SQE1_PANGI
ID SQE1_PANGI Reviewed; 539 AA.
AC O48651; A0A0N7APM2; Q75W20;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Squalene monooxygenase SE1 {ECO:0000303|Ref.1};
DE EC=1.14.14.17 {ECO:0000250|UniProtKB:Q9SM02};
DE AltName: Full=Squalene epoxidase 1 {ECO:0000303|PubMed:19857882, ECO:0000303|PubMed:29509695, ECO:0000303|Ref.1, ECO:0000303|Ref.2};
DE Short=PgSQE1 {ECO:0000303|PubMed:19857882, ECO:0000303|PubMed:29509695};
DE Short=SE {ECO:0000303|Ref.1, ECO:0000303|Ref.2};
DE Short=SE1 {ECO:0000303|PubMed:19857882};
DE Short=gse {ECO:0000303|PubMed:15493471};
GN Name=SQE1 {ECO:0000303|PubMed:19857882, ECO:0000303|PubMed:29509695};
GN Synonyms=GSE {ECO:0000303|PubMed:15493471},
GN SE {ECO:0000303|PubMed:30577538, ECO:0000303|Ref.1, ECO:0000303|Ref.2},
GN SQE {ECO:0000303|PubMed:15821288};
OS Panax ginseng (Korean ginseng).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Araliaceae; Panax.
OX NCBI_TaxID=4054;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Suzuki H.;
RT "Isolation and characterization of a cDNA encoding the squalene epoxidase
RT from Panax ginseng.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Leaf;
RA In J.-G., Yang D.C., Lee B.S.;
RT "Isolation and characterization of squalene epoxidase in Panax ginseng.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Hou S., Han M., Liu C., Yang L.;
RT "Cloning and expression analysis of HMGR, SS, SE, DS, and bAS genes in
RT Panax ginseng.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INDUCTION BY OLIGOGALACTURONIC ACID; HYDROGEN PEROXIDE AND JASMONIC ACID.
RX DOI=10.1034/j.1399-3054.2003.00124.x;
RA Hu X., Neill S., Cai W., Tang Z.;
RT "Hydrogen peroxide and jasmonic acid mediate oligogalacturonic acid-induced
RT saponin accumulation in suspension-cultured cells of Panax ginseng.";
RL Physiol. Plantarum 118:414-421(2003).
RN [5]
RP INDUCTION BY METYL JASMONATE.
RC STRAIN=cv. Chunpoong; TISSUE=Leaf;
RX PubMed=15356323; DOI=10.1093/pcp/pch126;
RA Lee M.-H., Jeong J.-H., Seo J.-W., Shin C.-G., Kim Y.-S., In J.-G.,
RA Yang D.-C., Yi J.-S., Choi Y.-E.;
RT "Enhanced triterpene and phytosterol biosynthesis in Panax ginseng
RT overexpressing squalene synthase gene.";
RL Plant Cell Physiol. 45:976-984(2004).
RN [6]
RP INDUCTION BY CHITOSAN.
RX PubMed=15493471; DOI=10.1360/03yc0074;
RA Hu X., Neill S.J., Fang J., Cai W., Tang Z.;
RT "Mitogen-activated protein kinases mediate the oxidative burst and saponin
RT synthesis induced by chitosan in cell cultures of Panax ginseng.";
RL Sci. China, Ser. C, Life Sci. 47:303-312(2004).
RN [7]
RP INDUCTION BY CLE; ETHYLENE; ROSE BENGAL; NITRIC OXIDE AND HYDROGEN
RP PEROXIDE.
RX PubMed=15821288; DOI=10.1093/pcp/pci103;
RA Xu X., Hu X., Neill S.J., Fang J., Cai W.;
RT "Fungal elicitor induces singlet oxygen generation, ethylene release and
RT saponin synthesis in cultured cells of Panax ginseng C. A. Meyer.";
RL Plant Cell Physiol. 46:947-954(2005).
