ID A0A1S6YGE8_DELLE Unreviewed; 379 AA.
AC A0A1S6YGE8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531, ECO:0000256|RuleBase:RU362117};
GN Name=CYTB {ECO:0000313|EMBL:AQX44357.1,
GN ECO:0000313|RefSeq:YP_009352188.1};
GN Synonyms=cytb {ECO:0000313|EMBL:AVY83262.1};
GN ORFNames=B6K20_mgp01 {ECO:0000313|RefSeq:YP_009352188.1};
OS Delphinapterus leucas (Beluga whale).
OG Mitochondrion {ECO:0000313|EMBL:AQX44357.1,
OG ECO:0000313|RefSeq:YP_009352188.1}.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|EMBL:AQX44357.1};
RN [1] {ECO:0000313|EMBL:AQX44357.1, ECO:0000313|RefSeq:YP_009352188.1}
RP NUCLEOTIDE SEQUENCE.
RA Kim J.H., Lee Y.-R., Koh J.-R., Jun J.W., Giri S.S., Kim H.J., Chi C.,
RA Yun S., Kim S.G., Kim S.W., Kim H.K., Jeong D.G., Park S.C.;
RT "Complete mitochondrial genome of the beluga whale Delphinapterus leucas
RT (Cetacea: Monodontidae).";
RL Conserv. Genet. 0:0-0(2017).
RN [2] {ECO:0000313|RefSeq:YP_009352188.1}
RP NUCLEOTIDE SEQUENCE.
RG NCBI Genome Project;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AVY83262.1}
RP NUCLEOTIDE SEQUENCE.
RA Meschersky I.G., Chernetsky A.D., Krasnova V.V., Solovyev B.A.,
RA Udovik D.A., Shpak O.V., Glazov D.M., Rozhnov V.V.;
RT "Mitochondrial Lineages of the Beluga Whale Delphinapterus leucas in the
RT Russian Arctic.";
RL Biol. Bull. Russ. Acad. Sci. 45:147-154(2018).
RN [4] {ECO:0000313|EMBL:QJH88517.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=32315590;
RA Louis M., Skovrind M., Samaniego Castruita J.A., Garilao C., Kaschner K.,
RA Gopalakrishnan S., Haile J.S., Lydersen C., Kovacs K.M., Garde E.,
RA Heide-Jorgensen M.P., Postma L., Ferguson S.H., Willerslev E.,
RA Lorenzen E.D.;
RT "Influence of past climate change on phylogeography and demographic history
RT of narwhals, Monodon monoceros.";
RL Proc. R. Soc. B 287:0-20192964(2020).
RN [5] {ECO:0000313|RefSeq:YP_009352188.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00002566,
CC ECO:0000256|RuleBase:RU362117}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|RuleBase:RU362117};
CC Note=Binds 2 heme groups non-covalently.
CC {ECO:0000256|RuleBase:RU362117};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR038885-2};
CC Note=Binds 2 heme groups non-covalently.
CC {ECO:0000256|PIRSR:PIRSR038885-2};
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:0000256|ARBA:ARBA00011088}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004448}.
CC -!- SIMILARITY: Belongs to the cytochrome b family.
CC {ECO:0000256|RuleBase:RU362117}.
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; KY444734; AQX44357.1; -; Genomic_DNA.
DR EMBL; MF919069; AVY83262.1; -; Genomic_DNA.
DR EMBL; MT251225; QJH88517.1; -; Genomic_DNA.
DR RefSeq; YP_009352188.1; NC_034236.1.
DR STRING; 9749.A0A1S6YGE8; -.
DR Ensembl; ENSDLET00000000036; ENSDLEP00000000014; ENSDLEG00000000036.
DR KEGG; dle:31412994; -.
DR OrthoDB; 232320at2759; -.
DR Proteomes; UP000248483; Mitochondrion MT.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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 {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|RuleBase:RU362117};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038885-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038885-2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362117};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR038885-2};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU362117};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660,
KW ECO:0000256|RuleBase:RU362117};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362117};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362117};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362117};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075}.
FT TRANSMEM 30..56
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 77..98
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 140..158
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 178..200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 229..246
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 288..307
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 319..338
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 350..372
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT DOMAIN 1..209
FT /note="Cytochrome b/b6 N-terminal region profile"
FT /evidence="ECO:0000259|PROSITE:PS51002"
FT DOMAIN 210..379
FT /note="Cytochrome b/b6 C-terminal region profile"
FT /evidence="ECO:0000259|PROSITE:PS51003"
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:0000256|PIRSR:PIRSR038885-2"
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:0000256|PIRSR:PIRSR038885-2"
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:0000256|PIRSR:PIRSR038885-2"
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:0000256|PIRSR:PIRSR038885-2"
FT BINDING 201
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000256|PIRSR:PIRSR038885-1"
SQ SEQUENCE 379 AA; 42793 MW; 2C8C9BB0D4F1B8C0 CRC64;
MTNIRKTHPL MKILNNAFID LPTPSNISSW WNFGSLLGLC LIMQILTGLF LAMHYTPDTS
TAFSSVAHIC RDVNYGWIIR YLHANGASMF FICLYTHIGR SLYYGSHTSQ ETWNIGVLLL
LMVMATAFVG YVLPWGQMSF WGATVITNLL SAIPYIGNTL VEWIWGGFSV DKATLTRFFT
FHFILPFIIT ALVAVHLLFL HETGSNNPTG IPSNMDTIPF HPYYTIKDIL GALLLILTLL
TVTLFTPDLL GDPDNYTPAN PLNTPAHIKP EWYFLFAYTI LRSIPNKLGG VLALLLSILI
LLFIPMLQTS KQRSMMFRPL SQLLFWTLIA DFLILTWIGG QPVEHPYITV GQLASILYFL
LILVLMPVAS LIENKLLKW
//
