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CYB_RHIWE
ID   CYB_RHIWE               Reviewed;         380 AA.
AC   Q9XNW4;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 84.
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   Rhipidomys wetzeli (Wetzel's climbing mouse).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Sigmodontinae; Rhipidomys.
OX   NCBI_TaxID=89106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate USNM 560658;
RA   Smith M.F., Patton J.L.;
RT   "Phylogenetic relationships and the radiation of sigmodontine rodents in
RT   South America: evidence from cytochrome b.";
RL   J. Mammal. Evol. 6:89-128(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; AF108680; AAD45462.1; -; Genomic_DNA.
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_0000061505"
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   380 AA;  42663 MW;  EF0C7AEF015F5526 CRC64;
     MTIMRKKHPL LKMINHSFID LPTPSNISSW WNFGSLLGMC LMIQILTGLF LAMHYTSDTT
     TAFSSVAHIC RDVNYGWLIR YLHANGASMF FICLFIHVGR GIYYGSYMLL ETWNIGIVLL
     LTTMATAFVG YVLPWGQMSF WGATVITNLL SAIPYXGNTL VEWIWGGFSV DKATLTRFFA
     FHFILPFIIT ALVLVHLLFL HETGSNNPSG LDSNSDKIPF HPYYTIKDLL GALILLMVLM
     ILVLFFPDVL GDPDNYTPAN PLNTPAHIKP EWYFLFAYAI LRSIPNKLGG VLALILSILI
     LATLPLLNSS KQHGLIYRPI TQALYWIFVA NLLTXTWIGG QPVEXPFTLI GXIASXLXFX
     IIIIFMPIAS TIXNNIPXLH
 
 
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