CYB_LOXAF
ID CYB_LOXAF Reviewed; 378 AA.
AC P24958; O47887; O48349; Q9G5G0; Q9XNF4;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 125.
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 Loxodonta africana (African elephant).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785;
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=9493356; DOI=10.1007/pl00006308;
RA Noro M., Masuda R., Dubrovo I.A., Yoshida M.C., Kato M.;
RT "Molecular phylogenetic inference of the woolly mammoth Mammuthus
RT primigenius, based on complete sequences of mitochondrial cytochrome b and
RT 12S ribosomal RNA genes.";
RL J. Mol. Evol. 46:314-326(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RA Hauf J., Waddell P.J., Chalwatzis N., Joger U., Zimmermann F.K.;
RT "The complete mitochondrial genome sequence of the African elephant
RT (Loxodonta africana), phylogenetic relationships of Proboscidea to other
RT mammals and D-loop heteroplasmy.";
RL Zoology 102:184-195(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-376.
RX PubMed=10457597; DOI=10.1016/s0764-4469(99)80093-6;
RA Barriel V., Thuet E., Tassy P.;
RT "Molecular phylogeny of Elephantidae. Extreme divergence of the extant
RT forest African elephant.";
RL C. R. Acad. Sci. III, Sci. Vie 322:447-454(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-106.
RX PubMed=8577738; DOI=10.1073/pnas.93.3.1190;
RA Yang H., Golenberg E.M., Shoshani J.;
RT "Phylogenetic resolution within the Elephantidae using fossil DNA sequence
RT from the American mastodon (Mammut americanum) as an outgroup.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:1190-1194(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 339-378.
RA Mueller S., Steinborn R., Mueller M.;
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
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; X56285; CAA39732.1; -; Genomic_DNA.
DR EMBL; D84150; BAA25011.1; -; Genomic_DNA.
DR EMBL; D84151; BAA25012.1; -; Genomic_DNA.
DR EMBL; D84152; BAA25013.1; -; Genomic_DNA.
DR EMBL; AJ224821; CAA12150.1; -; Genomic_DNA.
DR EMBL; AF132528; AAD44171.1; -; Genomic_DNA.
DR EMBL; U23741; AAA73784.1; -; Genomic_DNA.
DR EMBL; AF219242; AAG44238.1; -; Genomic_DNA.
DR PIR; T45562; S17412.
DR RefSeq; NP_009291.1; NC_000934.1.
DR AlphaFoldDB; P24958; -.
DR SMR; P24958; -.
DR STRING; 9785.ENSLAFP00000029503; -.
DR Ensembl; ENSLAFT00000038069; ENSLAFP00000029503; ENSLAFG00000033303.
DR GeneID; 808783; -.
DR KEGG; lav:808783; -.
DR CTD; 4519; -.
DR eggNOG; KOG4663; Eukaryota.
DR GeneTree; ENSGT00390000017948; -.
DR HOGENOM; CLU_031114_3_0_1; -.
DR InParanoid; P24958; -.
DR OMA; RFFAFHF; -.
DR OrthoDB; 1125966at2759; -.
DR TreeFam; TF353088; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:Ensembl.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:Ensembl.
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; Reference proteome; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..378
FT /note="Cytochrome b"
FT /id="PRO_0000061136"
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 3
FT /note="H -> D (in Ref. 1; CAA39732)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="I -> M (in Ref. 1; CAA39732)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="F -> L (in Ref. 1; CAA39732)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="Y -> C (in Ref. 2; BAA25012/BAA25013)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="T -> I (in Ref. 2; BAA25012/BAA25013)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="M -> H (in Ref. 1; CAA39732)"
FT /evidence="ECO:0000305"
FT CONFLICT 257..260
FT /note="MPAD -> TLAN (in Ref. 1; CAA39732)"
FT /evidence="ECO:0000305"
FT CONFLICT 264..266
FT /note="TPL -> NPP (in Ref. 1; CAA39732)"
FT /evidence="ECO:0000305"
FT CONFLICT 322..325
FT /note="QVLF -> LCAYC (in Ref. 1; CAA39732)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 42740 MW; 05E75F539C8F9D6F CRC64;
MTHIRKSHPL LKIINKSFID LPTPSNISTW WNFGSLLGAC LITQILTGLF LAMHYTPDTM
TAFSSMSHIC RDVNYGWIIR QLHSNGASIF FLCLYTHIGR NIYYGSYLYS ETWNTGIMLL
LITMATAFMG YVLPWGQMSF WGATVITNLF SAIPYIGTNL VEWIWGGFSV DKATLNRFFA
LHFILPFTMI ALAGVHLTFL HETGSNNPLG LTSDSDKIPF HPYYTIKDFL GLLILILLLL
LLALLSPDML GDPDNYMPAD PLNTPLHIKP EWYFLFAYAI LRSVPNKLGG VLALLLSILI
LGLMPLLHTS KHRSMMLRPL SQVLFWTLTM DLLTLTWIGS QPVEYPYIII GQMASILYFS
IILAFLPIAG VIENYLIK
