CYB_MOUSE
ID CYB_MOUSE Reviewed; 381 AA.
AC P00158;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 167.
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, mt-Cytb, Mtcyb;
OS Mus musculus (Mouse).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7332926; DOI=10.1016/0092-8674(81)90300-7;
RA Bibb M.J., van Etten R.A., Wright C.T., Walberg M.W., Clayton D.A.;
RT "Sequence and gene organization of mouse mitochondrial DNA.";
RL Cell 26:167-180(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=12954771; DOI=10.1093/nar/gkg739;
RA Bayona-Bafaluy M.P., Acin-Perez R., Mullikin J.C., Park J.S.,
RA Moreno-Loshuertos R., Hu P., Perez-Martos A., Fernandez-Silva P., Bai Y.,
RA Enriquez J.A.;
RT "Revisiting the mouse mitochondrial DNA sequence.";
RL Nucleic Acids Res. 31:5349-5355(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-381.
RX PubMed=2176148; DOI=10.1002/j.1460-2075.1990.tb07879.x;
RA Shan B., Vazquez E., Lewis J.A.;
RT "Interferon selectively inhibits the expression of mitochondrial genes: a
RT novel pathway for interferon-mediated responses.";
RL EMBO J. 9:4307-4314(1990).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=6326133; DOI=10.1073/pnas.81.9.2606;
RA Gupte S., Wu E.S., Hoechli L., Hoechli M., Jacobson K., Sowers A.E.,
RA Hackenbrock C.R.;
RT "Relationship between lateral diffusion, collision frequency, and electron
RT transfer of mitochondrial inner membrane oxidation-reduction components.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:2606-2610(1984).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000269|PubMed:6326133}; 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA24092.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J01420; AAB48656.1; -; Genomic_DNA.
DR EMBL; V00711; CAA24092.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY172335; AAN85134.1; -; Genomic_DNA.
DR EMBL; X57780; CAA40926.1; -; mRNA.
DR PIR; A00153; CBMS.
DR RefSeq; NP_904340.1; NC_005089.1.
DR PDB; 7O37; EM; 3.20 A; C/N=1-381.
DR PDB; 7O3C; EM; 3.30 A; C/N=1-381.
DR PDB; 7O3E; EM; 3.60 A; C/N=1-381.
DR PDB; 7O3H; EM; 2.60 A; C/N=1-381.
DR PDBsum; 7O37; -.
DR PDBsum; 7O3C; -.
DR PDBsum; 7O3E; -.
DR PDBsum; 7O3H; -.
DR AlphaFoldDB; P00158; -.
DR SMR; P00158; -.
DR BioGRID; 201544; 2.
DR ComplexPortal; CPX-563; Mitochondrial respiratory chain complex III.
DR CORUM; P00158; -.
DR IntAct; P00158; 1.
DR STRING; 10090.ENSMUSP00000081003; -.
DR PhosphoSitePlus; P00158; -.
DR jPOST; P00158; -.
DR PaxDb; P00158; -.
DR PRIDE; P00158; -.
DR ProteomicsDB; 285437; -.
DR Antibodypedia; 35365; 181 antibodies from 28 providers.
DR Ensembl; ENSMUST00000082421; ENSMUSP00000081003; ENSMUSG00000064370.
DR GeneID; 17711; -.
DR KEGG; mmu:17711; -.
DR CTD; 4519; -.
DR MGI; MGI:102501; mt-Cytb.
DR VEuPathDB; HostDB:ENSMUSG00000064370; -.
DR eggNOG; KOG4663; Eukaryota.
DR GeneTree; ENSGT00390000017948; -.
DR HOGENOM; CLU_031114_3_0_1; -.
DR InParanoid; P00158; -.
DR OMA; RFFAFHF; -.
DR OrthoDB; 1125966at2759; -.
DR PhylomeDB; P00158; -.
DR TreeFam; TF353088; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR ChiTaRS; mt-Cytb; mouse.
DR PRO; PR:P00158; -.
DR Proteomes; UP000000589; Mitochondrion.
DR RNAct; P00158; protein.
DR Bgee; ENSMUSG00000064370; Expressed in retinal neural layer and 61 other tissues.
DR ExpressionAtlas; P00158; baseline and differential.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0045333; P:cellular respiration; IC:ComplexPortal.
DR GO; GO:0015990; P:electron transport coupled proton transport; ISO:MGI.
DR GO; GO:0042538; P:hyperosmotic salinity response; ISO:MGI.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IC:ComplexPortal.
DR GO; GO:0046686; P:response to cadmium ion; ISO:MGI.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR GO; GO:0033590; P:response to cobalamin; IEA:Ensembl.
DR GO; GO:0046688; P:response to copper ion; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0033762; P:response to glucagon; ISO:MGI.
DR GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0046689; P:response to mercury ion; ISO:MGI.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Respiratory chain; Transmembrane; Transmembrane helix; Transport;
KW Ubiquinone.
FT CHAIN 1..381
FT /note="Cytochrome b"
FT /id="PRO_0000061211"
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:0000255|PROSITE-ProRule:PRU00968"
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 TURN 5..7
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 11..18
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 33..52
FT /evidence="ECO:0007829|PDB:7O3H"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 76..103
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 110..132
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 137..150
FT /evidence="ECO:0007829|PDB:7O3H"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 172..201
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 223..243
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 272..281
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 287..303
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 319..339
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 347..363
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 365..376
FT /evidence="ECO:0007829|PDB:7O3H"
SQ SEQUENCE 381 AA; 43210 MW; 6B46D5B1DD8E001A CRC64;
MTNMRKTHPL FKIINHSFID LPAPSNISSW WNFGSLLGVC LMVQIITGLF LAMHYTSDTM
TAFSSVTHIC RDVNYGWLIR YMHANGASMF FICLFLHVGR GLYYGSYTFM ETWNIGVLLL
FAVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTTL VEWIWGGFSV DKATLTRFFA
FHFILPFIIA ALAIVHLLFL HETGSNNPTG LNSDADKIPF HPYYTIKDIL GILIMFLILM
TLVLFFPDML GDPDNYMPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALILSILI
LALMPFLHTS KQRSLMFRPI TQILYWILVA NLLILTWIGG QPVEHPFIII GQLASISYFS
IILILMPISG IIEDKMLKLY P
