CYB_CRODS
ID CYB_CRODS Reviewed; 379 AA.
AC Q8SE89; Q8SE87; Q8SE88; Q8SJX6; Q8SJX7; Q8SJX8; Q8SJX9;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 Crocidura dsinezumi (Dsinezumi shrew) (Japanese white-toothed shrew).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Soricidae; Crocidurinae; Crocidura.
OX NCBI_TaxID=62277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate DAO1Cds98/8/21-1Aomori, Isolate HA5295, Isolate HA5296,
RC Isolate HA5464, Isolate HA5796, Isolate HA6134, Isolate HEG113,
RC Isolate HEG232, Isolate HEG240, Isolate HEG246, Isolate HS1237,
RC Isolate HS1295, Isolate HS1296, Isolate HS1297, Isolate HS1306,
RC Isolate HSO960925-1, Isolate HSO960926-1, Isolate HSO960926-2,
RC Isolate SO2Kmisc100, and Isolate SO2Kmisc101;
RA Ohdachi S.D., Iwasa M.A., Han S.;
RT "Molecular phylogeny of East Asiatic white-toothed shrews genus
RT Crocidura.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
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; AB077059; BAB88559.1; -; Genomic_DNA.
DR EMBL; AB077060; BAB88560.1; -; Genomic_DNA.
DR EMBL; AB077061; BAB88561.1; -; Genomic_DNA.
DR EMBL; AB077062; BAB88562.1; -; Genomic_DNA.
DR EMBL; AB077063; BAB88563.1; -; Genomic_DNA.
DR EMBL; AB077064; BAB88564.1; -; Genomic_DNA.
DR EMBL; AB077065; BAB88565.1; -; Genomic_DNA.
DR EMBL; AB077066; BAB88566.1; -; Genomic_DNA.
DR EMBL; AB077067; BAB88567.1; -; Genomic_DNA.
DR EMBL; AB077068; BAB88568.1; -; Genomic_DNA.
DR EMBL; AB077069; BAB88569.1; -; Genomic_DNA.
DR EMBL; AB077070; BAB88570.1; -; Genomic_DNA.
DR EMBL; AB077270; BAB88598.1; -; Genomic_DNA.
DR EMBL; AB077271; BAB88599.1; -; Genomic_DNA.
DR EMBL; AB077272; BAB88600.1; -; Genomic_DNA.
DR EMBL; AB077273; BAB88601.1; -; Genomic_DNA.
DR EMBL; AB077274; BAB88602.1; -; Genomic_DNA.
DR EMBL; AB077275; BAB88603.1; -; Genomic_DNA.
DR EMBL; AB077276; BAB88604.1; -; Genomic_DNA.
DR EMBL; AB077277; BAB88605.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8SE89; -.
DR SMR; Q8SE89; -.
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_0000060826"
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 23
FT /note="A -> T (in strain: Isolate DAO1Cds98/8/21-1Aomori)"
FT VARIANT 158
FT /note="T -> I (in strain: Isolate SO2Kmisc100 and Isolate
FT SO2Kmisc101)"
FT VARIANT 258
FT /note="P -> L (in strain: Isolate SO2Kmisc100)"
FT VARIANT 302
FT /note="A -> G (in strain: Isolate SO2Kmisc101)"
FT VARIANT 345
FT /note="H -> Y (in strain: Isolate HS1296, Isolate HS1297
FT and Isolate HSO960926-1)"
FT VARIANT 360
FT /note="M -> T (in strain: Isolate HA6134, Isolate HS1237,
FT Isolate HS1295, Isolate HS1296, Isolate HS1297, Isolate
FT HSO960926-1, Isolate SO2Kmisc100 and Isolate SO2Kmisc101)"
FT VARIANT 365
FT /note="I -> V (in strain: Isolate HA6134, Isolate
FT SO2Kmisc100 and Isolate SO2Kmisc101)"
SQ SEQUENCE 379 AA; 42553 MW; A8B5072B34AD966F CRC64;
MNNIRKTHPL MKIVNSSFID LPAPSNISSW WNFGSLLGIC LIAQILTGLF LAMHYTSDTM
TAFSSVTHIC RDVNYGWLIR YLHANGASMF FICLFLHVGR GLYYGSYMYL ETWNIGVLLL
FAVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTNL VEWIWGGFSV DKATLTRFFA
FHFILPFIVA ALAGVHLLFL HETGSNNPSG LNSDTDKIPF HPYYTIKDIL GALIMITALS
SLVLFSPDLL GDPDNYIPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALVLSIAI
LAIIPLLHTA KQRSMMFRPL SQCLFWILVA DLFTLTWIGG QPVEHPFVVI GQLASVIYFM
LILLIMPTTS MIENRLLKW
