CYB_UROBI
ID CYB_UROBI Reviewed; 379 AA.
AC Q36201; Q6Y8K0; Q6Y8K3; Q6Y8K5; Q6Y8L0; Q6Y8M3; Q6Y8M5; Q6Y8N0; Q6Y8N6;
AC Q6Y8P2; Q6Y8Q2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 98.
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 Uroderma bilobatum (Tent-making bat).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC Stenodermatinae; Uroderma.
OX NCBI_TaxID=27663;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate MVZ 168867, Isolate MVZ 192681, Isolate ROM 104264,
RC Isolate ROM 104368, Isolate ROM 105930, Isolate TK 104603,
RC Isolate TK 104630, Isolate TK 14522, Isolate TK 17624, Isolate TK 22594,
RC Isolate TK 34552, Isolate TK 34555, Isolate TK 34560, Isolate TK 34567,
RC Isolate TK 34836, Isolate TK 34842, Isolate TK 34914, Isolate TK 34963,
RC Isolate TK 34964, Isolate TK 40011, Isolate TK 40043, Isolate TK 40045,
RC Isolate TK 40082, Isolate TK 40084, Isolate TK 40095, Isolate TK 40099,
RC Isolate TK 40107, Isolate TK 40111, Isolate TK 40114, Isolate TK 40139,
RC Isolate TK 40140, Isolate TK 40314, Isolate TK 40318, Isolate TK 40398,
RC Isolate TK 40399, Isolate TK 40400, Isolate TK 40401, Isolate TK 40402,
RC Isolate TK 40403, Isolate TK 40404, Isolate TK 40405, Isolate TK 40406,
RC Isolate TK 40408, Isolate TK 40409, Isolate TK 40410, Isolate TK 40411,
RC Isolate TK 40412, Isolate TK 40413, and Isolate TK 40414;
RX PubMed=14629379; DOI=10.1046/j.1365-294x.2003.01959.x;
RA Hoffmann F.G., Owen J.G., Baker R.J.;
RT "mtDNA perspective of chromosomal diversification and hybridization in
RT Peters' tent-making bat (Uroderma bilobatum: Phyllostomidae).";
RL Mol. Ecol. 12:2981-2993(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-134.
RC STRAIN=Isolate TK 25256; TISSUE=Muscle;
RX PubMed=8412654; DOI=10.1093/oxfordjournals.molbev.a040060;
RA den Bussche R.A., Baker R.J., Wichman H.A., Hamilton M.J.;
RT "Molecular phylogenetics of Stenodermatini bat genera: congruence of data
RT from nuclear and mitochondrial DNA.";
RL Mol. Biol. Evol. 10:944-959(1993).
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; AY169900; AAO41776.1; -; Genomic_DNA.
DR EMBL; AY169901; AAO41777.1; -; Genomic_DNA.
DR EMBL; AY169902; AAO41778.1; -; Genomic_DNA.
DR EMBL; AY169906; AAO41782.1; -; Genomic_DNA.
DR EMBL; AY169908; AAO41784.1; -; Genomic_DNA.
DR EMBL; AY169909; AAO41785.1; -; Genomic_DNA.
DR EMBL; AY169911; AAO41787.1; -; Genomic_DNA.
DR EMBL; AY169912; AAO41788.1; -; Genomic_DNA.
DR EMBL; AY169913; AAO41789.1; -; Genomic_DNA.
DR EMBL; AY169916; AAO41792.1; -; Genomic_DNA.
DR EMBL; AY169917; AAO41793.1; -; Genomic_DNA.
DR EMBL; AY169918; AAO41794.1; -; Genomic_DNA.
DR EMBL; AY169919; AAO41795.1; -; Genomic_DNA.
DR EMBL; AY169920; AAO41796.1; -; Genomic_DNA.
DR EMBL; AY169921; AAO41797.1; -; Genomic_DNA.
DR EMBL; AY169922; AAO41798.1; -; Genomic_DNA.
DR EMBL; AY169923; AAO41799.1; -; Genomic_DNA.
DR EMBL; AY169924; AAO41800.1; -; Genomic_DNA.
DR EMBL; AY169925; AAO41801.1; -; Genomic_DNA.
DR EMBL; AY169926; AAO41802.1; -; Genomic_DNA.
DR EMBL; AY169927; AAO41803.1; -; Genomic_DNA.
DR EMBL; AY169928; AAO41804.1; -; Genomic_DNA.
DR EMBL; AY169929; AAO41805.1; -; Genomic_DNA.
DR EMBL; AY169930; AAO41806.1; -; Genomic_DNA.
DR EMBL; AY169931; AAO41807.1; -; Genomic_DNA.
DR EMBL; AY169932; AAO41808.1; -; Genomic_DNA.
DR EMBL; AY169933; AAO41809.1; -; Genomic_DNA.
DR EMBL; AY169934; AAO41810.1; -; Genomic_DNA.
