ERG14_ARATH
ID ERG14_ARATH Reviewed; 531 AA.
AC Q9SM02; G1JSH7; Q9C649;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Squalene epoxidase 1;
DE Short=AtSQE1;
DE EC=1.14.14.17 {ECO:0000269|PubMed:17426032};
DE AltName: Full=Protein DROUGHT HYPERSENSITIVE 2;
DE AltName: Full=Squalene monooxygenase;
DE AltName: Full=XF1 protein;
GN Name=SQE1; Synonyms=DRY2, XF1; OrderedLocusNames=At1g58440;
GN ORFNames=F9K23.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=10548732; DOI=10.1016/s0378-1119(99)00403-5;
RA Kato A., Suzuki M., Kuwahara A., Ooe H., Higano-Inaba K., Komeda Y.;
RT "Isolation and analysis of cDNA within a 300 kb Arabidopsis thaliana
RT genomic region located around the 100 map unit of chromosome 1.";
RL Gene 239:309-316(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21810963; DOI=10.1104/pp.111.181990;
RA Guo Y.-L., Fitz J., Schneeberger K., Ossowski S., Cao J., Weigel D.;
RT "Genome-wide comparison of nucleotide-binding site-leucine-rich repeat-
RT encoding genes in Arabidopsis.";
RL Plant Physiol. 157:757-769(2011).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17426032; DOI=10.1074/jbc.m611831200;
RA Rasbery J.M., Shan H., LeClair R.J., Norman M., Matsuda S.P., Bartel B.;
RT "Arabidopsis thaliana squalene epoxidase 1 is essential for root and seed
RT development.";
RL J. Biol. Chem. 282:17002-17013(2007).
RN [7]
RP FUNCTION, MUTAGENESIS OF GLY-183, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=19309460; DOI=10.1111/j.1365-313x.2009.03849.x;
RA Pose D., Castanedo I., Borsani O., Nieto B., Rosado A., Taconnat L.,
RA Ferrer A., Dolan L., Valpuesta V., Botella M.A.;
RT "Identification of the Arabidopsis dry2/sqe1-5 mutant reveals a central
RT role for sterols in drought tolerance and regulation of reactive oxygen
RT species.";
RL Plant J. 59:63-76(2009).
RN [8]
RP FUNCTION.
RX PubMed=19847116; DOI=10.4161/psb.4.9.9425;
RA Pose D., Botella M.A.;
RT "Analysis of the arabidopsis dry2/sqe1-5 mutant suggests a role for sterols
RT in signaling.";
RL Plant Signal. Behav. 4:873-874(2009).
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. Can produce not only oxidosqualene, but also
CC 2,3:22,23-dioxidosqualene. Main squalene epoxidase in the root. Sqe1
CC mutants may show defects in membrane lipid rafts, impairing the correct
CC localization of RHD2 NADPH oxidase and the proper polarized production
CC of ROS. {ECO:0000269|PubMed:17426032, ECO:0000269|PubMed:19309460,
CC ECO:0000269|PubMed:19847116}.
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:0000269|PubMed:17426032};
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 -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves, stems,
CC inflorescences, sepals, style and siliques. Expressed in expanded
CC cotyledons, root tips and cortical cells of the root elongation zone,
CC but not in root hair cells. In leaves, expressed in most cells, with a
CC very strong expression in stomata. {ECO:0000269|PubMed:17426032,
CC ECO:0000269|PubMed:19309460}.
CC -!- DISRUPTION PHENOTYPE: Non viable, sterile dwarf plants with short,
CC highly branched roots. {ECO:0000269|PubMed:17426032}.
CC -!- MISCELLANEOUS: SEQ4 or SEQ5 are unable to complement seq1 mutants.
CC {ECO:0000305|PubMed:17426032}.
CC -!- SIMILARITY: Belongs to the squalene monooxygenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50645.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEM36345.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB008021; BAA88268.1; -; mRNA.
