SMT1_ARATH
ID SMT1_ARATH Reviewed; 336 AA.
AC Q9LM02; Q8LKW1;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Cycloartenol-C-24-methyltransferase;
DE EC=2.1.1.41 {ECO:0000269|PubMed:10852933};
DE AltName: Full=24-sterol C-methyltransferase 1;
DE Short=Sterol C-methyltransferase 1;
DE AltName: Full=Protein CEPHALOPOD;
DE AltName: Full=Protein STEROL METHYLTRANSFERASE 1;
GN Name=SMT1; Synonyms=CPH; OrderedLocusNames=At5g13710; ORFNames=MSH12.18;
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].
RC STRAIN=cv. Columbia;
RA Schaeffer A., Schaller H., Benveniste P.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=10852933; DOI=10.2307/3871215;
RA Diener A.C., Li H., Zhou W.-X., Whoriskey W.J., Nes W.D., Fink G.R.;
RT "Sterol methyltransferase 1 controls the level of cholesterol in plants.";
RL Plant Cell 12:853-870(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=12100483; DOI=10.1046/j.1365-313x.2002.01333.x;
RA Schrick K., Mayer U., Martin G., Bellini C., Kuhnt C., Schmidt J.,
RA Juergens G.;
RT "Interactions between sterol biosynthesis genes in embryonic development of
RT Arabidopsis.";
RL Plant J. 31:61-73(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
RN [5]
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 [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Catalyzes the methyl transfer from S-adenosyl-methionine to
CC the C-24 of cycloartenol to form 24-methylene cycloartenol.
CC {ECO:0000269|PubMed:10852933}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cycloartenol + S-adenosyl-L-methionine = 24-
CC methylenecycloartanol + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:59012, ChEBI:CHEBI:1307, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17030, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.41;
CC Evidence={ECO:0000269|PubMed:10852933};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59013;
CC Evidence={ECO:0000305|PubMed:10852933};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=42 uM for cycloartenol {ECO:0000269|PubMed:10852933};
CC Vmax=5.2 pmol/min/mg enzyme with cycloartenol as substrate
CC {ECO:0000269|PubMed:10852933};
CC -!- PATHWAY: Steroid biosynthesis; sterol biosynthesis.
CC {ECO:0000305|PubMed:10852933}.
CC -!- TISSUE SPECIFICITY: Highly expressed in vascular tissue, mature leaves
CC and in regions undergoing cellular expansion.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Erg6/SMT family. {ECO:0000255|PROSITE-ProRule:PRU01022}.
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DR EMBL; AF090372; AAF78847.1; -; mRNA.
DR EMBL; AF195648; AAG28462.1; -; mRNA.
DR EMBL; AF494289; AAM53553.1; -; mRNA.
DR EMBL; AB006704; BAB08698.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91930.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91931.1; -; Genomic_DNA.
DR EMBL; AY120716; AAM53274.1; -; mRNA.
DR EMBL; BT000058; AAN15377.1; -; mRNA.
DR RefSeq; NP_001078579.1; NM_001085110.1.
DR RefSeq; NP_196875.1; NM_121374.4.
DR AlphaFoldDB; Q9LM02; -.
DR SMR; Q9LM02; -.
DR STRING; 3702.AT5G13710.1; -.
DR BindingDB; Q9LM02; -.
DR ChEMBL; CHEMBL4264; -.
DR iPTMnet; Q9LM02; -.
DR PaxDb; Q9LM02; -.
DR PRIDE; Q9LM02; -.
DR ProteomicsDB; 232661; -.
DR DNASU; 831216; -.
DR EnsemblPlants; AT5G13710.1; AT5G13710.1; AT5G13710.
DR EnsemblPlants; AT5G13710.2; AT5G13710.2; AT5G13710.
DR GeneID; 831216; -.
DR Gramene; AT5G13710.1; AT5G13710.1; AT5G13710.
DR Gramene; AT5G13710.2; AT5G13710.2; AT5G13710.
DR KEGG; ath:AT5G13710; -.
DR Araport; AT5G13710; -.
DR TAIR; locus:2173229; AT5G13710.
DR eggNOG; KOG1269; Eukaryota.
DR HOGENOM; CLU_039068_5_0_1; -.
DR InParanoid; Q9LM02; -.
DR OMA; ISNMCKV; -.
DR OrthoDB; 661953at2759; -.
DR PhylomeDB; Q9LM02; -.
DR BioCyc; ARA:AT5G13710-MON; -.
DR BioCyc; MetaCyc:AT5G13710-MON; -.
DR BRENDA; 2.1.1.142; 399.
DR UniPathway; UPA00766; -.
DR PRO; PR:Q9LM02; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LM02; baseline and differential.
DR Genevisible; Q9LM02; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003838; F:sterol 24-C-methyltransferase activity; IDA:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0016126; P:sterol biosynthetic process; IMP:TAIR.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR030384; MeTrfase_SMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR013705; Sterol_MeTrfase_C.
DR Pfam; PF08241; Methyltransf_11; 1.
DR Pfam; PF08498; Sterol_MT_C; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51685; SAM_MT_ERG6_SMT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transferase.
FT CHAIN 1..336
FT /note="Cycloartenol-C-24-methyltransferase"
FT /id="PRO_0000124800"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 119
FT /note="V -> A (in Ref. 3; AAM53553)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="S -> N (in Ref. 3; AAM53553)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 38268 MW; 4649BB3868DE1CE9 CRC64;
MDLASNLGGK IDKSDVLTAV EKYEQYHVFH GGNEEERKAN YTDMVNKYYD LATSFYEYGW
GESFHFAQRW KGESLRESIK RHEHFLALQL GIQPGQKVLD VGCGIGGPLR EIARFSNSVV
TGLNNNEYQI TRGKELNRLA GVDKTCNFVK ADFMKMPFPE NSFDAVYAIE ATCHAPDAYG
CYKEIYRVLK PGQCFAAYEW CMTDAFDPDN AEHQKIKGEI EIGDGLPDIR LTTKCLEALK
QAGFEVIWEK DLAKDSPVPW YLPLDKNHFS LSSFRLTAVG RFITKNMVKI LEYIRLAPQG
SQRVSNFLEQ AAEGLVDGGR REIFTPMYFF LARKPE
