ID   ERG12_BRANA             Reviewed;         518 AA.
AC   O65726;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Squalene monooxygenase 1,2;
DE            EC=1.14.14.17 {ECO:0000250|UniProtKB:Q9SM02};
DE   AltName: Full=Squalene epoxidase 1,2;
DE            Short=SE 1,2;
GN   Name=SQP1,2;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Westar; TISSUE=Shoot;
RX   PubMed=10350086; DOI=10.1023/a:1006172120929;
RA   Schafer U.A., Reed D.W., Hunter D.G., Yao K., Weninger A.M., Tsang E.W.T.,
RA   Reaney M.J.T., MacKenzie S.L., Covello P.S.;
RT   "An example of intron junctional sliding in the gene families encoding
RT   squalene monooxygenase homologues in Arabidopsis thaliana and Brassica
RT   napus.";
RL   Plant Mol. Biol. 39:721-728(1999).
CC   -!- FUNCTION: Catalyzes the stereospecific oxidation of squalene to (S)-
CC       2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in
CC       steroid biosynthesis. {ECO:0000250|UniProtKB:Q9SM02}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + reduced [NADPH--hemoprotein reductase] + squalene = (S)-
CC         2,3-epoxysqualene + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:25282, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15440, ChEBI:CHEBI:15441, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; EC=1.14.14.17;
CC         Evidence={ECO:0000250|UniProtKB:Q9SM02};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q14534};
CC   -!- PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from
CC       farnesyl diphosphate: step 2/3.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the squalene monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ005928; CAA06770.1; -; mRNA.
DR   PIR; T07940; T07940.
DR   RefSeq; NP_001302490.2; NM_001315561.2.
DR   AlphaFoldDB; O65726; -.
DR   SMR; O65726; -.
DR   GeneID; 106415877; -.
DR   KEGG; bna:106415877; -.
DR   UniPathway; UPA00767; UER00752.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004506; F:squalene monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016126; P:sterol biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR013698; Squalene_epoxidase.
DR   InterPro; IPR040125; Squalene_monox.
DR   PANTHER; PTHR10835; PTHR10835; 1.
DR   Pfam; PF08491; SE; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Membrane; Oxidoreductase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..518
FT                   /note="Squalene monooxygenase 1,2"
FT                   /id="PRO_0000209845"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        448..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         58..59
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q14534"
FT   BINDING         78..79
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q14534"
FT   BINDING         86
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q14534"
FT   BINDING         91
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q14534"
FT   BINDING         158
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q14534"
FT   BINDING         174
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q14534"
FT   BINDING         337
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q14534"
FT   BINDING         350
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q14534"
SQ   SEQUENCE   518 AA;  57400 MW;  A39E6A5EB5752E9F CRC64;
     MDMAFVEVCL RMLLVFVLSW TIFHVNNRKK KKATKLADLA TEERKEGGPD VIIVGAGVGG
     SALAYALAKD GRRVHVIERD MREPVRMMGE FMQPGGRLML SKLGLQDCLE EIDAQKSTGI
     RLFKDGKETV ACFPVDTNFP YEPSGRFFHN GRFVQRLRQK ASSLPNVRLE EGTVRSLIEE
     KGVVKGVTYK NSSGEETTSF APLTVVCDGC HSNLRRSLND NNAEVTAYEI GYISRNCRLE
     QPDKLHLIMA KPSFAMLYQV SSTDVRCNFE LLSKNLPSVS NGEMTSFVRN SIAPQVPLKL
     RKTFLKGLDE GSHIKITQAK RIPATLSRKK GVIVLGDAFN MRHPVIASGM MVLLSDILIL
     SRLLKPLGNL GDENKVSEVM KSFYALRKPM SATVNTLGNS FWQVLIASTD EAKEAMRQGC
     FDYLSSGGFR TSGLMALIGG MNPRPLSLFY HLFVISLSSI GQLLSPFPTP LRVWHSLRLL
     DLSLKMLVPH LKAEGIGQML SPTNAAAYRK SYMAATVV