ID   ERG11_BRANA             Reviewed;         506 AA.
AC   O65727;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Squalene monooxygenase 1,1;
DE            EC=1.14.14.17 {ECO:0000250|UniProtKB:Q9SM02};
DE   AltName: Full=Squalene epoxidase 1,1;
DE            Short=SE 1,1;
GN   Name=SQP1,1;
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; AJ005931; CAA06773.1; -; mRNA.
DR   PIR; T07942; T07942.
DR   RefSeq; NP_001302760.1; NM_001315831.1.
DR   AlphaFoldDB; O65727; -.
DR   SMR; O65727; -.
DR   GeneID; 106366016; -.
DR   KEGG; bna:106366016; -.
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..506
FT                   /note="Squalene monooxygenase 1,1"
FT                   /id="PRO_0000209844"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        447..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         57..58
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q14534"
FT   BINDING         77..78
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q14534"
FT   BINDING         85
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q14534"
FT   BINDING         90
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q14534"
FT   BINDING         157
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q14534"
FT   BINDING         173
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q14534"
FT   BINDING         336
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q14534"
FT   BINDING         349
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q14534"
SQ   SEQUENCE   506 AA;  55572 MW;  32C0301F1A66CD13 CRC64;
     MDLAFPHVCL WTLLAFVLTW TVFYVNNRRK KVAKLPDAAT EVRRDGDADV IIVGAGVGGS
     ALAYALAKDG RRVHVIERDM REPVRMMGEF MQPGGRLLLS KLGLEDCLEG IDEQIATGLA
     VYKDGQKALV SFPEDNDFPY EPTGRAFYNG RFVQRLRQKA SSLPTVQLEE GTVKSLIEEK
     GVIKGVTYKN SAGEETTAFA PLTVVCDGCY SNLRRSVNDN NAEVISYQVG YVSKNCQLED
     PEKLKLIMSK PSFTMLYQIS STDVRCVMEI FPGNIPSISN GEMAVYLKNT MAPQVPPELR
     KIFLKGIDEG AQIKAMPTKR MEATLSEKQG VIVLGDAFNM RHPAIASGMM VVLSDILILR
     RLLQPLRNLS DANKVSEVIK SFYVIRKPMS ATVNTLGNAF SQVLIASTDE AKEAMRQGCF
     DYLSSGGFRT SGMMALLGGM NPRPLSLIFH LCGITLSSIG QLLSPFPSPL GIWHSLRLFG
     AEGVSQMLSP AYAAAYRKSY MTATAL