RN [8]
RP INDUCTION BY METHYL JASMONATE.
RX PubMed=15538577; DOI=10.1007/s00299-004-0845-4;
RA Choi D.-W., Jung J., Ha Y.I., Park H.-W., In D.S., Chung H.-J., Liu J.R.;
RT "Analysis of transcripts in methyl jasmonate-treated ginseng hairy roots to
RT identify genes involved in the biosynthesis of ginsenosides and other
RT secondary metabolites.";
RL Plant Cell Rep. 23:557-566(2005).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY METHYL
RP JASMONATE AND SQUALENE.
RX PubMed=19857882; DOI=10.1016/j.phytochem.2009.09.031;
RA Han J.-Y., In J.-G., Kwon Y.-S., Choi Y.-E.;
RT "Regulation of ginsenoside and phytosterol biosynthesis by RNA
RT interferences of squalene epoxidase gene in Panax ginseng.";
RL Phytochemistry 71:36-46(2010).
RN [10]
RP INDUCED BY HEAVY METAL STRESS.
RX PubMed=23232757; DOI=10.1007/s00128-012-0891-5;
RA Balusamy S.R.D., Kim Y.-J., Rahimi S., Senthil K.S., Lee O.R., Lee S.,
RA Yang D.-C.;
RT "Transcript pattern of cytochrome P450, antioxidant and ginsenoside
RT biosynthetic pathway genes under heavy metal stress in Panax ginseng
RT Meyer.";
RL Bull. Environ. Contam. Toxicol. 90:194-202(2013).
RN [11]
RP INDUCTION BY DCCD.
RX PubMed=23467002; DOI=10.1016/j.jbiotec.2013.02.012;
RA Huang C., Qian Z.-G., Zhong J.-J.;
RT "Enhancement of ginsenoside biosynthesis in cell cultures of Panax ginseng
RT by N,N'-dicyclohexylcarbodiimide elicitation.";
RL J. Biotechnol. 165:30-36(2013).
RN [12]
RP GENE FAMILY.
RX PubMed=24198659; DOI=10.5142/jgr.2013.37.332;
RA Kim D.S., Song M., Kim S.-H., Jang D.-S., Kim J.-B., Ha B.-K., Kim S.H.,
RA Lee K.J., Kang S.-Y., Jeong I.Y.;
RT "The improvement of ginsenoside accumulation in Panax ginseng as a result
RT of gamma-irradiation.";
RL J. Ginseng Res. 37:332-340(2013).
RN [13]
RP INDUCTION BY VANADATE.
RX DOI=10.1016/j.procbio.2013.05.019;
RA Huang C., Zhong J.-J.;
RT "Elicitation of ginsenoside biosynthesis in cell cultures of Panax ginseng
RT by vanadate.";
RL Process Biochem. 48:1227-1234(2013).
RN [14]
RP FUNCTION, AND INDUCTION BY ASPERGILLUS NIGER.
RX PubMed=27746309; DOI=10.1016/j.jbiotec.2016.10.011;
RA Li J., Liu S., Wang J., Li J., Liu D., Li J., Gao W.;
RT "Fungal elicitors enhance ginsenosides biosynthesis, expression of
RT functional genes as well as signal molecules accumulation in adventitious
RT roots of Panax ginseng C. A. Mey.";
RL J. Biotechnol. 239:106-114(2016).
RN [15]
RP REVIEW.
RX PubMed=29378087; DOI=10.1002/bab.1649;
RA Lu J., Li J., Wang S., Yao L., Liang W., Wang J., Gao W.;
RT "Advances in ginsenoside biosynthesis and metabolic regulation.";
RL Biotechnol. Appl. Biochem. 65:514-522(2018).
RN [16]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=29509695; DOI=10.3390/molecules23030589;
RA Yang J.-L., Hu Z.-F., Zhang T.-T., Gu A.-D., Gong T., Zhu P.;
RT "Progress on the studies of the key enzymes of ginsenoside biosynthesis.";
RL Molecules 23:0-0(2018).
