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Database: UniProt
Entry: B0WU75_CULQU
LinkDB: B0WU75_CULQU
Original site: B0WU75_CULQU 
ID   B0WU75_CULQU            Unreviewed;       520 AA.
AC   B0WU75;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Cytochrome P450 9b1 {ECO:0000313|EMBL:EDS34795.1};
GN   Name=6043264 {ECO:0000313|EnsemblMetazoa:CPIJ010203-PA};
GN   ORFNames=CpipJ_CPIJ010203 {ECO:0000313|EMBL:EDS34795.1};
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;
RN   [1] {ECO:0000313|EMBL:EDS34795.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB {ECO:0000313|EMBL:EDS34795.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA   Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:CPIJ010203-PA}
RP   IDENTIFICATION.
RC   STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ010203-PA};
RG   EnsemblMetazoa;
RL   Submitted (FEB-2021) to UniProtKB.
CC   -!- FUNCTION: May be involved in the metabolism of insect hormones and in
CC       the breakdown of synthetic insecticides.
CC       {ECO:0000256|ARBA:ARBA00003690}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004406}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}. Microsome membrane
CC       {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004174}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; DS232101; EDS34795.1; -; Genomic_DNA.
DR   RefSeq; XP_001870910.1; XM_001870875.1.
DR   AlphaFoldDB; B0WU75; -.
DR   STRING; 7176.B0WU75; -.
DR   EnsemblMetazoa; CPIJ010203-RA; CPIJ010203-PA; CPIJ010203.
DR   GeneID; 6043264; -.
DR   KEGG; cqu:CpipJ_CPIJ010203; -.
DR   VEuPathDB; VectorBase:CPIJ010203; -.
DR   VEuPathDB; VectorBase:CQUJHB016715; -.
DR   eggNOG; KOG0158; Eukaryota.
DR   HOGENOM; CLU_001570_5_2_1; -.
DR   InParanoid; B0WU75; -.
DR   OMA; WKGAQPE; -.
DR   OrthoDB; 658605at2759; -.
DR   Proteomes; UP000002320; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   CDD; cd11056; CYP6-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24292:SF104; CYP9F3-RELATED; 1.
DR   PANTHER; PTHR24292; CYTOCHROME P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|RuleBase:RU000461};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000461};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW   ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002320};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        214..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   520 AA;  59973 MW;  9C4B0FF4C9D77436 CRC64;
     MELSYALGLS WLLTAVLLYK WITGSKDFFR NKPIPSVPFF SLRDNTYSLF LKQTDLGAFT
     VHLYNKFAGA KIFGIFDTIK PVFVVRDPEL IKQITVKDFD HFVDRPALFG YSFRDDPYAL
     FSKMLPVLHG ARWRNMRNIL SPAFTGSKMK QMFQLALGCC DNVVQFLNSV QQEQQHGEVE
     MLLKDVTSRY GTDVISCCLF GRKLNSFQDR KNKFYTYGMD MIVLHRIVVV LKMFLIRCFP
     ALAAKIKVDL LDRKHAKYFN AFVDETIEDR TRNNIKGNTL IDMMIEVQLH QQSQESVLPV
     TFTNHEIVAQ LLTLFLAGSG TFQFSSVALI HDLIMNPDVQ QKLYEEILQT QSELGTEKLN
     YDTIQNMKYM EMVTLESMRL HTSFSNAYRH CVKDYTVDDG NGLKFNIHQG SNVWIPILGL
     HMDPKYFPDP KRFDPERFNA ENRPNIHPAT YIPFGAGPRN CVARRFGLMK VKALLYHLLL
     NFSITASPNT PKVLPMNKAF AFLDTVDGDF PVTFKRRQKN
//
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