LUP2_ARATH
ID LUP2_ARATH Reviewed; 763 AA.
AC Q8RWT0; O64552; Q0WLS2; Q56X57; Q84L74;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Amyrin synthase LUP2;
DE EC=5.4.99.39;
DE EC=5.4.99.40;
DE EC=5.4.99.41;
DE AltName: Full=Alpha-amyrin synthase;
DE AltName: Full=Beta-amyrin synthase;
DE AltName: Full=Lupeol synthase 2;
DE Short=AtLUP2;
GN Name=LUP2; OrderedLocusNames=At1g78960; ORFNames=YUP8H12R.43;
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 81-763, FUNCTION, CATALYTIC ACTIVITY, AND
RP NOMENCLATURE.
RC STRAIN=cv. Columbia; TISSUE=Hypocotyl;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 209-763.
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 [6]
RP FUNCTION.
RA Kushiro T., Shibuya M., Masuda K., Ebizuka Y.;
RT "A novel multifunctional triterpene synthase from Arabidopsis thaliana.";
RL Tetrahedron Lett. 41:7705-7710(2000).
CC -!- FUNCTION: Multifunctional enzyme that converts oxidosqualene to nine
CC different triterpenes, mainly lupeol, beta-amyrin and alpha-amyrin in a
CC 15:50:30 ratio. {ECO:0000269|PubMed:11247608, ECO:0000269|Ref.6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3-epoxysqualene = beta-amyrin; Xref=Rhea:RHEA:31007,
CC ChEBI:CHEBI:10352, ChEBI:CHEBI:15441; EC=5.4.99.39;
CC Evidence={ECO:0000269|PubMed:11247608};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3-epoxysqualene = alpha-amyrin; Xref=Rhea:RHEA:31387,
CC ChEBI:CHEBI:10213, ChEBI:CHEBI:15441; EC=5.4.99.40;
CC Evidence={ECO:0000269|PubMed:11247608};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3-epoxysqualene = lupeol; Xref=Rhea:RHEA:31383,
CC ChEBI:CHEBI:6570, ChEBI:CHEBI:15441; EC=5.4.99.41;
CC Evidence={ECO:0000269|PubMed:11247608};
CC -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17070.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD94022.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC002986; AAC17070.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36185.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60689.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60690.1; -; Genomic_DNA.
DR EMBL; AY091131; AAM14080.1; -; mRNA.
DR EMBL; AY114039; AAM45087.1; -; mRNA.
DR EMBL; AF003472; AAC98864.1; -; mRNA.
DR EMBL; AK230119; BAF01935.1; -; mRNA.
DR EMBL; AK221820; BAD94022.1; ALT_INIT; mRNA.
DR PIR; T01059; T01059.
DR RefSeq; NP_001322959.1; NM_001334861.1.
DR RefSeq; NP_001322960.1; NM_001334862.1.
DR RefSeq; NP_178017.2; NM_106545.4.
DR AlphaFoldDB; Q8RWT0; -.
DR SMR; Q8RWT0; -.
DR STRING; 3702.AT1G78960.1; -.
DR PaxDb; Q8RWT0; -.
DR ProteomicsDB; 238785; -.
DR EnsemblPlants; AT1G78960.1; AT1G78960.1; AT1G78960.
DR EnsemblPlants; AT1G78960.2; AT1G78960.2; AT1G78960.
DR EnsemblPlants; AT1G78960.3; AT1G78960.3; AT1G78960.
DR GeneID; 844236; -.
DR Gramene; AT1G78960.1; AT1G78960.1; AT1G78960.
DR Gramene; AT1G78960.2; AT1G78960.2; AT1G78960.
DR Gramene; AT1G78960.3; AT1G78960.3; AT1G78960.
DR KEGG; ath:AT1G78960; -.
DR Araport; AT1G78960; -.
DR TAIR; locus:2207300; AT1G78960.
DR eggNOG; KOG0497; Eukaryota.
DR HOGENOM; CLU_009074_2_0_1; -.
