CYB_MYOGP
ID CYB_MYOGP Reviewed; 380 AA.
AC Q9G1R4; Q9G4P6; Q9G4P8; Q9G4P9;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 90.
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 Myodes gapperi (Southern red-backed vole) (Clethrionomys gapperi).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Arvicolinae; Myodes.
OX NCBI_TaxID=473866;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate AF 26033, Isolate AF 2644, Isolate AF 2780, Isolate AF 3221,
RC Isolate AF 4267, and Isolate AF 4995;
RA Cook J.A., Bidlack A.L., Conroy C.J., Demboski J.R., Fleming M.A.,
RA Runck A.M., Stone K.D., MacDonald S.O.;
RT "A phylogeographic perspective on endemism in the Alexander archipelago of
RT the North Pacific.";
RL Biol. Conserv. 97:215-227(2001).
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; AF272633; AAG44805.1; -; Genomic_DNA.
DR EMBL; AF272634; AAG44806.1; -; Genomic_DNA.
DR EMBL; AF272635; AAG44807.1; -; Genomic_DNA.
DR EMBL; AF272636; AAG44808.1; -; Genomic_DNA.
DR EMBL; AF272637; AAG44809.1; -; Genomic_DNA.
DR EMBL; AF272639; AAG44811.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9G1R4; -.
DR SMR; Q9G1R4; -.
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_0000060793"
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 11
FT /note="I -> M (in strain: Isolate AF 3221)"
FT VARIANT 17
FT /note="S -> A (in strain: Isolate AF 2664)"
FT VARIANT 23
FT /note="A -> T (in strain: Isolate AF 3221)"
FT VARIANT 40
FT /note="C -> W (in strain: Isolate AF 2664)"
FT VARIANT 42
FT /note="I -> A (in strain: Isolate AF 3221)"
FT VARIANT 42
FT /note="I -> T (in strain: Isolate AF 2664)"
FT VARIANT 237
FT /note="M -> T (in strain: Isolate AF 3221)"
FT VARIANT 286
FT /note="N -> S (in strain: Isolate AF 4995)"
FT VARIANT 300
FT /note="V -> I (in strain: Isolate AF 2664 and Isolate AF
FT 3221)"
FT VARIANT 349
FT /note="I -> V (in strain: Isolate AF 3221)"
FT VARIANT 360
FT /note="T -> A (in strain: Isolate AF 2664 and Isolate AF
FT 3221)"
FT VARIANT 363
FT /note="I -> V (in strain: Isolate AF 2664 and Isolate AF
FT 3221)"
FT VARIANT 365
FT /note="L -> F (in strain: Isolate AF 2664)"
FT VARIANT 375
FT /note="N -> S (in strain: Isolate AF 3221)"
FT VARIANT 378
FT /note="D -> G (in strain: Isolate AF 3221)"
SQ SEQUENCE 380 AA; 42876 MW; 6B9FF1E6E0475BA6 CRC64;
MTIIRKKHPL IKIINHSFID LPAPSNISSW WNFGSLLGLC LIIQILTGLF LAMHYTSDTS
TAFSSVTHIC RDVNYGWLIR YMHANGASMF FICLFLHVGR GMYYGSYNMI ETWNMGIILL
FAVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTTL VEWIWGGFSV DKATLTRFFA
FHFILPFIIT ALVFVHLLFL HETGSNNPTG LNSDADKIPF HPYYTIKDFL GVLILLMGLM
ILVLFFPDVL GDPDNYTPAN PLNTPAHIKP EWYFLFAYAI LRSIPNKLGG VLALILSILV
LALLPLLHTS KQRGLTFRPI TQTMYWILVA DLLILTWIGG QPVEYPFIII GQMASIAYFT
IIIILMPMAG MIENNILDLD
