SQS1_PANGI
ID SQS1_PANGI Reviewed; 415 AA.
AC O48666; A0A1P7Y098; B1PX80;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Squalene synthase 1 {ECO:0000303|PubMed:15356323, ECO:0000303|PubMed:29509695};
DE Short=PgSS {ECO:0000303|PubMed:15493471};
DE Short=PgSS1 {ECO:0000303|PubMed:15356323, ECO:0000303|PubMed:29509695};
DE Short=PgssA {ECO:0000303|Ref.3};
DE Short=SQS 1 {ECO:0000305};
DE Short=SQS 4 {ECO:0000303|PubMed:25642758, ECO:0000303|Ref.4};
DE EC=2.5.1.21 {ECO:0000250|UniProtKB:P53799};
DE AltName: Full=FPP:FPP farnesyltransferase SS1 {ECO:0000305};
DE AltName: Full=Farnesyl-diphosphate farnesyltransferase SS1 {ECO:0000305};
GN Name=SS1 {ECO:0000303|PubMed:15356323, ECO:0000303|PubMed:29509695};
GN Synonyms=GSS {ECO:0000303|PubMed:15493471},
GN PSS {ECO:0000303|PubMed:15356323}, SQS {ECO:0000303|PubMed:15821288},
GN SS {ECO:0000303|PubMed:30577538, ECO:0000303|Ref.4},
GN SS4 {ECO:0000303|PubMed:25642758}, ssA {ECO:0000303|Ref.3};
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 synthase
RT from Panax ginseng.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION BY METHYL 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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Leaf;
RA Zhao L., Fu Q., Wang L.S.;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND INDUCTION BY METHYL
RP JASMONATE.
RC STRAIN=cv. Damaya;
RX PubMed=25642758; DOI=10.3390/ijms16023035;
RA Cao H., Nuruzzaman M., Xiu H., Huang J., Wu K., Chen X., Li J., Wang L.,
RA Jeong J.-H., Park S.-J., Yang F., Luo J., Luo Z.;
RT "Transcriptome analysis of methyl jasmonate-elicited Panax ginseng
RT adventitious roots to discover putative ginsenoside biosynthesis and
RT transport genes.";
RL Int. J. Mol. Sci. 16:3035-3057(2015).
RN [6]
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 [7]
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 [8]
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 [9]
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 [10]
RP INDUCTION BY METHYL JASMONATE.
RX DOI=10.1007/s11240-009-9535-9;
RA Kim O.T., Bang K.H., Kim Y.C., Hyun D.Y., Kim M.Y., Cha S.W.;
RT "Upregulation of ginsenoside and gene expression related to triterpene
RT biosynthesis in ginseng hairy root cultures elicited by methyl jasmonate.";
RL Plant Cell Tissue Organ Cult. 98:25-33(2009).
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 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 [13]
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 [14]
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 [15]
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 [16]
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:15356323,
CC PubMed:27746309, PubMed:29378087). Catalyzes the biosynthesis of
CC squalene (PubMed:15356323). {ECO:0000269|PubMed:15356323,
CC ECO:0000269|PubMed:27746309, ECO:0000303|PubMed:29378087}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate +
CC NAD(+) + squalene; Xref=Rhea:RHEA:32299, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:175763; EC=2.5.1.21;
CC Evidence={ECO:0000250|UniProtKB:P53799};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32300;
CC Evidence={ECO:0000303|PubMed:29509695};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADPH = 2 diphosphate
CC + NADP(+) + squalene; Xref=Rhea:RHEA:32295, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:175763; EC=2.5.1.21;
CC Evidence={ECO:0000250|UniProtKB:P53799};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32296;
CC Evidence={ECO:0000303|PubMed:29509695};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P53799};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P53799};
CC -!- PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from
CC farnesyl diphosphate: step 1/3. {ECO:0000250|UniProtKB:P53799}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P53799}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O48666-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O48666-2; Sequence=VSP_060120;
CC -!- TISSUE SPECIFICITY: Mostly expressed in the shoot apex (buds) and
CC roots, and, to a lower extent, in stems, leaves, flowers and seeds.
CC {ECO:0000269|PubMed:15356323, ECO:0000269|PubMed:30577538}.
CC -!- DEVELOPMENTAL STAGE: Rapid decrease in leaves from the leaf opened to
CC the green fruit stage (PubMed:30577538). At the leaf opened stage,
CC 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:25642758, Ref.6,
CC PubMed:15538577, Ref.10). Induced by chitosan (CHN) (PubMed:15493471).
