ID D3KSX4_CULQU Unreviewed; 135 AA.
AC D3KSX4;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Cytochrome P450 CYP12 family-like protein {ECO:0000313|EMBL:BAI77971.1};
DE Flags: Fragment;
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|EMBL:BAI77971.1};
RN [1] {ECO:0000313|EMBL:BAI77971.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JPal-per {ECO:0000313|EMBL:BAI77971.1};
RA Komagata O., Kasai S., Tomita T.;
RT "Overexpression of cytochrome P450 genes in pyrethroid-resistant Culex
RT quinquefasciatus.";
RL Insect Biochem. Mol. Biol. 40:146-152(2010).
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}.
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; AB454490; BAI77971.1; -; mRNA.
DR AlphaFoldDB; D3KSX4; -.
DR VEuPathDB; VectorBase:CPIJ008980; -.
DR VEuPathDB; VectorBase:CQUJHB010654; -.
DR HOGENOM; CLU_001570_28_0_1; -.
DR InParanoid; D3KSX4; -.
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:InterPro.
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; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24291:SF198; CYTOCHROME P450 302A1; 1.
DR PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022848};
KW Heme {ECO:0000256|PIRSR:PIRSR602403-1};
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023033}.
FT BINDING 134
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:BAI77971.1"
FT NON_TER 135
FT /evidence="ECO:0000313|EMBL:BAI77971.1"
SQ SEQUENCE 135 AA; 15266 MW; 735417528B72C339 CRC64;
VCSILYQLAT RPAEQQKVYE ELRRIMPDPK TPLTIPLLDQ AHYLKAFIKE VLRVYSTVIG
NGRTLQEDTV ICGYRIPKGV QCVFPNLVTG TMEEYVTDAK TFKPERWLKP SQGGTGDNLH
PFASLPYGYG ARMCL
//
