ID   C4D10_DROMT             Reviewed;         513 AA.
AC   O18596;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Cytochrome P450 4d10;
DE            EC=1.14.-.-;
DE   AltName: Full=CYPIVD10;
GN   Name=Cyp4d10;
OS   Drosophila mettleri (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7228;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   TISSUE=Larva;
RX   PubMed=9738880; DOI=10.1007/s004380050788;
RA   Danielson P.B., Foster J.L., McMahill M.M., Smith M.K., Fogleman J.C.;
RT   "Induction by alkaloids and phenobarbital of family 4 cytochrome P450s in
RT   Drosophila: evidence for involvement in host plant utilization.";
RL   Mol. Gen. Genet. 259:54-59(1998).
CC   -!- FUNCTION: May play an important role in the maintenance of specific
CC       insect-host plant relationships. May be involved in xenobiotic
CC       metabolism.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Peripheral membrane protein {ECO:0000305}. Microsome membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC   -!- INDUCTION: By isoquinoline alkaloids and phenobarbital.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; U91634; AAB68664.1; -; mRNA.
DR   AlphaFoldDB; O18596; -.
DR   SMR; O18596; -.
DR   FlyBase; FBgn0021345; Dmet\Cyp4d10.
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; -; 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   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase.
FT   CHAIN           1..513
FT                   /note="Cytochrome P450 4d10"
FT                   /id="PRO_0000051836"
FT   BINDING         317
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         457
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:0000250"
SQ   SEQUENCE   513 AA;  58731 MW;  294931CC398B5759 CRC64;
     MSLSLPPLIA VACLVVALAR ISWLPLRSWL RRRRRTHQLA AQLPGPRNLP LLGNFHMFFG
     LEPWQVPHLI NQLAKKYDGT FKLKMGSNFS LMMFQPRDIE VVLGSSQLLD KAVEYSFLRG
     WLNDGLLLSG GRKWHRRRKI ITPAFHFRIL ESYDEIFDRQ TRLLIHKWQQ TLGHSFDLGH
     DVHLFTLDVI CETAMGVSTN AQTNADSDYV RAVKTISTVL HKRMFNIFYR FDLTYMLTPL
     AWAERRALNV LHKFTEKIIV QRREELLRGG VTQTTDGADV GAKSKMVFLD ILLQSNIDDK
     PLTNLDIREE VDTFMFEGHD TTSSGITFFF YNIALYPECQ RKCVEEIVSV LGKDTETPVT
     YDLLNNLNYM DLCIKETLRM YPSVPLLGRK VLQECEINGK IIPAGTNIGI SPLFLGRSED
     ISSEPNTFKP ERFDVVTSAE KLNPHAYIPF SAGPRNCIGQ KFAMLEIKAI AANVLRHYEI
     EFVGNAEESP VLIAELILRT KDPLMFKLKK RVI