CYB_SHEEP
ID CYB_SHEEP Reviewed; 379 AA.
AC P24959; O78758; Q35207; Q35271;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 117.
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 Ovis aries (Sheep).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1901092; DOI=10.1007/bf02515385;
RA Irwin D.M., Kocher T.D., Wilson A.C.;
RT "Evolution of the cytochrome b gene of mammals.";
RL J. Mol. Evol. 32:128-144(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RA Arai K., Munechika I., Ito I., Kikkawa A., Kanazawa T., Kosugiyama M.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hassanin A., Pasquet E., Vigne J.-D.;
RT "Molecular systematics of the subfamily Caprinae (Artiodactyla, Bovidae) as
RT determined from cytochrome b sequences.";
RL J. Mammal. Evol. 5:217-236(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Merinolandschaf {ECO:0000312|Proteomes:UP000002356}; TISSUE=Liver;
RX PubMed=9767689; DOI=10.1007/pl00006401;
RA Hiendleder S., Lewalski H., Wassmuth R., Janke A.;
RT "The complete mitochondrial DNA sequence of the domestic sheep (Ovis aries)
RT and comparison with the other major ovine haplotype.";
RL J. Mol. Evol. 47:441-448(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 204-379.
RX PubMed=8536319; DOI=10.1007/bf00311887;
RA Zardoya R., Villalta M., Lopez-Perez M.J., Garrido-Pertierra A.,
RA Montoya J., Bautista J.M.;
RT "Nucleotide sequence of the sheep mitochondrial DNA D-loop and its flanking
RT tRNA genes.";
RL Curr. Genet. 28:94-96(1995).
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; X56284; CAA39731.1; -; Genomic_DNA.
DR EMBL; D84205; BAA12255.1; -; Genomic_DNA.
DR EMBL; AF034730; AAC31685.1; -; Genomic_DNA.
DR EMBL; AF010406; AAD10107.1; -; Genomic_DNA.
DR EMBL; L29055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S17413; S17413.
DR RefSeq; NP_008418.1; NC_001941.1.
DR PDB; 5J4Z; EM; 5.80 A; AC/AN=2-379.
DR PDB; 5J7Y; EM; 6.70 A; AC/AN=2-379.
DR PDB; 5J8K; EM; 7.80 A; AC/AN=2-379.
DR PDB; 6Q9E; EM; 3.90 A; b1/b2=1-379.
DR PDB; 6QBX; EM; 4.20 A; b1/b2=1-379.
DR PDB; 6QC2; EM; 4.20 A; b1/b2=1-379.
DR PDB; 6QC3; EM; 4.20 A; b1/b2=1-379.
DR PDB; 6QC4; EM; 4.60 A; b1/b2=1-379.
DR PDBsum; 5J4Z; -.
DR PDBsum; 5J7Y; -.
DR PDBsum; 5J8K; -.
DR PDBsum; 6Q9E; -.
DR PDBsum; 6QBX; -.
DR PDBsum; 6QC2; -.
DR PDBsum; 6QC3; -.
DR PDBsum; 6QC4; -.
DR AlphaFoldDB; P24959; -.
DR SMR; P24959; -.
DR STRING; 9940.ENSOARP00000000013; -.
DR GeneID; 808260; -.
DR KEGG; oas:808260; -.
DR CTD; 4519; -.
DR eggNOG; KOG4663; Eukaryota.
DR OrthoDB; 1125966at2759; -.
DR Proteomes; UP000002356; Mitochondrion.
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 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..379
FT /note="Cytochrome b"
FT /id="PRO_0000061537"
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 295
FT /note="V -> I"
FT CONFLICT 191
FT /note="A -> G (in Ref. 2; BAA12255)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="I -> T (in Ref. 3; AAC31685 and 5; L29055)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 42849 MW; 88EBEF36398C7F12 CRC64;
MINIRKTHPL MKIVNNAFID LPAPSNISSW WNFGSLLGIC LILQILTGLF LAMHYTPDTT
TAFSSVTHIC RDVNYGWIIR YMHANGASMF FICLFMHVGR GLYYGSYTFL ETWNIGVILL
FATMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTNL VEWIWGGFSV DKATLTRFFA
FHFIFPFIIA ALAMVHLLFL HETGSNNPTG IPSDTDKIPF HPYYTIKDIL GAILLILILM
LLVLFTPDLL GDPDNYTPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALVLSILV
LVIMPLLHTS KQRSMMFRPI SQCMFWILVA DLLTLTWIGG QPVEHPYIII GQLASIMYFL
IILVMMPVAS IIENNLLKW
