CAS1_ARATH
ID CAS1_ARATH Reviewed; 759 AA.
AC P38605; P92967;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Cycloartenol synthase {ECO:0000303|PubMed:7505443};
DE Short=AtCYC;
DE EC=5.4.99.8 {ECO:0000269|PubMed:7505443};
DE AltName: Full=2,3-epoxysqualene--cycloartenol cyclase;
GN Name=CAS1; Synonyms=CYC; OrderedLocusNames=At2g07050; ORFNames=T4E14.16;
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], AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=7505443; DOI=10.1073/pnas.90.24.11628;
RA Corey E.J., Matsuda S.P.T., Bartel B.;
RT "Isolation of an Arabidopsis thaliana gene encoding cycloartenol synthase
RT by functional expression in a yeast mutant lacking lanosterol synthase by
RT the use of a chromatographic screen.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11628-11632(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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].
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 [5]
RP MUTAGENESIS OF TYR-410 AND ILE-481.
RX DOI=10.1021/ja0013226;
RA Herrera J.B.R., Wilson W.K., Matsuda S.P.T.;
RT "A tyrosine-to-threonine mutation converts cycloartenol synthase to an
RT oxidosqualene cyclase that forms lanosterol as its major product.";
RL J. Am. Chem. Soc. 122:6765-6766(2000).
RN [6]
RP 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 [7]
RP MUTAGENESIS OF HIS-477.
RX PubMed=12465912; DOI=10.1021/ol0269897;
RA Segura M.J.R., Lodeiro S., Meyer M.M., Patel A.J., Matsuda S.P.T.;
RT "Directed evolution experiments reveal mutations at cycloartenol synthase
RT residue His477 that dramatically alter catalysis.";
RL Org. Lett. 4:4459-4462(2002).
RN [8]
RP MUTAGENESIS OF TYR-410; ALA-469; HIS-477; ILE-481 AND TYR-532.
RX PubMed=12081472; DOI=10.1021/bi0200920;
RA Wu T.-K., Griffin J.H.;
RT "Conversion of a plant oxidosqualene-cycloartenol synthase to an
RT oxidosqualene-lanosterol cyclase by random mutagenesis.";
RL Biochemistry 41:8238-8244(2002).
RN [9]
RP MUTAGENESIS OF TYR-410; HIS-477 AND ILE-481.
RX PubMed=15515077; DOI=10.1002/cbic.200400086;
RA Lodeiro S., Segura M.J.R., Stahl M., Schulz-Gasch T., Matsuda S.P.T.;
RT "Oxidosqualene cyclase second-sphere residues profoundly influence the
RT product profile.";
RL ChemBioChem 5:1581-1585(2004).
RN [10]
RP TISSUE 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 [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18287026; DOI=10.1073/pnas.0712190105;
RA Babiychuk E., Bouvier-Nave P., Compagnon V., Suzuki M., Muranaka T.,
RA Van Montagu M., Kushnir S., Schaller H.;
RT "Allelic mutant series reveal distinct functions for Arabidopsis
RT cycloartenol synthase 1 in cell viability and plastid biogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:3163-3168(2008).
CC -!- FUNCTION: Converts oxidosqualene to cycloartenol and 1% parkeol.
CC Involved in plastid biogenesis. Essential for the male gametophyte
CC function. {ECO:0000269|PubMed:18287026, ECO:0000269|PubMed:7505443}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3-epoxysqualene = cycloartenol; Xref=Rhea:RHEA:21308,
CC ChEBI:CHEBI:15441, ChEBI:CHEBI:17030; EC=5.4.99.8;
CC Evidence={ECO:0000269|PubMed:7505443};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21309;
CC Evidence={ECO:0000269|PubMed:7505443};
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, inflorescences
CC and siliques. {ECO:0000269|PubMed:16531458}.
CC -!- DISRUPTION PHENOTYPE: Albino phenotype leading to lethality.
CC {ECO:0000269|PubMed:18287026}.
CC -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC {ECO:0000305}.
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DR EMBL; U02555; AAC04931.1; -; mRNA.
DR EMBL; AC005171; AAM15015.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06032.1; -; Genomic_DNA.
DR EMBL; AY094394; AAM19773.1; -; mRNA.
DR EMBL; BT001118; AAN64509.1; -; mRNA.
DR PIR; A49398; A49398.
DR PIR; H84481; H84481.
DR RefSeq; NP_178722.1; NM_126681.3.
DR AlphaFoldDB; P38605; -.
DR SMR; P38605; -.
DR STRING; 3702.AT2G07050.1; -.
DR BindingDB; P38605; -.
DR ChEMBL; CHEMBL5356; -.
DR iPTMnet; P38605; -.
DR PaxDb; P38605; -.
DR PRIDE; P38605; -.
DR ProteomicsDB; 223909; -.
DR EnsemblPlants; AT2G07050.1; AT2G07050.1; AT2G07050.
DR GeneID; 815275; -.
DR Gramene; AT2G07050.1; AT2G07050.1; AT2G07050.
DR KEGG; ath:AT2G07050; -.
DR Araport; AT2G07050; -.
DR TAIR; locus:2060121; AT2G07050.
DR eggNOG; KOG0497; Eukaryota.
DR HOGENOM; CLU_009074_2_0_1; -.
DR InParanoid; P38605; -.
DR OrthoDB; 365003at2759; -.
DR PhylomeDB; P38605; -.
DR BioCyc; ARA:AT2G07050-MON; -.
DR BioCyc; MetaCyc:AT2G07050-MON; -.
DR BRENDA; 5.4.99.8; 399.
DR PRO; PR:P38605; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P38605; baseline and differential.