RN [17]
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND INDUCTION BY ABIOTIC FACTORS.
RX PubMed=30577538; DOI=10.3390/molecules24010014;
RA Zhang T., Han M., Yang L., Han Z., Cheng L., Sun Z., Yang L.;
RT "The effects of environmental factors on ginsenoside biosynthetic enzyme
RT gene expression and saponin abundance.";
RL Molecules 24:0-0(2018).
CC -!- FUNCTION: Component of the triterpene saponins (e.g. ginsenosides or
CC panaxosides) and phytosterols biosynthetic pathways (PubMed:19857882,
CC PubMed:27746309, PubMed:29378087). Catalyzes the first oxygenation step
CC in sterol biosynthesis and is suggested to be one of the rate-limiting
CC enzymes in this pathway (By similarity). {ECO:0000250|UniProtKB:Q9SM02,
CC ECO:0000269|PubMed:19857882, ECO:0000269|PubMed:27746309,
CC ECO:0000303|PubMed:29378087}.
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25283;
CC Evidence={ECO:0000303|PubMed:29509695};
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: Microsome membrane
CC {ECO:0000250|UniProtKB:P32476}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P32476}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P32476}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P32476}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O48651-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O48651-2; Sequence=VSP_060119;
CC -!- TISSUE SPECIFICITY: Mostly expressed in flower buds and leaves, and, to
CC a lower extent, at high levels thought, in roots and petioles
CC (PubMed:19857882, PubMed:30577538). In petioles, preferentially
CC observed in vascular bundle tissue (phloem cells and parenchymatous
CC cells near xylem) and resin ducts (PubMed:19857882).
CC {ECO:0000269|PubMed:19857882, ECO:0000269|PubMed:30577538}.
CC -!- DEVELOPMENTAL STAGE: Rapid decrease in roots and leaves from the leaf
CC opened to the green fruit stage (PubMed:30577538). At the leaf opened
CC stage, accumulates mostly in leaves (PubMed:30577538).
CC {ECO:0000269|PubMed:30577538}.
CC -!- INDUCTION: Induced by jasmonic acid (JA) and methyl jasmonate (MeJA) in
CC adventitious roots (PubMed:15356323, PubMed:15538577, PubMed:19857882,
CC Ref.4). Induced by chitosan (CHN) (PubMed:15493471). Accumulates upon
CC Cle-mediated signaling, an elicitor derived from fungal cell walls of
CC C.lagenarium, thus inducing the accumulation of saponins
CC (PubMed:15821288). Triggered by ethylene (ACC), rose bengal (RB),
CC nitric oxide (NO) (PubMed:15821288). Accumulates in response to
CC hydrogen peroxide (H(2)O(2)) (PubMed:15821288, Ref.4). Accumulates in
CC the presence of squalene (PubMed:19857882). Induced by N,N'-
CC dicyclohexylcarbodiimide (DCCD) in a nitric oxide (NO) dependent manner
CC thus leading to increased ginsenosides accumulation (PubMed:23467002).
CC Induced by A.niger mycelium-derived elicitor, thus improving
CC ginsenosides production in adventitious roots culture
CC (PubMed:27746309). Triggered by vanadate (Ref.13). Stimulated by the
CC plant cell wall-derived elicitor oligogalacturonic acid (Ref.4).
CC Accumulates under heavy metal stress in the presence of CdCl(2)
CC (PubMed:23232757). Influenced in roots by temperature and
CC photosynthetically active radiation (PAR), and in leaves by relative
CC humidity and rain (PubMed:30577538). {ECO:0000269|PubMed:15356323,
CC ECO:0000269|PubMed:15493471, ECO:0000269|PubMed:15538577,
CC ECO:0000269|PubMed:15821288, ECO:0000269|PubMed:19857882,
CC ECO:0000269|PubMed:23232757, ECO:0000269|PubMed:23467002,
CC ECO:0000269|PubMed:27746309, ECO:0000269|PubMed:30577538,
CC ECO:0000269|Ref.13, ECO:0000269|Ref.4}.
