CYB_SORAR
ID CYB_SORAR Reviewed; 379 AA.
AC O79445; O21393; Q8W7T3; Q8W857; Q8W9E0; Q8W9E1; Q8W9E2; Q8W9E3; Q9MJQ6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 96.
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 araneus (Eurasian common shrew) (European shrew).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Soricidae; Soricinae; Sorex.
OX NCBI_TaxID=42254;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10666706; DOI=10.1093/oxfordjournals.molbev.a026238;
RA Mouchaty S.K., Gullberg A., Janke A., Arnason U.;
RT "The phylogenetic position of the Talpidae within Eutheria based on
RT analysis of complete mitochondrial sequences.";
RL Mol. Biol. Evol. 17:60-67(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS.
RC STRAIN=Isolate IZEA-2887, Isolate IZEA-3303, Isolate IZEA-3383,
RC Isolate IZEA-5326, Isolate IZEA-5339, Isolate IZEA-5381, Isolate IZEA-5561,
RC Isolate IZEA-6137, Isolate JS3032, Isolate JZ665, Isolate JZ835,
RC Isolate San Rhemy, and Isolate Si-91.4;
RA Brunner H., Lugon-Moulin N., Balloux F., Fumagalli L., Hausser J.;
RT "A taxonomical revaluation of the chromosome race Valais of the common
RT shrew, Sorex araneus (Insectivora: Soricidae).";
RL Acta Theriol. 47:245-275(2002).
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-134.
RC STRAIN=Isolate #361; TISSUE=Liver;
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).
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; AJ245893; CAB71157.1; -; Genomic_DNA.
DR EMBL; AJ312028; CAC84886.1; -; Genomic_DNA.
DR EMBL; AJ312029; CAC84887.1; -; Genomic_DNA.
DR EMBL; AJ312030; CAC84888.1; -; Genomic_DNA.
DR EMBL; AJ312031; CAC84889.1; -; Genomic_DNA.
DR EMBL; AJ312032; CAC84890.1; -; Genomic_DNA.
DR EMBL; AJ312033; CAC84891.1; -; Genomic_DNA.
DR EMBL; AJ312034; CAC84892.1; -; Genomic_DNA.
DR EMBL; AJ312035; CAC84893.1; -; Genomic_DNA.
DR EMBL; AJ312036; CAC84894.1; -; Genomic_DNA.
DR EMBL; AJ312037; CAC84895.1; -; Genomic_DNA.
DR EMBL; AJ312038; CAC84896.1; -; Genomic_DNA.
DR EMBL; AJ312039; CAC84897.1; -; Genomic_DNA.
DR EMBL; AJ312040; CAC84898.1; -; Genomic_DNA.
DR EMBL; AJ000415; CAA04063.2; -; Genomic_DNA.
DR EMBL; AJ000416; CAA04064.2; -; Genomic_DNA.
DR EMBL; D85351; BAA21344.1; -; Genomic_DNA.
DR AlphaFoldDB; O79445; -.
DR SMR; O79445; -.
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_0000061550"
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 16
FT /note="S -> N (in strain: Isolate IZEA-6137)"
FT VARIANT 122
FT /note="A -> T (in strain: Isolate IZEA-6137)"
FT VARIANT 194
FT /note="G -> A (in strain: Isolate IZEA-5339)"
FT VARIANT 234
FT /note="L -> F (in strain: Isolate IZEA-5326, Isolate IZEA-
FT 5381 and Isolate IZEA-5561)"
FT VARIANT 238
FT /note="T -> A (in strain: Isolate IZEA-3303, Isolate IZEA-
FT 5326, Isolate IZEA-5339, Isolate IZEA-5381, Isolate IZEA-
FT 5561, Isolate San Rhemy and Isolate SI-91.4)"
FT VARIANT 257
FT /note="M -> T (in strain: Isolate IZEA-2887, Isolate IZEA-
FT 3303, Isolate IZEA-3383, Isolate IZEA-5326, Isolate IZEA-
FT 5339, Isolate IZEA-5381, Isolate IZEA-5561, Isolate IZEA-
FT 6137, Isolate JS3032, Isolate JZ665, Isolate JZ835, Isolate
FT San Rhemy and Isolate SI-91.4)"
FT VARIANT 295
FT /note="A -> V (in strain: Isolate IZEA-2887, Isolate IZEA-
FT 3303, Isolate IZEA-3383, Isolate IZEA-IZEA-5326, Isolate
FT IZEA-5339, Isolate IZEA-5381, Isolate IZEA-5561, Isolate
FT IZEA-6137, Isolate JS3032, Isolate JZ665, Isolate JZ835,
FT Isolate San Rhemy and Isolate SI-91.4)"
FT VARIANT 379
FT /note="W -> WK (in strain: Isolate IZEA-5381 and Isolate
FT JS3032)"
SQ SEQUENCE 379 AA; 42645 MW; 3BE014C304A45C52 CRC64;
MTNLRKTHPL MKIVNSSFID LPAPSNISSW WNFGSLLGVC LIIQILTGLF LAMHYTSDTM
TAFSSVTHIC RDVNYGWLIR YLHANGASMF FICLFLHVGR GLYYGSYMYL ETWNIGVLLL
FAVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGSDL VEWIWGGFSV DKATLTRFFA
FHFILPFIIA ALAGVHLLFL HETGSNNPSG LCSDADKIPF HPYYTIKDIL GVLLLILTLT
SLVLFSPDLL GDPDNYMPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALALSILI
LAVVPFLHTS KQRSMMFRPF SQCLFWILVA DLLTLTWIGG QPVEHPFIII GQLASILYFL
LILVIMPITS LFENNLLKW
