PEN4_ARATH
ID PEN4_ARATH Reviewed; 766 AA.
AC Q9FI37; Q0WSZ0; Q7XJ43;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Thalianol synthase 1 {ECO:0000303|PubMed:18356490};
DE Short=AtTHAS1 {ECO:0000303|PubMed:18356490};
DE EC=5.4.99.31 {ECO:0000269|PubMed:15125655};
DE AltName: Full=Oxidosqualene cyclase {ECO:0000303|PubMed:18356490};
DE AltName: Full=Pentacyclic triterpene synthase 4 {ECO:0000303|PubMed:11247608};
DE Short=AtPEN4 {ECO:0000303|PubMed:11247608};
GN Name=THAS1 {ECO:0000303|PubMed:18356490};
GN Synonyms=OSC {ECO:0000303|PubMed:18356490},
GN PEN4 {ECO:0000303|PubMed:11247608};
GN OrderedLocusNames=At5g48010 {ECO:0000312|Araport:AT5G48010};
GN ORFNames=MDN11.9 {ECO:0000312|EMBL:BAB11065.1};
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 [MRNA] (ISOFORM 2).
RA Benveniste P., Nave P., Schaller H.;
RT "Triterpene synthases.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
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 MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION, AND NOMENCLATURE.
RX PubMed=11247608; DOI=10.1023/a:1006476123930;
RA Husselstein-Muller T., Schaller H., Benveniste P.;
RT "Molecular cloning and expression in yeast of 2,3-oxidosqualene-
RT triterpenoid cyclases from Arabidopsis thaliana.";
RL Plant Mol. Biol. 45:75-92(2001).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15125655; DOI=10.1021/ja0318784;
RA Fazio G.C., Xu R., Matsuda S.P.T.;
RT "Genome mining to identify new plant triterpenoids.";
RL J. Am. Chem. Soc. 126:5678-5679(2004).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18356490; DOI=10.1126/science.1154990;
RA Field B., Osbourn A.E.;
RT "Metabolic diversification -- independent assembly of operon-like gene
RT clusters in different plants.";
RL Science 320:543-547(2008).
RN [8]
RP INDUCTION BY GRAVITY AND LIGHT, AND REPRESSION BY CLB.
RC STRAIN=cv. Columbia;
RX PubMed=21252258; DOI=10.1093/jxb/erq468;
RA de Silva K., Laska B., Brown C., Sederoff H.W., Khodakovskaya M.;
RT "Arabidopsis thaliana calcium-dependent lipid-binding protein (AtCLB): a
RT novel repressor of abiotic stress response.";
RL J. Exp. Bot. 62:2679-2689(2011).
CC -!- FUNCTION: Converts oxidosqualene to thalianol.
CC {ECO:0000269|PubMed:15125655, ECO:0000269|PubMed:18356490}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3-epoxysqualene = thalianol; Xref=Rhea:RHEA:26160,
CC ChEBI:CHEBI:15441, ChEBI:CHEBI:52317; EC=5.4.99.31;
CC Evidence={ECO:0000269|PubMed:15125655};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FI37-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FI37-2; Sequence=VSP_036570;
CC -!- TISSUE SPECIFICITY: Expressed primarily in the root epidermis.
CC {ECO:0000269|PubMed:18356490}.
CC -!- INDUCTION: Induced by gravity and light (PubMed:21252258).
CC Transcriptional expression is repressed by CLB (PubMed:21252258).
CC {ECO:0000269|PubMed:21252258}.
CC -!- DISRUPTION PHENOTYPE: Loss of thalianol production in roots.
CC {ECO:0000269|PubMed:18356490}.
CC -!- MISCELLANEOUS: Constitutes with three contiguous genes an operon-like
CC gene cluster that is involved in the thalianol pathway.
CC -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11065.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY327541; AAP92117.1; -; mRNA.
DR EMBL; AB017064; BAB11065.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95609.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95610.1; -; Genomic_DNA.
DR EMBL; AK227776; BAE99758.1; -; mRNA.
DR RefSeq; NP_001078733.1; NM_001085264.2. [Q9FI37-1]
DR RefSeq; NP_199612.3; NM_124175.4. [Q9FI37-2]
DR AlphaFoldDB; Q9FI37; -.
DR SMR; Q9FI37; -.
DR STRING; 3702.AT5G48010.2; -.
DR PaxDb; Q9FI37; -.
DR PRIDE; Q9FI37; -.
DR ProteomicsDB; 236681; -. [Q9FI37-1]
DR EnsemblPlants; AT5G48010.1; AT5G48010.1; AT5G48010. [Q9FI37-2]
DR EnsemblPlants; AT5G48010.2; AT5G48010.2; AT5G48010. [Q9FI37-1]
DR GeneID; 834852; -.
