ID A0A6F8Z2Q7_9TELE Unreviewed; 377 AA. AC A0A6F8Z2Q7; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 14-DEC-2022, entry version 10. DE RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531, ECO:0000256|RuleBase:RU362117}; DE Flags: Fragment; GN Name=CYTB {ECO:0000313|EMBL:BCD40179.1}; OS Cobitis sp. BIWAE type C. OG Mitochondrion {ECO:0000313|EMBL:BCD40179.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cobitidae; Cobitinae; Cobitis. OX NCBI_TaxID=1396432 {ECO:0000313|EMBL:BCD40179.1}; RN [1] {ECO:0000313|EMBL:BCD40179.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Caudal fin {ECO:0000313|EMBL:BCD40179.1}; RA Miuchi Y., Sekiguchi S.; RT "Gene diversity of Cobitis sp. BIWAE typeC in south Kanto region."; RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases. 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|ARBA:ARBA00002566, CC ECO:0000256|RuleBase:RU362117}. CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|RuleBase:RU362117}; CC Note=Binds 2 heme groups non-covalently. CC {ECO:0000256|RuleBase:RU362117}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|PIRSR:PIRSR038885-2}; CC Note=Binds 2 heme groups non-covalently. CC {ECO:0000256|PIRSR:PIRSR038885-2}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane CC protein {ECO:0000256|ARBA:ARBA00004448}. 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; LC535844; BCD40179.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6F8Z2Q7; -. 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:0022904; P:respiratory electron transport chain; 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; SSF81648; a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1. DR SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 1. DR PROSITE; PS51003; CYTB_CTER; 1. DR PROSITE; PS51002; CYTB_NTER; 1. PE 3: Inferred from homology; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, KW ECO:0000256|RuleBase:RU362117}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038885-2}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038885-2}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362117}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR038885-2}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, KW ECO:0000256|RuleBase:RU362117}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660, KW ECO:0000256|RuleBase:RU362117}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU362117}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU362117}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362117}; KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075}. FT TRANSMEM 24..47 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 82..102 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 108..128 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 140..161 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 173..195 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 224..245 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 283..303 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 315..335 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 341..364 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT DOMAIN 1..204 FT /note="CYTB_NTER" FT /evidence="ECO:0000259|PROSITE:PS51002" FT DOMAIN 205..375 FT /note="CYTB_CTER" FT /evidence="ECO:0000259|PROSITE:PS51003" FT BINDING 78 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="b562" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2" FT BINDING 92 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="b566" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2" FT BINDING 177 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="b562" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2" FT BINDING 191 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="b566" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2" FT BINDING 196 FT /ligand="a ubiquinone" FT /ligand_id="ChEBI:CHEBI:16389" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-1" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BCD40179.1" FT NON_TER 377 FT /evidence="ECO:0000313|EMBL:BCD40179.1" SQ SEQUENCE 377 AA; 42154 MW; D90D9D13ED1A05B1 CRC64; KTHPLFKIAN DALVDLPAPS NISVWWNFGS LLGLCLIVQI LTGLFLAMHY TSDITTAFSS VAHICRDVNY GWLIRNIHAN GASFFFICIY IHIARGLYYG SYLYKETWNI GVVLLLLVMM TAFVGYVLPW GQMSFWGATV ITNLLSAVPY VGNALVQWIW GGFSLDNATL TRFFAFHFLF PFIIAAATIL HLLFLHETGS NNPMGLNSDA DKVSFHPYFS YKDLLGFAVV LLALTSLSLF SPNLLGDPDN FTPANPLVTP PHIKPEWYFL FAYAILRSIP NKLGGVLALL FSILVLMVVP ILHTSKQRGL AFRPITQFLF WALVADMLIL TWIGGMPVEH PFIIIGQLAS VLYFTLFLVL IPLAGWLENK ALEWACP //