CYB_DANRE
ID CYB_DANRE Reviewed; 380 AA.
AC Q9MIX8; Q9TA52;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
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-cyb; Synonyms=cob, cytb, mtcyb;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX PubMed=11691861; DOI=10.1101/gr.156801;
RA Broughton R.E., Milam J.E., Roe B.A.;
RT "The complete sequence of the zebrafish (Danio rerio) mitochondrial genome
RT and evolutionary patterns in vertebrate mitochondrial DNA.";
RL Genome Res. 11:1958-1967(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-141.
RA Gilles A., Lecointre G.;
RT "A more accurate phylogeny of European cyprinids based on the mitochondrial
RT control region.";
RL Submitted (JUN-1999) 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 cytochrome bc1 complex contains 3 respiratory subunits
CC (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and UQCRC2) and
CC probably 6 low-molecular weight proteins.
CC {ECO:0000250|UniProtKB:P00157}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00157}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00157}.
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; AC024175; AAF74309.1; -; Genomic_DNA.
DR EMBL; AJ388456; CAB62058.1; -; Genomic_DNA.
DR RefSeq; NP_059343.1; NC_002333.2.
DR AlphaFoldDB; Q9MIX8; -.
DR SMR; Q9MIX8; -.
DR STRING; 7955.ENSDARP00000087881; -.
DR PaxDb; Q9MIX8; -.
DR Ensembl; ENSDART00000093625; ENSDARP00000087881; ENSDARG00000063924.
DR GeneID; 140512; -.
DR KEGG; dre:140512; -.
DR CTD; 4519; -.
DR ZFIN; ZDB-GENE-011205-17; mt-cyb.
DR eggNOG; KOG4663; Eukaryota.
DR GeneTree; ENSGT00390000017948; -.
DR HOGENOM; CLU_031114_3_0_1; -.
DR InParanoid; Q9MIX8; -.
DR OMA; RFFAFHF; -.
DR OrthoDB; 1125966at2759; -.
DR PhylomeDB; Q9MIX8; -.
DR TreeFam; TF353088; -.
DR Reactome; R-DRE-611105; Respiratory electron transport.
DR PRO; PR:Q9MIX8; -.
DR Proteomes; UP000000437; Mitochondrion MT.
DR Proteomes; UP000814640; Mitochondrion.
DR Bgee; ENSDARG00000063924; Expressed in mature ovarian follicle and 22 other tissues.
DR ExpressionAtlas; Q9MIX8; baseline.
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 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..380
FT /note="Cytochrome b"
FT /id="PRO_0000060693"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 77..98
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT BINDING 83
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 97
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 182
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 196
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 201
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT CONFLICT 51
FT /note="L -> W (in Ref. 2; CAB62058)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="D -> Y (in Ref. 2; CAB62058)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="F -> Y (in Ref. 2; CAB62058)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="Y -> D (in Ref. 2; CAB62058)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 42819 MW; 421E2DDD8AEAC350 CRC64;
MTSLRKTHPV LKIANDALVD LPTPLNISAW WNFGSLLGLC LITQILTGLF LAMHYTSDIS
TAFSSVVHIC RDVNFGWLIR SIHANGASFF FICLYIHIAR GLYYGSYLYN ETWNIGVVLF
LLVMMTAFVG YVLPWGQMSF WGATVITNLL SAVPYVGDTL VQWIWGGFSV DNATLTRFFA
FHFLLPFIII AMVILHLLFL HETGSNNPLG LNPNMDKIPF HPYFSNKDLL GFVIMLFSLS
LLALFSPNLL GDPENFTPAN PLVTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALLFSILV
LMVVPILHTS KQRGMAFRPV TQFLFWTLVA DMLVLTWIGG MPVEHPYIII GQMASILYFS
LFLVLFPITG ILENKALQWS
