CYB_SORCI
ID CYB_SORCI Reviewed; 379 AA.
AC O79451; O21396; Q8SFK8; Q8SFK9; Q8SFL0; Q8SFL1;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 3.
DT 03-AUG-2022, entry version 98.
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 Sorex cinereus (Masked shrew).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Soricidae; Soricinae; Sorex.
OX NCBI_TaxID=36803;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate AFTC 25384, Isolate AFTC 4300, Isolate AFTC 7380, and
RC Isolate NK 7943;
RA Demboski J.R., Cook J.A.;
RT "Phylogenetic diversification within the Sorex cinereus group
RT (Soricidae).";
RL J. Mammal. 84:144-158(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-134.
RC STRAIN=Alberta; TISSUE=Hindfoot;
RA Ohdachi S., Masuda R., Abe H., Adachi J., Dokuchaev N.E., Haukisalmi V.,
RA Yoshida M.C.;
RT "Molecular phylogeny from nucleotide sequences of the mitochondrial
RT cytochrome b gene and evolutionary history of Eurasian soricine shrews
RT (Mammalia, Insectivora).";
RL Zool. Sci. 14:527-532(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 44-379.
RX PubMed=10191067; DOI=10.1006/mpev.1998.0568;
RA Fumagalli L., Taberlet P., Stewart D.T., Gielly L., Hausser J., Vogel P.;
RT "Molecular phylogeny and evolution of Sorex shrews (Soricidae: Insectivora)
RT inferred from mitochondrial DNA sequence data.";
RL Mol. Phylogenet. Evol. 11:222-235(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; AY014941; AAG40500.1; -; Genomic_DNA.
DR EMBL; AY014943; AAG40502.1; -; Genomic_DNA.
DR EMBL; AY014949; AAG40508.1; -; Genomic_DNA.
DR EMBL; AY014952; AAG40511.1; -; Genomic_DNA.
DR EMBL; D85355; BAA21348.1; -; Genomic_DNA.
DR EMBL; AJ000456; CAA04100.1; -; Genomic_DNA.
DR AlphaFoldDB; O79451; -.
DR SMR; O79451; -.
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_0000061553"
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 238
FT /note="T -> I"
FT VARIANT 238
FT /note="T -> V"
FT VARIANT 304
FT /note="I -> V"
FT CONFLICT 50..52
FT /note="FLA -> LLP (in Ref. 1; CAA04100)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="T -> S (in Ref. 1; CAA04100)"
FT /evidence="ECO:0000305"
FT CONFLICT 72..74
FT /note="DVN -> EVD (in Ref. 1; CAA04100)"
FT /evidence="ECO:0000305"
FT CONFLICT 346..349
FT /note="PFII -> LLLL (in Ref. 1; CAA04100)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="L -> I (in Ref. 1; CAA04100)"
FT /evidence="ECO:0000305"
FT CONFLICT 363..365
FT /note="LVL -> FVV (in Ref. 1; CAA04100)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="F -> L (in Ref. 1; CAA04100)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 42627 MW; EC1EF2454E7B6F5B CRC64;
MTNLRKTHPL MKIINSSFID LPAPSNISSW WNFGSLLGVC LIVQILTGLF LAMHYTSDTM
TAFSSVTHIC RDVNYGWLIR YLHANGASMF FICLFLHVGR GLYYGSYMFL ETWNIGVLLL
FAVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGSDL VEWIWGGFSV DKATLTRFFA
FHFILPFIIA ALAGVHLLFL HETGSNNPSG LCSDADKIPF HPYYTIKDIL GVLLLILTLT
SLVLFSPDLL GDPDNYTPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALVLSILV
LAVIPFLHTS KQRSMMFRPF SQCLFWILVA DLLTLTWIGG QPVEHPFIII GQLASILYFL
LILVLMPITS LFENNLLKW
