ID A0A1S4KJU6_CULQU Unreviewed; 378 AA.
AC A0A1S4KJU6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531};
DE AltName: Full=Complex III subunit 3 {ECO:0000256|ARBA:ARBA00031681};
DE AltName: Full=Complex III subunit III {ECO:0000256|ARBA:ARBA00032600};
DE AltName: Full=Cytochrome b-c1 complex subunit 3 {ECO:0000256|ARBA:ARBA00029812};
DE AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome b subunit {ECO:0000256|ARBA:ARBA00032818};
GN Name=9829914 {ECO:0000313|EnsemblMetazoa:CPIJ040086-PA};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176 {ECO:0000313|EnsemblMetazoa:CPIJ040086-PA, ECO:0000313|Proteomes:UP000002320};
RN [1] {ECO:0000313|EnsemblMetazoa:CPIJ040086-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ040086-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 -!- 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 main subunits of complex b-c1 are: cytochrome b,
CC cytochrome c1 and the Rieske protein. {ECO:0000256|ARBA:ARBA00011649}.
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 ---------------------------------------------------------------------------
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 RefSeq; YP_003934133.1; NC_014574.1.
DR AlphaFoldDB; A0A1S4KJU6; -.
DR EnsemblMetazoa; CPIJ040086-RA; CPIJ040086-PA; CPIJ040086.
DR GeneID; 9829914; -.
DR KEGG; cqu:CYTB; -.
DR CTD; 4519; -.
DR VEuPathDB; VectorBase:CPIJ040086; -.
DR VEuPathDB; VectorBase:CQUJHB007645; -.
DR InParanoid; A0A1S4KJU6; -.
DR OrthoDB; 232320at2759; -.
DR Proteomes; UP000002320; Unassembled WGS sequence.
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 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR038885-2};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Reference proteome {ECO:0000313|Proteomes:UP000002320};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075}.
FT DOMAIN 1..210
FT /note="Cytochrome b/b6 N-terminal region profile"
FT /evidence="ECO:0000259|PROSITE:PS51002"
FT DOMAIN 211..378
FT /note="Cytochrome b/b6 C-terminal region profile"
FT /evidence="ECO:0000259|PROSITE:PS51003"
FT BINDING 84
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 98
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 183
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 197
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 202
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000256|PIRSR:PIRSR038885-1"
SQ SEQUENCE 378 AA; 43263 MW; 19DEDD8A2879FB08 CRC64;
MNKPLRKSHP LISIANNALV DLPAPSNISA WWNFGSLLGL CLVIQILTGL FLAMHYTADI
ETAFNSVNHI YRDVNNGWFL RICHANGASF FFACLFIHVG RGVYYNSYLY IPTWMIGVII
LFMVMATGFL GYVLPWGQMS FWGATVITNL LSAVPYLGTD LVQWIWGGFA VDNATLTRFF
TFHFILPFIV LALTMIHLLF LHQTGSNNPL GLNSNVDKIP FHPYFVYKDI VGFIIFMWIL
IGFIWKFNYL LMDPENFIPA NPLVTPVHIQ PEWYFLFAYA ILRSIPNKLG GVIALVLSIA
ILMILPFTHT SKFRGLQFYP LNQILFWNMV IVASLLTWIG ARPVEDPYVL TGQILTVLYF
SYFIINPLMS KYWDKLLN
//
