CYB_BOSIN
ID CYB_BOSIN Reviewed; 379 AA.
AC Q8HCJ4;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 90.
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 Bos indicus (Zebu).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9915;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate E1, Isolate E4, and Isolate Elisabeth;
RX PubMed=12399392; DOI=10.1093/genetics/162.2.823;
RA Steinborn R., Schinogl P., Wells D.N., Bergthaler A., Mueller M., Brem G.;
RT "Coexistence of Bos taurus and B. indicus mitochondrial DNAs in nuclear
RT transfer-derived somatic cattle clones.";
RL Genetics 162:823-829(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate Ongole ON2270; TISSUE=Blood;
RA Xuebin Q., Jianlin H., Hanotte O., Rege J.E.O.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15522811; DOI=10.1016/j.ympev.2004.08.009;
RA Hassanin A., Ropiquet A.;
RT "Molecular phylogeny of the tribe Bovini (Bovidae, Bovinae) and the
RT taxonomic status of the Kouprey, Bos sauveli Urbain 1937.";
RL Mol. Phylogenet. Evol. 33:896-907(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RA Hiendleder S., Lewalski H., Wolf E.;
RT "Complete sequence of the Bos indicus mitochondrial genome.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Miretti M.M., Pereira H.A. Jr., Greggio C., Suzuki J. Jr., Ferro J.A.,
RA Ferro M.I., Meirelles F., Garcia J.M., Smith L.C.;
RT "The complete mitochondrial genome nucleotide sequence of Bos indicus.";
RL Submitted (JUN-2002) 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 11 subunits: 3 respiratory
CC subunits (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and
CC UQCRC2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7,
CC UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of
CC UQCRFS1). This cytochrome bc1 complex then forms a dimer.
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; AF419237; AAL57481.2; -; Genomic_DNA.
DR EMBL; AF531473; AAO15014.1; -; Genomic_DNA.
DR EMBL; AY689190; AAV51240.1; -; Genomic_DNA.
DR EMBL; AF492350; AAQ06592.1; -; Genomic_DNA.
DR EMBL; AY126697; AAM95742.1; -; Genomic_DNA.
DR RefSeq; YP_052709.1; NC_005971.1.
DR AlphaFoldDB; Q8HCJ4; -.
DR SMR; Q8HCJ4; -.
DR GeneID; 2885974; -.
DR KEGG; biu:2885974; -.
DR CTD; 4519; -.
DR OrthoDB; 1125966at2759; -.
DR Proteomes; UP000515132; Mitochondrion MT.
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..379
FT /note="Cytochrome b"
FT /id="PRO_0000253510"
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"
SQ SEQUENCE 379 AA; 42591 MW; 02F90B99E031E012 CRC64;
MTNIRKSHPL MKIVNNAFID LPAPSNISSW WNFGSLLGIC LILQILTGLF LAMHYTSDTT
TAFSSVTHIC RDVNYGWIIR YMHANGASMF FICLYMHVGR GLYYGSYTFL ETWNIGVILL
LTVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTNL VEWIWGGFSV DKATLTRFFA
FHFILPFIIM AIAMVHLLFL HETGSNNPTG ISSDVDKIPF HPYYTIKDIL GALLLILALM
LLVLFAPDLL GDPDNYTPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALAFSILI
LALIPLLHTS KQRSMMFRPL SQCLFWALVA DLLTLTWIGG QPVEHPYITI GQLASILYFL
LILVLMPTAG TVENKLLKW