DR InParanoid; Q8RWT0; -.
DR OrthoDB; 365003at2759; -.
DR PhylomeDB; Q8RWT0; -.
DR PRO; PR:Q8RWT0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RWT0; baseline and differential.
DR Genevisible; Q8RWT0; AT.
DR GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR GO; GO:0042300; F:beta-amyrin synthase activity; IDA:TAIR.
DR GO; GO:0042299; F:lupeol synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016104; P:triterpenoid biosynthetic process; IDA:TAIR.
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 SUPFAM; SSF48239; SSF48239; 2.
DR TIGRFAMs; TIGR01787; squalene_cyclas; 1.
DR PROSITE; PS01074; TERPENE_SYNTHASES; 1.
PE 1: Evidence at protein level;
KW Isomerase; Reference proteome; Repeat.
FT CHAIN 1..763
FT /note="Amyrin synthase LUP2"
FT /id="PRO_0000366132"
FT REPEAT 149..190
FT /note="PFTB 1"
FT REPEAT 592..632
FT /note="PFTB 2"
FT REPEAT 641..682
FT /note="PFTB 3"
FT ACT_SITE 486
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P48449"
FT CONFLICT 515
FT /note="L -> S (in Ref. 4; AAC98864)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="A -> P (in Ref. 4; AAC98864)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="Q -> R (in Ref. 4; AAC98864)"
FT /evidence="ECO:0000305"
FT CONFLICT 667
FT /note="E -> G (in Ref. 4; AAC98864)"
FT /evidence="ECO:0000305"
FT CONFLICT 676
FT /note="N -> D (in Ref. 4; AAC98864)"
FT /evidence="ECO:0000305"
FT CONFLICT 686
FT /note="A -> G (in Ref. 4; AAC98864)"
FT /evidence="ECO:0000305"
FT CONFLICT 710..712
FT /note="IIT -> VIS (in Ref. 4; AAC98864)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="Q -> R (in Ref. 4; AAC98864)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="N -> K (in Ref. 4; AAC98864)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 763 AA; 87515 MW; 1D0147DD380FD698 CRC64;
MWKLKIGEGN GEDPYLFSSN NFVGRQTWEF DPKAGTPEER AAVEDARRNY LDNRPRVKGC
SDLLWRMQFL KEAKFEQVIP PVKIDDGEGI TYKNATDALR RAVSFYSALQ SSDGHWPAEI
TGTLFFLPPL VFCFYITGHL EKIFDAEHRK EMLRHIYCHQ NEDGGWGLHI EGKSVMFCTV
LNYICLRMLG EGPNGGRNNA CKRARQWILD HGGVTYIPSW GKIWLSILGI YDWSGTNPMP
PEIWLLPSFF PIHLGKTLCY TRMVYMPMSY LYGKRFVGPL TPLIMLLRKE LHLQPYEEIN
WNKARRLCAK EDMIYPHPLV QDLLWDTLHN FVEPILTNWP LKKLVREKAL RVAMEHIHYE
DENSHYITIG CVEKVLCMLA CWIENPNGDH FKKHLARIPD FMWVAEDGLK MQSFGSQLWD
TVFAIQALLA CDLSDETDDV LRKGHSFIKK SQVRENPSGD FKSMYRHISK GAWTLSDRDH
GWQVSDCTAE ALKCCMLLSM MPAEVVGQKI DPEQLYDSVN LLLSLQGEKG GLTAWEPVRA
QEWLELLNPT DFFTCVMAER EYVECTSAVI QALVLFKQLY PDHRTKEIIK SIEKGVQFIE
SKQTPDGSWH GNWGICFIYA TWFALSGLAA AGKTYKSCLA VRKGVDFLLA IQEEDGGWGE
SHLSCPEQRY IPLEGNRSNL VQTAWAMMGL IHAGQAERDP TPLHRAAKLI ITSQLENGDF
PQQEILGVFM NTCMLHYATY RNIFPLWALA EYRKAAFATH QDL