DR EMBL; AY169935; AAO41811.1; -; Genomic_DNA.
DR EMBL; AY169936; AAO41812.1; -; Genomic_DNA.
DR EMBL; AY169937; AAO41813.1; -; Genomic_DNA.
DR EMBL; AY169938; AAO41814.1; -; Genomic_DNA.
DR EMBL; AY169939; AAO41815.1; -; Genomic_DNA.
DR EMBL; AY169940; AAO41816.1; -; Genomic_DNA.
DR EMBL; AY169941; AAO41817.1; -; Genomic_DNA.
DR EMBL; AY169942; AAO41818.1; -; Genomic_DNA.
DR EMBL; AY169943; AAO41819.1; -; Genomic_DNA.
DR EMBL; AY169944; AAO41820.1; -; Genomic_DNA.
DR EMBL; AY169945; AAO41821.1; -; Genomic_DNA.
DR EMBL; AY169946; AAO41822.1; -; Genomic_DNA.
DR EMBL; AY169947; AAO41823.1; -; Genomic_DNA.
DR EMBL; AY169948; AAO41824.1; -; Genomic_DNA.
DR EMBL; AY169949; AAO41825.1; -; Genomic_DNA.
DR EMBL; AY169950; AAO41826.1; -; Genomic_DNA.
DR EMBL; AY169951; AAO41827.1; -; Genomic_DNA.
DR EMBL; AY169952; AAO41828.1; -; Genomic_DNA.
DR EMBL; AY169953; AAO41829.1; -; Genomic_DNA.
DR EMBL; AY169954; AAO41830.1; -; Genomic_DNA.
DR EMBL; AY169955; AAO41831.1; -; Genomic_DNA.
DR EMBL; L19519; AAA32135.1; -; Genomic_DNA.
DR AlphaFoldDB; Q36201; -.
DR SMR; Q36201; -.
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..379
FT /note="Cytochrome b"
FT /id="PRO_0000061698"
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 15
FT /note="N -> T (in strain: Isolate TK 34552 and Isolate TK
FT 34560)"
FT VARIANT 152
FT /note="A -> G (in strain: Isolate TK 40095, Isolate TK
FT 40403 and Isolate TK 40411)"
FT VARIANT 161
FT /note="V -> G (in strain: Isolate TK 40114 and Isolate TK
FT 40403)"
FT VARIANT 171
FT /note="D -> H (in strain: Isolate TK 40043 and Isolate TK
FT 40140)"
FT VARIANT 190
FT /note="T -> A (in strain: Isolate MVZ 168867, Isolate MVZ
FT 192681, Isolate ROM 104264, Isolate ROM 104368, Isolate ROM
FT 105930, Isolate TK 14522, Isolate TK 17624, Isolate TK
FT 34552, Isolate TK 34555, Isolate TK 34560, Isolate TK
FT 34836, Isolate TK 34842, Isolate TK 34963, Isolate TK
FT 40043, Isolate TK 40082, Isolate TK 40084, Isolate TK
FT 40095, Isolate TK 40099, Isolate TK 40107, Isolate TK
FT 40111, Isolate TK 40114, Isolate TK 40139, Isolate TK
FT 40314, Isolate TK 40318, Isolate TK 40398, Isolate TK
FT 40399, Isolate TK 40401, Isolate TK 40402, Isolate TK
FT 40403, Isolate TK 40406, Isolate TK 40408, Isolate TK
FT 40409, Isolate TK 40410, Isolate TK 40411, Isolate TK
FT 40414, Isolate TK 104603 and Isolate TK 104630)"
FT VARIANT 220
FT /note="F -> I (in strain: Isolate TK 40140)"
FT VARIANT 274
FT /note="F -> L (in strain: Isolate ROM 104264)"
FT VARIANT 333
FT /note="F -> L (in strain: Isolate TK 40403)"
FT VARIANT 356
FT /note="V -> A (in strain: Isolate TK 40314 and Isolate TK
FT 40318)"
FT CONFLICT 5
FT /note="R -> L (in Ref. 2; AAA32135)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="S -> W (in Ref. 2; AAA32135)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 42605 MW; 9EF60C983F6A0949 CRC64;
MTNIRKTHPL LKIINSSFVD LPAPSSLSSW WNFGSLLGVC LGVQILTGLF LAMHYTSDTA
TAFNSVTHIC RDVNYGWLLR YLHANGASMF FICLYLHVGR GLYYGSYTYS ETWNIGILLL
FAVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTDL VQWIWGGFSV DKATLTRFFA
FHFLLPFIVT ALVMVHLLFL HETGSNNPTG IPSDSDMIPF HPYYTIKDIL GFLIMLTALS
SLVLFSPDLL GDPDNYIPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALVMSILI
LAIVPILHVS KQRSMMFRPL SQCLFWLLVA VLFTLTWIGG QPVEHPYIII GQTASVLYFL
IILILMPAIS LTENYLLKW
