CYB_DROME
ID CYB_DROME Reviewed; 378 AA.
AC P18935;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Cytochrome b;
DE AltName: Full=Complex III subunit 3;
DE AltName: Full=Complex III subunit III;
DE AltName: Full=Cytochrome b-c1 complex subunit 3;
DE AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome b subunit;
GN Name=mt:Cyt-b; Synonyms=Cob, cytb;
OS Drosophila melanogaster (Fruit fly).
OG Mitochondrion.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bretagne;
RX PubMed=3130291; DOI=10.1093/genetics/118.4.649;
RA Garesse R.;
RT "Drosophila melanogaster mitochondrial DNA: gene organization and
RT evolutionary considerations.";
RL Genetics 118:649-663(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8825764; DOI=10.1111/j.1365-2583.1995.tb00032.x;
RA Lewis D.L., Farr C.L., Kaguni L.S.;
RT "Drosophila melanogaster mitochondrial DNA: completion of the nucleotide
RT sequence and evolutionary comparisons.";
RL Insect Mol. Biol. 4:263-278(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RA Wan K., Celniker S.;
RL Submitted (AUG-2014) 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:0000250|UniProtKB:P00157}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:P00157};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000250|UniProtKB:P00157};
CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC cytochrome c1 and the Rieske protein. {ECO:0000250|UniProtKB:P00157}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00163}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00163}.
CC -!- MISCELLANEOUS: Heme 1 (or BL or b562) is low-potential and absorbs at
CC about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs
CC at about 566 nm. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000255|PROSITE-
CC ProRule:PRU00967, ECO:0000255|PROSITE-ProRule:PRU00968}.
CC -!- CAUTION: The full-length protein contains only eight transmembrane
CC helices, not nine as predicted by bioinformatics tools.
CC {ECO:0000250|UniProtKB:P00157}.
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DR EMBL; M37275; AAA69714.1; -; Genomic_DNA.
DR EMBL; U37541; AAC47822.1; -; Genomic_DNA.
DR EMBL; KJ947872; AIC64015.1; -; Genomic_DNA.
DR PIR; S01190; S01190.
DR RefSeq; YP_009047277.1; NC_024511.2.
DR AlphaFoldDB; P18935; -.
DR SMR; P18935; -.
DR STRING; 7227.FBpp0100186; -.
DR PaxDb; P18935; -.
DR PRIDE; P18935; -.
DR EnsemblMetazoa; FBtr0433502; FBpp0390634; FBgn0013678.
DR GeneID; 19893556; -.
DR KEGG; dme:Dmel_CG34090; -.
DR CTD; 4519; -.
DR FlyBase; FBgn0013678; mt:Cyt-b.
DR VEuPathDB; VectorBase:FBgn0013678; -.
DR eggNOG; KOG4663; Eukaryota.
DR HOGENOM; CLU_031114_3_0_1; -.
DR InParanoid; P18935; -.
DR OrthoDB; 1125966at2759; -.
DR PhylomeDB; P18935; -.
DR Reactome; R-DME-611105; Respiratory electron transport.
DR BioGRID-ORCS; 19893556; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Cyt-b5-r; fly.
DR GenomeRNAi; 19893556; -.
DR PRO; PR:P18935; -.
DR Proteomes; UP000000803; Mitochondrion.
DR Bgee; FBgn0013678; Expressed in Malpighian tubule and 14 other tissues.
DR ExpressionAtlas; P18935; baseline and differential.
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-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
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; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..378
FT /note="Cytochrome b"
FT /id="PRO_0000060893"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 78..99
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT BINDING 84
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:0000250|UniProtKB:P00157"
FT BINDING 98
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:0000250|UniProtKB:P00157"
FT BINDING 183
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:0000250|UniProtKB:P00157"
FT BINDING 197
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:0000250|UniProtKB:P00157"
FT BINDING 202
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT CONFLICT 143
FT /note="G -> V (in Ref. 1; AAA69714 and 2; AAC47822)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="S -> Y (in Ref. 1; AAA69714 and 2; AAC47822)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="N -> T (in Ref. 1; AAA69714 and 2; AAC47822)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 43119 MW; 6DFC118E6C92FC88 CRC64;
MNKPLRNSHP LFKIANNALV DLPAPINISS WWNFGSLLGL CLIIQILTGL FLAMHYTADI
NLAFYSVNHI CRDVNYGWLL RTLHANGASF FFICIYLHVG RGIYYGSYKF TPTWLIGVII
LFLVMGTAFM GYVLPWGQMS FWGATVITNL LSAIPYLGMD LVQWLWGGFA VDNATLTRFF
TFHFILPFIV LAMTMIHLLF LHQTGSNNPI GLNSNIDKIP FHPYFTFKDI VGFIVMIFIL
ISLVLISPNL LGDPDNFIPA NPLVTPAHIQ PEWYFLFAYA ILRSIPNKLG GVIALVLSIA
ILMILPFYNL SKFRGIQFYP INQVMFWSML VTVILLTWIG ARPVEEPYVL IGQILTVVYF
LYYLVNPLIT KWWDNLLN
