CYB_RHIFE
ID CYB_RHIFE Reviewed; 379 AA.
AC O21298; O21297; Q8HC80; Q8HCG5; Q8HQF3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 3.
DT 03-AUG-2022, entry version 97.
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 Rhinolophus ferrumequinum (Greater horseshoe bat).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Rhinolophidae;
OC Rhinolophinae; Rhinolophus.
OX NCBI_TaxID=59479;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Sakai T., Kikkawa Y., Tuchiya K., Harada M., Kanoe M., Yoshiyuki M.,
RA Yonekawa H.;
RT "Bats cytochrome b gene.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-119 AND 282-379.
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; AB085721; BAC16615.1; -; Genomic_DNA.
DR EMBL; AB085722; BAC16616.1; -; Genomic_DNA.
DR EMBL; AB085723; BAC16617.1; -; Genomic_DNA.
DR EMBL; AB085724; BAC16618.1; -; Genomic_DNA.
DR EMBL; AB085725; BAC16619.1; -; Genomic_DNA.
DR EMBL; AB085726; BAC16620.1; -; Genomic_DNA.
DR EMBL; AB085727; BAC16621.1; -; Genomic_DNA.
DR EMBL; AB085728; BAC16622.1; -; Genomic_DNA.
DR EMBL; AB085729; BAC16623.1; -; Genomic_DNA.
DR EMBL; AB085730; BAC16624.1; -; Genomic_DNA.
DR EMBL; AB085731; BAC16625.1; -; Genomic_DNA.
DR EMBL; U95513; AAC48750.1; -; Genomic_DNA.
DR EMBL; U95514; AAC48751.1; -; Genomic_DNA.
DR AlphaFoldDB; O21298; -.
DR SMR; O21298; -.
DR Proteomes; UP000472240; Mitochondrion.
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_0000061496"
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 78
FT /note="V -> A"
FT VARIANT 117
FT /note="I -> T"
FT CONFLICT 303
FT /note="A -> V (in Ref. 2; AAC48751)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="A -> T (in Ref. 2; AAC48751)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 42367 MW; 0EEDEB7D29C79DFA CRC64;
MTNIRKSHPL FKIINDSFVD LPAPSSISSW WNFGSLLGIC LAIQILTGLF LAMHYTSDTA
TAFHSVTHIC RDVNYGWVLR YLHANGASMF FICLFLHVGR GIYYGSYTFS ETWNIGIILL
FAVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYVGTTL VEWVWGGFSV DKATLTRFFA
LHFLLPFIIA AMVMVHLLFL HETGSNNPTG IPSDADMIPF HPYYTIKDIL GLVLMLMALL
SLVLFAPDLL GDPDNYTPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VVALVLSILI
LAAIPLLHTS KQRSMAFRPL SQCLFWLLVA DLLTLTWIGG QPVEHPFIII GQLASILYFL
IILVLMPLAS IAENHLLKW
