CYB_MICAR
ID CYB_MICAR Reviewed; 380 AA.
AC Q36922; Q34963; Q34964; Q34965; Q34966; Q34967; Q34968; Q37039; Q85B03;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 Microtus arvalis (Common vole) (Field vole).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Arvicolinae; Microtus.
OX NCBI_TaxID=47230;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate TK 44564, Isolate TK 44566, Isolate TK 44605,
RC Isolate TK 44624, Isolate TK 44634, Isolate TK 44635, Isolate TK 44636,
RC Isolate TK 44637, Isolate TK 44638, Isolate TK 44739, Isolate TK 44741,
RC Isolate TK 44751, Isolate TK 44788, Isolate TK 44790, and Isolate TK 44828;
RC TISSUE=Liver;
RX PubMed=8614463; DOI=10.1038/380707a0;
RA Baker R.J., Van Den Bussche R.A., Wright A.J., Wiggins L.E., Hamilton M.J.,
RA Reat E.P., Smith M.H., Lomakin M.D., Chesser R.K.;
RT "High levels of genetic change in rodents of Chernobyl.";
RL Nature 380:707-708(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-134.
RC STRAIN=Isolate TK 44605, Isolate TK 44634, Isolate TK 44635,
RC Isolate TK 44636, Isolate TK 44637, Isolate TK 44638, Isolate TK 44916,
RC Isolate TK 44917, Isolate TK 44918, Isolate TK 44919, Isolate TK 44920, and
RC Isolate TK 44921; TISSUE=Liver;
RA Baker R.J., DeWoody J.A., Wright A.J., Chesser R.K.;
RT "On the utility of heteroplasmy in genotoxicity studies: an example from
RT Chernobyl.";
RL Ecotoxicology 8:301-309(1999).
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; U54479; AAA98674.1; -; Genomic_DNA.
DR EMBL; U54480; AAA98675.1; -; Genomic_DNA.
DR EMBL; U54481; AAA98676.1; -; Genomic_DNA.
DR EMBL; U54482; AAA98677.1; -; Genomic_DNA.
DR EMBL; U54483; AAA98678.1; -; Genomic_DNA.
DR EMBL; U54487; AAA98682.1; -; Genomic_DNA.
DR EMBL; U54488; AAA98683.1; -; Genomic_DNA.
DR EMBL; U54489; AAA98684.1; -; Genomic_DNA.
DR EMBL; U54490; AAA98685.1; -; Genomic_DNA.
DR EMBL; U54491; AAA98686.1; -; Genomic_DNA.
DR EMBL; U54492; AAA98687.1; -; Genomic_DNA.
DR EMBL; AF190257; AAO21480.1; -; Genomic_DNA.
DR EMBL; AF190258; AAO21481.1; -; Genomic_DNA.
DR EMBL; AF190259; AAO21482.1; -; Genomic_DNA.
DR EMBL; AF190260; AAO21483.1; -; Genomic_DNA.
DR EMBL; AF190261; AAO21484.1; -; Genomic_DNA.
DR EMBL; AF190262; AAO21485.1; -; Genomic_DNA.
DR EMBL; AF190263; AAO21486.1; -; Genomic_DNA.
DR EMBL; AF190264; AAO21487.1; -; Genomic_DNA.
DR EMBL; AF190265; AAO21488.1; -; Genomic_DNA.
DR EMBL; AF190266; AAO21489.1; -; Genomic_DNA.
DR EMBL; AF190267; AAO21490.1; -; Genomic_DNA.
DR EMBL; AF190268; AAO21491.1; -; Genomic_DNA.
DR AlphaFoldDB; Q36922; -.
DR SMR; Q36922; -.
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; Respiratory chain; Transmembrane;
KW Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..380
FT /note="Cytochrome b"
FT /id="PRO_0000061175"
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 VARIANT 71
FT /note="R -> W (in strain: Isolate TK 44564)"
FT VARIANT 72
FT /note="D -> A (in strain: Isolate TK 44624)"
FT VARIANT 102
FT /note="V -> I (in strain: Isolate TK 44739, Isolate TK
FT 44741, Isolate TK 44790 and Isolate TK 44828)"
FT VARIANT 132
FT /note="V -> A (in strain: Isolate TK 44564 and Isolate TK
FT 44624)"
FT VARIANT 133..134
FT /note="LP -> FQ (in strain: Isolate TK 44566)"
FT VARIANT 153
FT /note="I -> F (in strain: Isolate TK 44566)"
FT VARIANT 206
FT /note="N -> K (in strain: Isolate TK 44564)"
FT VARIANT 303
FT /note="F -> V (in strain: Isolate TK 44636)"
FT VARIANT 314
FT /note="A -> S (in strain: Isolate TK 44564, Isolate TK
FT 44566, Isolate TK 44624 and Isolate TK 44751)"
FT VARIANT 353
FT /note="T -> H (in strain: Isolate TK 44751)"
FT VARIANT 377
FT /note="M -> L (in strain: Isolate TK 44739, Isolate TK
FT 44741, Isolate TK 44788, Isolate TK 44790 and Isolate TK
FT 44828)"
SQ SEQUENCE 380 AA; 42829 MW; 4FFC24DD912003D2 CRC64;
MTVIRKKHPL IKIINHSFID LPAPSNISSW WNFGSLLGLC LIVQILTGLF LAMHYTSDTA
TAFSSVAHIC RDVNYGWLIR YMHANGASMF FICLFLHVGR GVYYGSYNMI ETWNMGIVLL
FAVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTTL VEWIWGGFSV DKATLTRFFA
FHFILPFIIT ALVLVHLLFL HETGSNNPTG LNSDADKIPF HPYYTVKDFL GVLILLMAFM
ILTLFFPDIL GDPDNYTPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALILSIVI
LAFMPLLHTS KQRALTFRPI TQTMYWILVA DLLVLTWIGG QPVEYPFIII GQTASIAYFA
IIVIFMPMAG MIENDIMDLD