CC -!- DISRUPTION PHENOTYPE: Reduced ginsenoside production. Strong up-
CC regulation of squalene epoxidase 2 (SQE2) and cycloartenol synthase
CC (OSCPNX1) expression resulting in an enhanced accumulation of
CC phytosterol (campesterol, stigmasterol and sitosterol).
CC {ECO:0000269|PubMed:19857882}.
CC -!- SIMILARITY: Belongs to the squalene monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AB003516; BAA24448.1; -; mRNA.
DR EMBL; AB122078; BAD15330.1; -; mRNA.
DR EMBL; KJ939265; AJV26446.1; -; mRNA.
DR AlphaFoldDB; O48651; -.
DR SMR; O48651; -.
DR BRENDA; 1.14.99.7; 7895.
DR UniPathway; UPA00767; UER00752.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0009723; P:response to ethylene; IEP:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0010038; P:response to metal ion; IEP:UniProtKB.
DR GO; GO:0002238; P:response to molecule of fungal origin; IEP:UniProtKB.
DR GO; GO:0071731; P:response to nitric oxide; IEP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR GO; GO:1902438; P:response to vanadate(3-); IEP:UniProtKB.
DR GO; GO:0016126; P:sterol biosynthetic process; IMP:UniProtKB.
DR GO; GO:0046246; P:terpene biosynthetic process; IMP:UniProtKB.
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 Alternative splicing; Endoplasmic reticulum; FAD; Flavoprotein;
KW Isoprene biosynthesis; Membrane; Microsome; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..539
FT /note="Squalene monooxygenase SE1"
FT /id="PRO_0000209846"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 84..85
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 104..105
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 112
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 183
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 199
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 361
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 374
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT SITE 146
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT VAR_SEQ 1..8
FT /note="MNSSSSTT -> MNSSSSS (in isoform 2)"
FT /id="VSP_060119"
FT CONFLICT 19..20
FT /note="Missing (in Ref. 2; BAD15330 and 3; AJV26446)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="S -> P (in Ref. 3; AJV26446)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="N -> K (in Ref. 2; BAD15330 and 3; AJV26446)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="C -> R (in Ref. 3; AJV26446)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="G -> A (in Ref. 2; BAD15330 and 3; AJV26446)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="I -> V (in Ref. 2; BAD15330 and 3; AJV26446)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="T -> A (in Ref. 3; AJV26446)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="I -> T (in Ref. 2; BAD15330 and 3; AJV26446)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 539 AA; 59375 MW; 84AC3547EB591502 CRC64;
MNSSSSTTTT DTLHSFMEAS ALLIDQYFLG WIFAFLFGFL LLLNFKRKRE KNNSTEFGTD
DSNGYYTPEN IAGSTDVIIV GAGVAGSALA YTLANDGRRV HVIERDLTEQ DRIVGELLQP
GGYLKLIELG LEDCVNEIDA QRVFGYALYM DGKNTRLSYP LEKFHSDVAG RSFHNGRFVQ
RMREKAASLP NVRMEQGTVT SLVEKKGSVK GVQYKTKDGQ ELSAFAPLTI VCDGCFSNLR
RSLCNPKVEV PSCFVGLILE NIDLPHINHG HVILADPSPI LFYKISSTEI RCLVDVPGQK
VPCISNGELA NYLKTVVAPQ VPKQLYNSFI AAVDKGNIRT MPNRSMPADP HPTPGALLLG
DAFNMRHPLT GGGMTVALSD IVLIRDLLRP LRDLHDSSTL CKYLESFYTL RKPVASTINT
LAGALYKVFC ASPDKARQEM RNACFDYLSL GGICSQGPIA LLSGLNPRPI SLFLHFFAVA
IYGVGRLLIP FPSPKRMWLG ARLILGASGI IFPIIKSEGL RQMFFPAIVP AYYRAPPIH
