ID   CP2F3_CAPHI             Reviewed;         491 AA.
AC   O18809;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Cytochrome P450 2F3;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIF3;
GN   Name=CYP2F3;
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   PubMed=9448722; DOI=10.1006/abbi.1997.0479;
RA   Wang H., Lanza D.L., Yost G.S.;
RT   "Cloning and expression of CYP2F3, a cytochrome P450 that bioactivates the
RT   selective pneumotoxins 3-methylindole and naphthalene.";
RL   Arch. Biochem. Biophys. 349:329-340(1998).
CC   -!- FUNCTION: Bioactivates 3-methylindole (3MI) by dehydrogenation to the
CC       putative electrophile 3-methylene-indolenine. Stereoselectively
CC       catalyzes the formation of the 1R,2S-oxide from naphthalene. Lack
CC       activity with other common P450 substrates including 7-ethoxycoumarin.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC         reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:142491; EC=1.14.14.1;
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- TISSUE SPECIFICITY: Lung specific.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF016293; AAB81719.1; -; mRNA.
DR   RefSeq; NP_001274499.1; NM_001287570.1.
DR   AlphaFoldDB; O18809; -.
DR   SMR; O18809; -.
DR   STRING; 9925.ENSCHIP00000012667; -.
DR   GeneID; 102191547; -.
DR   KEGG; chx:102191547; -.
DR   CTD; 102191547; -.
DR   OrthoDB; 702827at2759; -.
DR   Proteomes; UP000291000; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR020469; Cyt_P450_CYP2_fam.
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; PR01957; EP450ICYP2F.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..491
FT                   /note="Cytochrome P450 2F3"
FT                   /id="PRO_0000051762"
FT   BINDING         436
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   491 AA;  55962 MW;  D5713A214372E541 CRC64;
     MDSISTAILL LILALICLLL TTSSKGKGRL PPGPRALPFL GNLLQLRSQD MLTSLTKLSK
     EFGAVYTVYL GPRRVVVLSG YQAVKEALVD QAEEFSGRGD YPAFFNFTKG NGIAFSNGDR
     WKALRKYSLQ ILRNFGMGKR TIEERILEEG HFLLEELRKT QGKPFDPTFV VSRSVSNIIC
     SVIFGSRFDY DDDRLLTIIH LINENFQIMS SPWGEMYNIF PNLLDWVPGP HRRLFKNYGR
     MKNLIARSVR EHQASLDPNS PRDFIDCFLT KMAQEKQDPL SHFFMDTLLM TTHNLLFGGT
     ETVGTTLRHA FRLLMKYPEV QVRVQEEIDR VVGRERLPTV EDRAEMPYTD AVIHEVQRFA
     DIIPMSLPHR VTRDTNFRGF TIPRGTDVIT LLNTVHYDPS QFLKPKEFNP EHFLDANMSF
     KKSPAFMPFS AGRRLCLGEA LARMELFLYL TAILQSFSLQ PLGAPEDIDL TPLSSGLGNV
     PRPYQLCVRA R