CYB_DAMDA
ID CYB_DAMDA Reviewed; 379 AA.
AC P24955; O47937;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 103.
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 Dama dama (Fallow deer) (Cervus dama).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Cervinae; Dama.
OX NCBI_TaxID=30532;
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].
RX PubMed=9628037; DOI=10.1098/rspb.1998.0362;
RA Randi E., Mucci N., Pierpaoli M., Douzery E.J.P.;
RT "New phylogenetic perspectives on the Cervidae (Artiodactyla) are provided
RT by the mitochondrial cytochrome b gene.";
RL Proc. R. Soc. B 265:793-801(1998).
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; X56290; CAA39737.1; -; Genomic_DNA.
DR EMBL; AJ000022; CAA03861.1; -; Genomic_DNA.
DR PIR; S17409; S17409.
DR AlphaFoldDB; P24955; -.
DR SMR; P24955; -.
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_0000060856"
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 CONFLICT 7
FT /note="T -> S (in Ref. 1; CAA39737)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="I -> M (in Ref. 1; CAA39737)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="T -> M (in Ref. 1; CAA39737)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="V -> M (in Ref. 1; CAA39737)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="V -> A (in Ref. 1; CAA39737)"
FT /evidence="ECO:0000305"
FT CONFLICT 232..241
FT /note="ILFLFLFLMT -> ALLMILVLMM (in Ref. 1; CAA39737)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="A -> S (in Ref. 1; CAA39737)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="L -> V (in Ref. 1; CAA39737)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="K -> N (in Ref. 1; CAA39737)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="H -> L (in Ref. 1; CAA39737)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="S -> L (in Ref. 1; CAA39737)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="L -> F (in Ref. 1; CAA39737)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="F -> L (in Ref. 1; CAA39737)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="V -> I (in Ref. 1; CAA39737)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="Y -> H (in Ref. 1; CAA39737)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="T -> I (in Ref. 1; CAA39737)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="E -> Q (in Ref. 1; CAA39737)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 42917 MW; 7D5B0752E4FBE59F CRC64;
MINIRKTHPL MKIVNNAFID LPAPSNISSW WNFGSLLGIC LILQILTGLF LAMHYTSDTM
TAFSSVTHIC RDVNYGWIIR YMHANGASMF FICLFIHVGR GLYYGSYTFL ETWNIGVILL
FTVMATAFVG YVLPWGQMSF WGATVITNLL SAIPYIGTNL VEWIWGGFSV DKATLTRFFA
FHFILPFIIA ALAMVHLLFL HETGSNNPTG IPSDVDKIPF HPYYTIKDIL GILFLFLFLM
TLVLFAPDLL GDPDKYTPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALVSSILI
LILMPFLHTS KQRSMMFRPF SQCLFWVLVA DLLTLTWIGG QPVEYPFITI GQLASILYFL
IILVLMPATS TIENNLLKW
