ID A0A3G1J753_TRIHK Unreviewed; 359 AA. AC A0A3G1J753; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 13-SEP-2023, entry version 17. DE RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531, ECO:0000256|RuleBase:RU362117}; DE Flags: Fragment; GN Name=CYTB {ECO:0000313|EMBL:ATC69235.1}; OS Tribolodon hakonensis (Big-scaled redfin). OG Mitochondrion {ECO:0000313|EMBL:ATC69235.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Leuciscidae; Pseudaspininae; Pseudaspius. OX NCBI_TaxID=3004147 {ECO:0000313|EMBL:ATC69235.1}; RN [1] {ECO:0000313|EMBL:ATC69235.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=29161943; RA Zolotova A.O., Kartavtsev Y.P.; RT "Analysis of sequence divergence in redfin (Cypriniformes, Cyprinidae, RT Tribolodon) based on mtDNA and nDNA markers with inferences in systematics RT and genetics of speciation."; RL Mitochondrial DNA A DNA Mapp Seq Anal 0:1-18(2017). 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; KY250607; ATC69235.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3G1J753; -. 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 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 PANTHER; PTHR19271; CYTOCHROME B; 1. DR PANTHER; PTHR19271:SF37; CYTOCHROME B; 1. 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 18..44 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 65..86 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 101..121 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 128..145 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 165..188 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 217..238 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 276..296 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 308..328 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 334..357 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT DOMAIN 1..197 FT /note="Cytochrome b/b6 N-terminal region profile" FT /evidence="ECO:0000259|PROSITE:PS51002" FT DOMAIN 198..359 FT /note="Cytochrome b/b6 C-terminal region profile" FT /evidence="ECO:0000259|PROSITE:PS51003" FT BINDING 85 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 170 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 184 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 189 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:ATC69235.1" FT NON_TER 359 FT /evidence="ECO:0000313|EMBL:ATC69235.1" SQ SEQUENCE 359 AA; 40046 MW; A977A250F4E5AEDD CRC64; IANHALVDLP TPSNISALWN FGSLLGLCLI TQIVTGLFLA MHYTSDISTA FSSVAHICRD VNYGWLIRSL YANGASFFFI CIYMHIARGL YYGSYLYKET WNIGVVLLLL VMATAFVGYV LPWGQMSFWG ATVITNLMSA VPYMGDTLVQ WIWGGFSVDN ATLTRFFAFH FLLPFIIAGA TILHLLFLHE TGSYNPAGLN SDADKISFHP YFSYKDLLGF VVMLLALTSL ALFSPNLLGD PDNFTPANPL VTPPHIQPEW YFLFAYAILR SIPNKLGGVL ALLFSILVLM VVPILHTSKQ RGLTFRPMTQ FLFWTLVADM IILTWIGGMP VEHPYVIIGQ IASTLYFALF LILVPLAGW //