CYB_PIPPI
ID CYB_PIPPI Reviewed; 379 AA.
AC O21223; O21103; O21802; O21827; O21832; Q7YD80;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 3.
DT 03-AUG-2022, entry version 96.
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 Pipistrellus pipistrellus (Common pipistrelle).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Pipistrellus.
OX NCBI_TaxID=59474;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX DOI=10.1644/1545-1542(2004)085<0133:MSOTFB>2.0.CO;2;
RA Stadelmann B.Y., Herrera L.G., Arroyo-Cabrales J., Flores-Martinez J.J.,
RA May B.P., Ruedi M.;
RT "Molecular systematics of the fishing bat Myotis (Pizonyx) vivesi.";
RL J. Mammal. 85:133-139(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-119 AND 282-379.
RC STRAIN=Clade 1A, Clade 1B, Clade 2A, and Clade 2B;
RX PubMed=9144281; DOI=10.1038/387138b0;
RA Barratt E.M., Deaville R., Burland T.M., Bruford M.W., Jones G.,
RA Racey P.A., Wayne R.K.;
RT "DNA answers the call of pipistrelle bat species.";
RL Nature 387:138-139(1997).
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; AJ504443; CAD43201.1; -; Genomic_DNA.
DR EMBL; U95499; AAC48736.1; -; Genomic_DNA.
DR EMBL; U95500; AAC48737.1; -; Genomic_DNA.
DR EMBL; U95501; AAC48738.1; -; Genomic_DNA.
DR EMBL; U95502; AAC48739.1; -; Genomic_DNA.
DR EMBL; U95503; AAC48740.1; -; Genomic_DNA.
DR EMBL; U95504; AAC48741.1; -; Genomic_DNA.
DR EMBL; U95505; AAC48742.1; -; Genomic_DNA.
DR EMBL; U95506; AAC48743.1; -; Genomic_DNA.
DR AlphaFoldDB; O21223; -.
DR SMR; O21223; -.
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_0000061402"
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 16
FT /note="N -> S (in clade 1A and clade 1B)"
FT VARIANT 82
FT /note="L -> M (in clade 1B)"
FT VARIANT 329
FT /note="T -> A (in clade 1A and clade 1B)"
FT CONFLICT 350
FT /note="I -> V (in Ref. 1; CAD43201)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 42855 MW; 679FB8A0700B20F1 CRC64;
MTNIRKSHPL IKIINNSFID LPAPSNISAW WNFGSLLGIC LGLQILTGLF LAMHYTSDTA
TAFSSVTHIC RDVNYGWVLR YLHANGASMF FICLYLHVGR GLYYGSYLFK ETWNMGVILL
FAVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTDL VEWIWGGFSV DKATLTRFFA
FHFLLPFIIS ALVMVHLLFL HETGSNNPTG IPSNMDMIPF HPYYTIKDIL GLFMMILVLL
SLVLFSPDML GDPDNYMPAN PLSTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALVLSILI
LVIIPFLHTS KQRSMTFRPL SQCLFWLLTA DLLTLTWIGG QPVEHPYVII GQLASILYFL
IIIVIMPLTS LMENHLLKW