DR EMBL; AB077822; BAB83875.1; -; Genomic_DNA.
DR EMBL; AC082643; AAG50645.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33549.1; -; Genomic_DNA.
DR EMBL; JN389445; AEM36345.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY099643; AAM20494.1; -; mRNA.
DR EMBL; BT000239; AAN15558.1; -; mRNA.
DR PIR; C96618; C96618.
DR PIR; T52462; T52462.
DR RefSeq; NP_564734.1; NM_104624.4.
DR AlphaFoldDB; Q9SM02; -.
DR SMR; Q9SM02; -.
DR STRING; 3702.AT1G58440.1; -.
DR iPTMnet; Q9SM02; -.
DR PaxDb; Q9SM02; -.
DR PRIDE; Q9SM02; -.
DR ProteomicsDB; 220573; -.
DR EnsemblPlants; AT1G58440.1; AT1G58440.1; AT1G58440.
DR GeneID; 842213; -.
DR Gramene; AT1G58440.1; AT1G58440.1; AT1G58440.
DR KEGG; ath:AT1G58440; -.
DR Araport; AT1G58440; -.
DR TAIR; locus:2037660; AT1G58440.
DR eggNOG; KOG1298; Eukaryota.
DR HOGENOM; CLU_026390_1_0_1; -.
DR InParanoid; Q9SM02; -.
DR OMA; KSKFWGL; -.
DR OrthoDB; 583514at2759; -.
DR PhylomeDB; Q9SM02; -.
DR BioCyc; ARA:AT1G58440-MON; -.
DR BioCyc; MetaCyc:AT1G58440-MON; -.
DR BRENDA; 1.14.14.17; 399.
DR UniPathway; UPA00767; UER00752.
DR PRO; PR:Q9SM02; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SM02; baseline and differential.
DR Genevisible; Q9SM02; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0009723; P:response to ethylene; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0016126; P:sterol biosynthetic process; IMP:TAIR.
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 1: Evidence at protein level;
KW FAD; Flavoprotein; Membrane; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..531
FT /note="Squalene epoxidase 1"
FT /id="PRO_0000422763"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 70..71
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 90..91
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 98
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 169
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 185
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 347
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 360
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT SITE 132
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT MUTAGEN 183
FT /note="G->R: In dry2/seq1-5; extreme sensitivity to
FT dehydration and ectopic localization of RHD2 NADPH oxidase
FT and ROS production."
FT /evidence="ECO:0000269|PubMed:19309460"
SQ SEQUENCE 531 AA; 58175 MW; A515A977728AFC8A CRC64;
MESQLWNWIL PLLISSLLIS FVAFYGFFVK PKRNGLRHDR KTVSTVTSDV GSVNITGDTV
ADVIVVGAGV AGSALAYTLG KDKRRVHVIE RDLSEPDRIV GELLQPGGYL KLLELGIEDC
VEEIDAQRVY GYALFKNGKR IRLAYPLEKF HEDVSGRSFH NGRFIQRMRE KAASLPNVQL
EQGTVLSLLE ENGTIKGVRY KNKAGEEQTA FAALTIVCDG CFSNLRRSLC NPQVEVPSCF
VGLVLENCNL PYANHGHVVL ADPSPILMYP ISSTEVRCLV DVPGQKVPSI ANGEMKNYLK
TVVAPQMPHE VYDSFIAAVD KGNIKSMPNR SMPASPYPTP GALLMGDAFN MRHPLTGGGM
TVALADIVVL RNLLRPLRDL SDGASLCKYL ESFYTLRKPV AATINTLANA LYQVFCSSEN
EARNEMREAC FDYLGLGGMC TSGPVSLLSG LNPRPLTLVC HFFAVAVYGV IRLLIPFPSP
KRIWLGAKLI SGASGIIFPI IKAEGVRQMF FPATVPAYYY KAPTVGETKC S
