heme b562 axial ligand). FT {ECO:0000256|PIRSR:PIRSR038885-2}. FT METAL 97 97 Iron 2 (heme b566 axial ligand). FT {ECO:0000256|PIRSR:PIRSR038885-2}. FT METAL 182 182 Iron 1 (heme b562 axial ligand). FT {ECO:0000256|PIRSR:PIRSR038885-2}. FT METAL 196 196 Iron 2 (heme b566 axial ligand). FT {ECO:0000256|PIRSR:PIRSR038885-2}. FT BINDING 201 201 Ubiquinone. {ECO:0000256|PIRSR: FT PIRSR038885-1}. FT NON_TER 380 380 {ECO:0000313|EMBL:AAN87027.1}. SQ SEQUENCE 380 AA; 42368 MW; D0531A294EAD99CD CRC64; MASLRKSHPL LKIANDALVD LPAPSNISVW WNFGSLLGLC LVTQIATGLF LAMHYTSDIA TAFTSVAHIC RDVNYGWLIR SIHANGASFF FICIYLHIGR GLYYGSYLYK ETWTIGVVLL LLVMMTAFVG YVLPWGQMSF WGATVITNLL SAVPYVGGTL VQWIWGGFSV DNATLTRFFA FHFLFPFIIA AATVIHLLFL HETGSNNPTG LNSDSDKVPF HPYFTYKDLL GFAVLLTALA SLALFSPNLL GDPDNFTPAN PLVTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALLFSILV LMLVPFLHTS KQRSLMFRPV TQFLFWSLVA DVMILTWIGG MPVEHPFVII GQVASLIYFS LFLVLIPTAG WMENKVLGWK //