CC Accumulates upon Cle-mediated signaling, an elicitor derived from
CC fungal cell walls of C.lagenarium, thus inducing the accumulation of
CC saponins (PubMed:15821288). Triggered by ethylene (ACC), rose bengal
CC (RB), nitric oxide (NO) (PubMed:15821288). Accumulates in response to
CC hydrogen peroxide (H(2)O(2)) (PubMed:15821288, Ref.6). 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.12). Stimulated by the
CC plant cell wall-derived elicitor oligogalacturonic acid (Ref.6).
CC Influenced in roots by photosynthetically active radiation (PAR), and
CC in leaves by relative humidity (PubMed:30577538).
CC {ECO:0000269|PubMed:15356323, ECO:0000269|PubMed:15493471,
CC ECO:0000269|PubMed:15538577, ECO:0000269|PubMed:15821288,
CC ECO:0000269|PubMed:23467002, ECO:0000269|PubMed:25642758,
CC ECO:0000269|PubMed:27746309, ECO:0000269|PubMed:30577538,
CC ECO:0000269|Ref.10, ECO:0000269|Ref.12, ECO:0000269|Ref.6}.
CC -!- SIMILARITY: Belongs to the phytoene/squalene synthase family.
CC {ECO:0000305}.
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DR EMBL; AB010148; BAA24289.1; -; mRNA.
DR EMBL; AB115496; BAD08242.1; -; mRNA.
DR EMBL; EU502717; ACA66014.1; -; mRNA.
DR EMBL; KJ939264; AJV26445.1; -; mRNA.
DR EMBL; KP689314; AJK30626.1; -; mRNA.
DR AlphaFoldDB; O48666; -.
DR SMR; O48666; -.
DR BioCyc; MetaCyc:MON-13442; -.
DR BRENDA; 2.5.1.21; 7895.
DR UniPathway; UPA00767; UER00751.
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:0004310; F:farnesyl-diphosphate farnesyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0051996; F:squalene synthase 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: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:0016135; P:saponin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016104; P:triterpenoid biosynthetic process; IDA:UniProtKB.
DR CDD; cd00683; Trans_IPPS_HH; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR002060; Squ/phyt_synthse.
DR InterPro; IPR006449; Squal_synth-like.
DR InterPro; IPR019845; Squalene/phytoene_synthase_CS.
DR InterPro; IPR044844; Trans_IPPS_euk-type.
DR InterPro; IPR033904; Trans_IPPS_HH.
DR PANTHER; PTHR11626; PTHR11626; 1.
DR Pfam; PF00494; SQS_PSY; 1.
DR SFLD; SFLDG01018; Squalene/Phytoene_Synthase_Lik; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR TIGRFAMs; TIGR01559; squal_synth; 1.
DR PROSITE; PS01044; SQUALEN_PHYTOEN_SYN_1; 1.
DR PROSITE; PS01045; SQUALEN_PHYTOEN_SYN_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Isoprene biosynthesis;
KW Magnesium; Membrane; Multifunctional enzyme; NADP; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..415
FT /note="Squalene synthase 1"
FT /id="PRO_0000446952"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 410..415
FT /note="LLLNKQ -> LPNSL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_060120"
FT CONFLICT 104
FT /note="K -> N (in Ref. 5; AJK30626)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="S -> P (in Ref. 3; ACA66014)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="I -> V (in Ref. 3; ACA66014)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 47056 MW; 2576E2F0DDCE51F7 CRC64;
MGSLGAILKH PEDFYPLLKL KFAARHAEKQ IPPEPHWAFC YSMLHKVSRS FGLVIQQLGP
QLRDAVCIFY LVLRALDTVE DDTSIPTEVK VPILMAFHRH IYDKDWHFSC GTKEYKVLMD
EFHHVSNAFL ELGSGYQEAI EDITMRMGAG MAKFICKEVE TINDYDEYCH YVAGLVGLGL
SKLFHASGAE DLATDSLSNS MGLFLQKTNI IRDYLEDINE IPKSRMFWPR QIWSKYVDKL
EDLKYEENSA KAVQCLNDMV TDALVHAEDC LKYMSDLRGP AIFRFCAIPQ IMAIGTLALC
FNNTQVFRGV VKMRRGLTAK VIDQTKTMSD VYGAFFDFSC LLKSKVDNND PNATKTLSRL
EAIQKTCKES GTLSKRKSYI IESESGHNSA LIAIIFIILA ILYAYLSSNL LLNKQ
