LAS1_ARATH
ID LAS1_ARATH Reviewed; 756 AA.
AC Q1G1A4; A0A1I9LTE2; Q9M1U6;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Lanosterol synthase {ECO:0000303|PubMed:16445886};
DE EC=5.4.99.7 {ECO:0000269|PubMed:16445886};
GN Name=LAS1; Synonyms=LSS; OrderedLocusNames=At3g45130; ORFNames=T14D3.70;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16445886; DOI=10.1016/j.abb.2005.12.010;
RA Kolesnikova M.D., Xiong Q., Lodeiro S., Hua L., Matsuda S.P.T.;
RT "Lanosterol biosynthesis in plants.";
RL Arch. Biochem. Biophys. 447:87-95(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=16531458; DOI=10.1093/pcp/pcj031;
RA Suzuki M., Xiang T., Ohyama K., Seki H., Saito K., Muranaka T., Hayashi H.,
RA Katsube Y., Kushiro T., Shibuya M., Ebizuka Y.;
RT "Lanosterol synthase in dicotyledonous plants.";
RL Plant Cell Physiol. 47:565-571(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
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).
CC -!- FUNCTION: Converts oxidosqualene to lanosterol.
CC {ECO:0000269|PubMed:16445886, ECO:0000269|PubMed:16531458}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3-epoxysqualene = lanosterol; Xref=Rhea:RHEA:14621,
CC ChEBI:CHEBI:15441, ChEBI:CHEBI:16521; EC=5.4.99.7;
CC Evidence={ECO:0000269|PubMed:16445886};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14622;
CC Evidence={ECO:0000269|PubMed:16445886};
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems and siliques. Low
CC expression in rosette leaves. {ECO:0000269|PubMed:16531458}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:16531458}.
CC -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB72151.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ508794; ABF57670.1; -; mRNA.
DR EMBL; AB247155; BAE95408.1; -; mRNA.
DR EMBL; AL138649; CAB72151.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77996.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65849.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65850.1; -; Genomic_DNA.
DR PIR; T47453; T47453.
DR RefSeq; NP_001327787.1; NM_001339197.1.
DR RefSeq; NP_001327788.1; NM_001339196.1.
DR RefSeq; NP_190099.3; NM_114382.5.
DR AlphaFoldDB; Q1G1A4; -.
DR SMR; Q1G1A4; -.
DR STRING; 3702.AT3G45130.1; -.
DR PaxDb; Q1G1A4; -.
DR PRIDE; Q1G1A4; -.
DR ProteomicsDB; 237148; -.
DR EnsemblPlants; AT3G45130.1; AT3G45130.1; AT3G45130.
DR EnsemblPlants; AT3G45130.4; AT3G45130.4; AT3G45130.
DR EnsemblPlants; AT3G45130.5; AT3G45130.5; AT3G45130.
DR GeneID; 823649; -.
DR Gramene; AT3G45130.1; AT3G45130.1; AT3G45130.
DR Gramene; AT3G45130.4; AT3G45130.4; AT3G45130.
DR Gramene; AT3G45130.5; AT3G45130.5; AT3G45130.
DR KEGG; ath:AT3G45130; -.
DR Araport; AT3G45130; -.
DR TAIR; locus:2096905; AT3G45130.
DR eggNOG; KOG0497; Eukaryota.
DR HOGENOM; CLU_009074_2_1_1; -.
DR InParanoid; Q1G1A4; -.
DR OMA; GEYYQRV; -.
DR PhylomeDB; Q1G1A4; -.
DR BioCyc; ARA:AT3G45130-MON; -.
DR BRENDA; 5.4.99.7; 399.
DR PRO; PR:Q1G1A4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q1G1A4; baseline and differential.
DR Genevisible; Q1G1A4; AT.
DR GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR GO; GO:0000250; F:lanosterol synthase activity; IDA:TAIR.
DR GO; GO:0016104; P:triterpenoid biosynthetic process; IEA:InterPro.
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 Isomerase; Reference proteome; Repeat.
FT CHAIN 1..756
FT /note="Lanosterol synthase"
FT /id="PRO_0000366143"
FT REPEAT 147..188
FT /note="PFTB 1"
FT REPEAT 512..557
FT /note="PFTB 2"
FT REPEAT 589..629
FT /note="PFTB 3"
FT REPEAT 638..679
FT /note="PFTB 4"
FT ACT_SITE 483
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P48449"
SQ SEQUENCE 756 AA; 86518 MW; 010E5B3FA7AF1E7E CRC64;
MWRLKLSEGD EESVNQHVGR QFWEYDNQFG TSEERHHINH LRSNFTLNRF SSKHSSDLLY
RFQCWKEKGK GMERLPQVKV KEGEERLINE EVVNVTLRRS LRFYSILQSQ DGFWPGDYGG
PLFLLPALVI GLYVTEVLDG TLTAQHQIEI RRYLYNHQNK DGGWGLHVEG NSTMFCTVLS
YVALRLMGEE LDGGDGAMES ARSWIHHHGG ATFIPSWGKF WLSVLGAYEW SGNNPLPPEL
WLLPYSLPFH PGRMWCHCRM VYLPMSYLYG RRFVCRTNGT ILSLRRELYT IPYHHIDWDT
ARNQCAKEDL YYPHPKIQDV LWSCLNKFGE PLLERWPLNN LRNHALQTVM QHIHYEDQNS
HYICIGPVNK VLNMLCCWVE SSNSEAFKSH LSRIKDYLWV AEDGMKMQGY NGSQLWDVTL
AVQAILATNL VDDYGLMLKK AHNYIKNTQI RKDTSGDPGL WYRHPCKGGW GFSTGDNPWP
VSDCTAEALK AALLLSQMPV NLVGEPMPEE HLVDAVNFIL SLQNKNGGFA SYELTRSYPE
LEVINPSETF GDIIIDYQYV ECTSAAIQGL VLFTTLNSSY KRKEIVGSIN KAVEFIEKTQ
LPDGSWYGSW GVCFTYATWF GIKGMLASGK TYESSLCIRK ACGFLLSKQL CCGGWGESYL
SCQNKVYTNL PGNKSHIVNT SWALLALIEA GQASRDPMPL HRGAKSLINS QMEDGDYPQQ
EILGVFNRNC MISYSAYRNI FPIWALGEYR KLMLSL
