ID   CYB_MAMPR               Reviewed;         378 AA.
AC   P92658; Q35052; Q35053; Q36723; Q38PR0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-JAN-2003, sequence version 3.
DT   27-MAR-2024, entry version 109.
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   Mammuthus primigenius (Siberian woolly mammoth).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Mammuthus.
OX   NCBI_TaxID=37349;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Muscle;
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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16362058; DOI=10.1038/nature04432;
RA   Krause J., Dear P.H., Pollack J.L., Slatkin M., Spriggs H., Barnes I.,
RA   Lister A.M., Ebersberger I., Paeaebo S., Hofreiter M.;
RT   "Multiplex amplification of the mammoth mitochondrial genome and the
RT   evolution of Elephantidae.";
RL   Nature 439:724-727(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Muscle;
RX   PubMed=16448217; DOI=10.1371/journal.pbio.0040073;
RA   Rogaev E.I., Moliaka Y.K., Malyarchuk B.A., Kondrashov F.A., Derenko M.V.,
RA   Chumakov I., Grigorenko A.P.;
RT   "Complete mitochondrial genome and phylogeny of Pleistocene mammoth
RT   Mammuthus primigenius.";
RL   PLoS Biol. 4:403-410(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-335.
RC   TISSUE=Muscle;
RX   PubMed=9089080; DOI=10.1007/pl00006160;
RA   Ozawa T., Hayashi S., Mikhelson V.M.;
RT   "Phylogenetic position of mammoth and Steller's sea cow within Tethytheria
RT   demonstrated by mitochondrial DNA sequences.";
RL   J. Mol. Evol. 44:406-413(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-143.
RA   Derenko M., Malyarchuk B., Shields G.F.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-106.
RC   STRAIN=Isolate allele Fairbank, and Isolate allele Lyakhovskiy;
RA   Yang H., Golenberg E.M., Shoshani J.;
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-114.
RC   TISSUE=Bone;
RX   PubMed=8047136; DOI=10.1038/370333b0;
RA   Hagelberg E., Thomas M.G., Cook C.E. Jr., Sher A.V., Baryshnikov G.F.,
RA   Lister A.M.;
RT   "DNA from ancient mammoth bones.";
RL   Nature 370:333-334(1994).
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; D50842; BAA25008.1; -; Genomic_DNA.
DR   EMBL; DQ188829; ABA29796.1; -; Genomic_DNA.
DR   EMBL; DQ316067; ABC17890.1; -; Genomic_DNA.
DR   EMBL; D83047; BAA20277.1; -; Genomic_DNA.
DR   EMBL; U79411; AAB38284.1; -; Genomic_DNA.
DR   EMBL; U23738; AAA73786.1; -; Genomic_DNA.
DR   EMBL; U23739; AAA73787.1; -; Genomic_DNA.
DR   EMBL; S72502; AAD14109.1; -; Genomic_DNA.
DR   RefSeq; YP_398766.1; NC_007596.2.
DR   AlphaFoldDB; P92658; -.
DR   SMR; P92658; -.
DR   GeneID; 3773153; -.
DR   CTD; 4519; -.
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   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; IPR048260; Cytochrome_b_C_euk/bac.
DR   InterPro; IPR048259; Cytochrome_b_N_euk/bac.
DR   InterPro; IPR016174; Di-haem_cyt_TM.
DR   PANTHER; PTHR19271; CYTOCHROME B; 1.
DR   PANTHER; PTHR19271:SF16; CYTOCHROME B; 1.
DR   Pfam; PF00032; Cytochrom_B_C; 1.
DR   Pfam; PF00033; Cytochrome_B; 1.
DR   PIRSF; PIRSF038885; COB; 1.
DR   SUPFAM; SSF81648; a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1.
DR   SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 1.
DR   PROSITE; PS51003; CYTB_CTER; 1.
DR   PROSITE; PS51002; CYTB_NTER; 1.
PE   3: Inferred from homology;
KW   Electron transport; Extinct organism protein; Heme; Iron; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW   Respiratory chain; Transmembrane; Transmembrane helix; Transport;
KW   Ubiquinone.
FT   CHAIN           1..378
FT                   /note="Cytochrome b"
FT                   /id="PRO_0000061150"
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        95..96
FT                   /note="Missing (in Ref. 7; AAD14109)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="I -> V (in Ref. 4; BAA20277)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   378 AA;  42777 MW;  786EDA681CDB0958 CRC64;
     MTHIRKSHPL LKILNKSFID LPTPSNISTW WNFGSLLGAC LITQILTGLF LAMHYTPDTM
     TAFSSMSHIC RDVNYGWIIR QLHSNGASIF FLCLYTHIGR NIYYGSYLYS ETWNTGIMLL
     LITMATAFMG YVLPWGQMSF WGATVITNLF SAIPYIGTDL VEWIWGGFSV DKATLNRFFA
     LHFILPFTMI ALAGVHLTFL HETGSNNPLG LTSDSDKIPF HPYYTIKDFL GLLILILFLL
     LLALLSPDML GDPDNYMPAD PLNTPLHIKP EWYFLFAYAI LRSVPNKLGG VLALLLSILI
     LGIMPLLHTS KHRSMMLRPL SQVLFWTLAT DLLMLTWIGS QPVEYPYIII GQMASILYFS
     IILAFLPIAG MIENYLIK
//