ID   SMT2_ARATH              Reviewed;         361 AA.
AC   Q39227; Q8H155; Q8L7L3; Q8LCB0; Q9LN25;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=24-methylenesterol C-methyltransferase 2;
DE            Short=24-sterol C-methyltransferase 2;
DE            Short=Sterol-C-methyltransferase 2;
DE            EC=2.1.1.143;
DE   AltName: Full=Protein COTYLEDON VASCULAR PATTERN 1;
GN   Name=SMT2; Synonyms=CVP1; OrderedLocusNames=At1g20330; ORFNames=F14O10.7;
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; TISSUE=Silique;
RX   PubMed=8641446; DOI=10.1016/0014-5793(96)00089-0;
RA   Husselstein T., Gachotte D., Desprez T., Bard M., Benveniste P.;
RT   "Transformation of Saccharomyces cerevisiae with a cDNA encoding a sterol-
RT   C-methyltransferase from Arabidopsis thaliana results in the synthesis of
RT   24-ethyl sterols.";
RL   FEBS Lett. 381:87-92(1996).
RN   [2]
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   [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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   CHARACTERIZATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=12215504; DOI=10.1105/tpc.003939;
RA   Carland F.M., Fujioka S., Takatsuto S., Yoshida S., Nelson T.;
RT   "The identification of CVP1 reveals a role for sterols in vascular
RT   patterning.";
RL   Plant Cell 14:2045-2058(2002).
CC   -!- FUNCTION: Catalyzes the methyl transfer from S-adenosyl-methionine to
CC       the methylene group of 24-methylene lophenol to form 24-ethylidene
CC       lophenol.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=24-methylidenelophenol + S-adenosyl-L-methionine = (Z)-24-
CC         ethylidenelophenol + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:21044, ChEBI:CHEBI:15378, ChEBI:CHEBI:29107,
CC         ChEBI:CHEBI:33203, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
CC         EC=2.1.1.143;
CC   -!- PATHWAY: Steroid biosynthesis; sterol biosynthesis.
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; X89867; CAA61966.1; -; mRNA.
DR   EMBL; AC026234; AAF88156.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29962.1; -; Genomic_DNA.
DR   EMBL; AY046042; AAK76716.1; -; mRNA.
DR   EMBL; AF332417; AAG48780.1; -; mRNA.
DR   EMBL; AY113961; AAM45009.1; -; mRNA.
DR   EMBL; AY128389; AAM91592.1; -; mRNA.
DR   EMBL; BT002093; AAN72104.1; -; mRNA.
DR   EMBL; BT000750; AAN31890.1; -; mRNA.
DR   EMBL; AY086699; AAM63753.1; -; mRNA.
DR   PIR; S63686; S63686.
DR   RefSeq; NP_173458.1; NM_101884.4.
DR   AlphaFoldDB; Q39227; -.
DR   SMR; Q39227; -.
DR   BioGRID; 23860; 2.
DR   STRING; 3702.AT1G20330.1; -.
DR   iPTMnet; Q39227; -.
DR   SwissPalm; Q39227; -.
DR   PaxDb; Q39227; -.
DR   PRIDE; Q39227; -.
DR   ProteomicsDB; 234532; -.
DR   EnsemblPlants; AT1G20330.1; AT1G20330.1; AT1G20330.
DR   GeneID; 838621; -.
DR   Gramene; AT1G20330.1; AT1G20330.1; AT1G20330.
DR   KEGG; ath:AT1G20330; -.
DR   Araport; AT1G20330; -.
DR   TAIR; locus:2012938; AT1G20330.
DR   eggNOG; KOG1269; Eukaryota.
DR   HOGENOM; CLU_039068_5_2_1; -.
DR   InParanoid; Q39227; -.
DR   OMA; EYFQHWD; -.
DR   OrthoDB; 661953at2759; -.
DR   PhylomeDB; Q39227; -.
DR   BioCyc; ARA:AT1G20330-MON; -.
DR   BioCyc; MetaCyc:AT1G20330-MON; -.
DR   UniPathway; UPA00766; -.
DR   PRO; PR:Q39227; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q39227; baseline and differential.
DR   Genevisible; Q39227; AT.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0030797; F:24-methylenesterol C-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:TAIR.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0009825; P:multidimensional cell growth; IMP:TAIR.
DR   GO; GO:0032876; P:negative regulation of DNA endoreduplication; IMP:TAIR.
DR   GO; GO:0007389; P:pattern specification process; IMP:TAIR.
DR   GO; GO:0016126; P:sterol biosynthetic process; IDA:TAIR.
DR   GO; GO:0010051; P:xylem and phloem pattern formation; 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; IPR044625; SMT2/3-like.
DR   InterPro; IPR013705; Sterol_MeTrfase_C.
DR   PANTHER; PTHR44742; PTHR44742; 1.
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   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..361
FT                   /note="24-methylenesterol C-methyltransferase 2"
FT                   /id="PRO_0000124801"
FT   CONFLICT        333
FT                   /note="Y -> C (in Ref. 1; CAA61966)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        339
FT                   /note="E -> Q (in Ref. 4; AAM91592/AAN72104)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        354
FT                   /note="P -> A (in Ref. 4; AAN31890)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   361 AA;  40450 MW;  7ED8AC27859919CB CRC64;
     MDSLTLFFTG ALVAVGIYWF LCVLGPAERK GKRAVDLSGG SISAEKVQDN YKQYWSFFRR
     PKEIETAEKV PDFVDTFYNL VTDIYEWGWG QSFHFSPSIP GKSHKDATRL HEEMAVDLIQ
     VKPGQKILDV GCGVGGPMRA IASHSRANVV GITINEYQVN RARLHNKKAG LDALCEVVCG
     NFLQMPFDDN SFDGAYSIEA TCHAPKLEEV YAEIYRVLKP GSMYVSYEWV TTEKFKAEDD
     EHVEVIQGIE RGDALPGLRA YVDIAETAKK VGFEIVKEKD LASPPAEPWW TRLKMGRLAY
     WRNHIVVQIL SAVGVAPKGT VDVHEMLFKT ADYLTRGGET GIFSPMHMIL CRKPESPEES
     S