DR Genevisible; P38605; AT.
DR GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0016871; F:cycloartenol synthase activity; IDA:TAIR.
DR GO; GO:0019745; P:pentacyclic triterpenoid biosynthetic process; IDA:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0010027; P:thylakoid membrane organization; IMP: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 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..759
FT /note="Cycloartenol synthase"
FT /id="PRO_0000072662"
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 REPEAT 700..741
FT /note="PFTB 5"
FT ACT_SITE 483
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P48449"
FT MUTAGEN 410
FT /note="Y->C: Produces lanosterol instead of cycloartenol."
FT /evidence="ECO:0000269|PubMed:12081472,
FT ECO:0000269|PubMed:15515077, ECO:0000269|Ref.5"
FT MUTAGEN 410
FT /note="Y->T: Produces 65% lanosterol, 2% parkeol and 33%
FT 9beta-delta7-lanosterol instead of cycloartenol. Produces
FT 75% lanosterol, 0.6% parkeol and 24% 9beta-delta7-
FT lanosterol instead of cycloartenol; when associated with V-
FT 481. Produces 75% lanosterol and 24% 9beta-delta7-
FT lanosterol instead of cycloartenol; when associated with N-
FT 477 or Q-477 and V-481."
FT /evidence="ECO:0000269|PubMed:12081472,
FT ECO:0000269|PubMed:15515077, ECO:0000269|Ref.5"
FT MUTAGEN 469
FT /note="A->V: Produces lanosterol and achilleol A instead of
FT cycloartenol."
FT /evidence="ECO:0000269|PubMed:12081472"
FT MUTAGEN 477
FT /note="H->N: Produces 88% lanosterol and 12% parkeol
FT instead of cycloartenol. Produces 75% lanosterol and 24%
FT 9beta-delta7-lanosterol instead of cycloartenol; when
FT associated with T-410 and V-481."
FT /evidence="ECO:0000269|PubMed:12081472,
FT ECO:0000269|PubMed:12465912, ECO:0000269|PubMed:15515077"
FT MUTAGEN 477
FT /note="H->Q: Produces 22% lanosterol, 73% parkeol and 5%
FT 9beta-delta7-lanosterol instead of cycloartenol. Produces
FT 75% lanosterol and 24% 9beta-delta7-lanosterol instead of
FT cycloartenol; when associated with T-410 and V-481."
FT /evidence="ECO:0000269|PubMed:12081472,
FT ECO:0000269|PubMed:12465912, ECO:0000269|PubMed:15515077"
FT MUTAGEN 477
FT /note="H->Y: Produces lanosterol instead of cycloartenol."
FT /evidence="ECO:0000269|PubMed:12081472,
FT ECO:0000269|PubMed:12465912, ECO:0000269|PubMed:15515077"
FT MUTAGEN 481
FT /note="I->T: Produces lanosterol and achilleol A instead of
FT cycloartenol."
FT /evidence="ECO:0000269|PubMed:12081472,
FT ECO:0000269|PubMed:15515077, ECO:0000269|Ref.5"
FT MUTAGEN 481
FT /note="I->V: Produces 24% lanosterol, 20% parkeol and 56%
FT cycloartenol. Produces 75% lanosterol, 0.6% parkeol and 24%
FT 9beta-delta7-lanosterol instead of cycloartenol; when
FT associated with T-410."
FT /evidence="ECO:0000269|PubMed:12081472,
FT ECO:0000269|PubMed:15515077, ECO:0000269|Ref.5"
FT MUTAGEN 532
FT /note="Y->H: Produces lanosterol and achilleol A instead of
FT cycloartenol."
FT /evidence="ECO:0000269|PubMed:12081472"
FT CONFLICT 501
FT /note="A -> E (in Ref. 1; AAC04931)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 759 AA; 86033 MW; DBA75CC57BB1F74D CRC64;
MWKLKIAEGG SPWLRTTNNH VGRQFWEFDP NLGTPEDLAA VEEARKSFSD NRFVQKHSAD
LLMRLQFSRE NLISPVLPQV KIEDTDDVTE EMVETTLKRG LDFYSTIQAH DGHWPGDYGG
PMFLLPGLII TLSITGALNT VLSEQHKQEM RRYLYNHQNE DGGWGLHIEG PSTMFGSVLN
YVTLRLLGEG PNDGDGDMEK GRDWILNHGG ATNITSWGKM WLSVLGAFEW SGNNPLPPEI
WLLPYFLPIH PGRMWCHCRM VYLPMSYLYG KRFVGPITST VLSLRKELFT VPYHEVNWNE
ARNLCAKEDL YYPHPLVQDI LWASLHKIVE PVLMRWPGAN LREKAIRTAI EHIHYEDENT
RYICIGPVNK VLNMLCCWVE DPNSEAFKLH LPRIHDFLWL AEDGMKMQGY NGSQLWDTGF
AIQAILATNL VEEYGPVLEK AHSFVKNSQV LEDCPGDLNY WYRHISKGAW PFSTADHGWP
ISDCTAEGLK AALLLSKVPK AIVGEPIDAK RLYEAVNVII SLQNADGGLA TYELTRSYPW
LELINPAETF GDIVIDYPYV ECTSAAIQAL ISFRKLYPGH RKKEVDECIE KAVKFIESIQ
AADGSWYGSW AVCFTYGTWF GVKGLVAVGK TLKNSPHVAK ACEFLLSKQQ PSGGWGESYL
SCQDKVYSNL DGNRSHVVNT AWAMLALIGA GQAEVDRKPL HRAARYLINA QMENGDFPQQ
EIMGVFNRNC MITYAAYRNI FPIWALGEYR CQVLLQQGE