DR Gramene; AT5G48010.1; AT5G48010.1; AT5G48010. [Q9FI37-2]
DR Gramene; AT5G48010.2; AT5G48010.2; AT5G48010. [Q9FI37-1]
DR KEGG; ath:AT5G48010; -.
DR Araport; AT5G48010; -.
DR TAIR; locus:2162672; AT5G48010.
DR eggNOG; KOG0497; Eukaryota.
DR InParanoid; Q9FI37; -.
DR OMA; GKAWLEW; -.
DR OrthoDB; 365003at2759; -.
DR PhylomeDB; Q9FI37; -.
DR BRENDA; 5.4.99.31; 399.
DR PRO; PR:Q9FI37; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FI37; baseline and differential.
DR Genevisible; Q9FI37; AT.
DR GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR GO; GO:0042300; F:beta-amyrin synthase activity; IBA:GO_Central.
DR GO; GO:0051746; F:thalianol synthase activity; IDA:TAIR.
DR GO; GO:0009629; P:response to gravity; IEP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IEP:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0080003; P:thalianol metabolic process; IMP:TAIR.
DR GO; GO:0010263; P:tricyclic triterpenoid biosynthetic process; IDA:TAIR.
DR GO; GO:0016104; P:triterpenoid biosynthetic process; IBA:GO_Central.
DR CDD; cd02892; SQCY_1; 1.
DR InterPro; IPR032696; SQ_cyclase_C.
DR InterPro; IPR032697; SQ_cyclase_N.
DR InterPro; IPR018333; Squalene_cyclase.
DR InterPro; IPR002365; Terpene_synthase_CS.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11764; PTHR11764; 1.
DR Pfam; PF13243; SQHop_cyclase_C; 1.
DR Pfam; PF13249; SQHop_cyclase_N; 1.
DR SFLD; SFLDG01016; Prenyltransferase_Like_2; 1.
DR SUPFAM; SSF48239; SSF48239; 2.
DR TIGRFAMs; TIGR01787; squalene_cyclas; 1.
DR PROSITE; PS01074; TERPENE_SYNTHASES; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isomerase; Reference proteome; Repeat.
FT CHAIN 1..766
FT /note="Thalianol synthase 1"
FT /id="PRO_0000366139"
FT REPEAT 149..190
FT /note="PFTB 1"
FT REPEAT 520..561
FT /note="PFTB 2"
FT REPEAT 646..687
FT /note="PFTB 3"
FT ACT_SITE 491
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P48449"
FT VAR_SEQ 551..566
FT /note="WLSPVEFLEDTIVEYE -> LLNIMIFR (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_036570"
FT CONFLICT 15
FT /note="H -> R (in Ref. 4; BAE99758)"
FT /evidence="ECO:0000305"
FT CONFLICT 755
FT /note="T -> A (in Ref. 4; BAE99758)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 766 AA; 88203 MW; 32D8D3E73A9E0B2C CRC64;
MWRLRTGPKA GEDTHLFTTN NYAGRQIWEF DANAGSPQEI AEVEDARHKF SDNTSRFKTT
ADLLWRMQFL REKKFEQKIP RVIIEDARKI KYEDAKTALK RGLLYFTALQ ADDGHWPAEN
SGPNFYTPPF LICLYITGHL EKIFTPEHVK ELLRHIYNMQ NEDGGWGLHV ESHSVMFCTV
INYVCLRIVG EEVGHDDQRN GCAKAHKWIM DHGGATYTPL IGKALLSVLG VYDWSGCNPI
PPEFWLLPSS FPVNGGTLWI YLRDTFMGLS YLYGKKFVAP PTPLILQLRE ELYPEPYAKI
NWTQTRNRCG KEDLYYPRSF LQDLFWKSVH MFSESILDRW PLNKLIRQRA LQSTMALIHY
HDESTRYITG GCLPKAFHML ACWIEDPKSD YFKKHLARVR EYIWIGEDGL KIQSFGSQLW
DTALSLHALL DGIDDHDVDD EIKTTLVKGY DYLKKSQITE NPRGDHFKMF RHKTKGGWTF
SDQDQGWPVS DCTAESLECC LFFESMPSEL IGKKMDVEKL YDAVDYLLYL QSDNGGIAAW
QPVEGKAWLE WLSPVEFLED TIVEYEYVEC TGSAIAALTQ FNKQFPGYKN VEVKRFITKA
AKYIEDMQTV DGSWYGNWGV CFIYGTFFAV RGLVAAGKTY SNCEAIRKAV RFLLDTQNPE
GGWGESFLSC PSKKYTPLKG NSTNVVQTAQ ALMVLIMGDQ MERDPLPVHR AAQVLINSQL
DNGDFPQQEI MGTFMRTVML HFPTYRNTFS LWALTHYTHA LRRLLP
