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   27-MAR-2024, entry version 145.
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;
GN   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=10.1105/tpc.12.6.853;
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   BioGRID; 16494; 2.
DR   STRING; 3702.Q9LM02; -.
DR   BindingDB; Q9LM02; -.
DR   ChEMBL; CHEMBL4264; -.
DR   iPTMnet; Q9LM02; -.
DR   PaxDb; 3702-AT5G13710-1; -.
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; AT5G13710; SMT1.
DR   eggNOG; KOG1269; Eukaryota.
DR   HOGENOM; CLU_039068_5_0_1; -.
DR   InParanoid; Q9LM02; -.
DR   OMA; AFNKAMH; -.
DR   OrthoDB; 275921at2759; -.
DR   PhylomeDB; Q9LM02; -.
DR   BioCyc; ARA:AT5G13710-MONOMER; -.
DR   BioCyc; MetaCyc:AT5G13710-MONOMER; -.
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   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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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   PANTHER; PTHR44068:SF1; HYPOTHETICAL LOC100005854; 1.
DR   PANTHER; PTHR44068; ZGC:194242; 1.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   Pfam; PF08498; Sterol_MT_C; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51685; SAM_MT_ERG6_SMT; 1.
DR   Genevisible; Q9LM02; AT.
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
//