ID Q5XM76_ANOGA Unreviewed; 105 AA.
AC Q5XM76;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:AAV28177.1};
DE Flags: Fragment;
GN Name=CYP9J3 {ECO:0000313|EMBL:AAV28177.1};
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165 {ECO:0000313|EMBL:AAV28177.1};
RN [1] {ECO:0000313|EMBL:AAV28177.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15753317; DOI=10.1073/pnas.0409348102;
RA David J.-P., Strode C., Vontas J., Nikou D., Vaughan A., Pignatelli P.M.,
RA Louis C., Hemingway J., Ranson H.;
RT "The Anopheles gambiae detoxification chip: a highly specific microarray to
RT study metabolic-based insecticide resistance in malaria vectors.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4080-4084(2005).
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 ECO:0000256|PIRSR:PIRSR602403-1};
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; AY748829; AAV28177.1; -; mRNA.
DR AlphaFoldDB; Q5XM76; -.
DR SMR; Q5XM76; -.
DR HOGENOM; CLU_001570_5_2_1; -.
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 Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
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; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022848};
KW Heme {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Microsome {ECO:0000256|ARBA:ARBA00022848};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000461}.
FT BINDING 98
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR602403-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAV28177.1"
FT NON_TER 105
FT /evidence="ECO:0000313|EMBL:AAV28177.1"
SQ SEQUENCE 105 AA; 12054 MW; C359FC133C508EBF CRC64;
LQSLPYLDMV VSETLRRWPI ATVLNRECVR NYQYDDGQGT RFTIEKGTLV FIPVVGIHFD
PKYFPEPERF DPERFSAANR NNIQPGTYLP FGAGPRNCIG SRFAL
//
