ID Q94SG9_GASAC Unreviewed; 380 AA.
AC Q94SG9;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531, ECO:0000256|RuleBase:RU362117};
GN Name=Cyt b {ECO:0000313|EMBL:BAB70364.1};
GN Synonyms=cytb {ECO:0000313|EMBL:BAW32847.1};
OS Gasterosteus aculeatus (Three-spined stickleback).
OG Mitochondrion {ECO:0000313|EMBL:BAB70364.1,
OG ECO:0000313|Ensembl:ENSGACP00000027672.1}.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|EMBL:BAB70364.1};
RN [1] {ECO:0000313|EMBL:BAB70364.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11606696;
RA Miya M., Kawaguchi A., Nishida M.;
RT "Mitogenomic exploration of higher teleostean phylogenies: a case study for
RT moderate-scale evolutionary genomics with 38 newly determined complete
RT mitochondrial DNA sequences.";
RL Mol. Biol. Evol. 18:1993-2009(2001).
RN [2] {ECO:0000313|Ensembl:ENSGACP00000027672.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:BAW32847.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26997522; DOI=10.1016/j.ympev.2016.03.022;
RA Takahashi H., Moller P.R., Shedko S.V., Ramatulla T., Joen S.-R.,
RA Zhang C.-G., Sideleva V.G., Takata K., Sakai H., Goto A., Nishida M.;
RT "Species phylogeny and diversification process of Northeast Asian Pungitius
RT revealed by AFLP and mtDNA markers.";
RL Mol. Phylogenet. Evol. 99:44-52(2016).
RN [4] {ECO:0000313|Ensembl:ENSGACP00000027672.1}
RP IDENTIFICATION.
RG Ensembl;
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 -!- 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}.
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DR EMBL; AP002944; BAB70364.1; -; Genomic_DNA.
DR EMBL; LC108042; BAW32847.1; -; Genomic_DNA.
DR EMBL; LC108085; BAW32890.1; -; Genomic_DNA.
DR STRING; 69293.ENSGACP00000027672; -.
DR Ensembl; ENSGACT00000027746.1; ENSGACP00000027672.1; ENSGACG00000020954.1.
DR eggNOG; KOG4663; Eukaryota.
DR GeneTree; ENSGT00390000017948; -.
DR OMA; NISAWWN; -.
DR TreeFam; TF353088; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000020954; Expressed in diencephalon and 13 other cell types or tissues.
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-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:UP000007635};
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 29..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 145..166
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..250
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 346..366
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..380
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 380 AA; 42285 MW; 4010D2D09DB07FE9 CRC64;
MASLRKTHPL LKIANNALVD LPAPSNISVW WNFGSLLGLC LIIQILTGLF LAMHYTSDIA
TAFSSVGHIC RDVNYGWLIR NLHANGASFF FICIYMHIGR GLYYGSYLYK ETWNIGVVLL
LLVMMTAFVG YVLPWGQMSF WGATVITNLL SAVPYVGNSL VQWIWGGFSV DNATLTRFFA
FHFLFPFVIA GATLVHLLFL HQTGSNNPLG LNSDADKISF HPYFSYKDLL GFAALLIALT
SLALFAPNLL GDPDNFTPAN PLVTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALLASILV
LMVVPILHTS KQRGLTFRPI TQFLFWTLIA DVAILTWIGG MPVEHPFIII GQVASVLYFS
LFLVLYPGAA VMENKMLEWT
//
