LCMT1_ARATH
ID LCMT1_ARATH Reviewed; 332 AA.
AC Q8VY08; O81910; Q570N7;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Leucine carboxyl methyltransferase 1 homolog {ECO:0000305};
DE EC=2.1.1.233 {ECO:0000269|PubMed:21558554};
DE AltName: Full=Protein SUPPRESSOR OF BRI1 {ECO:0000303|PubMed:21558554};
DE AltName: Full=[Phosphatase 2A protein]-leucine-carboxy methyltransferase 1 {ECO:0000305};
GN Name=LCMT1 {ECO:0000305}; Synonyms=SBI1 {ECO:0000303|PubMed:21558554};
GN OrderedLocusNames=At1g02100 {ECO:0000312|Araport:AT1G02100};
GN ORFNames=T7I23.16 {ECO:0000312|EMBL:AAC24381.1};
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 249-332.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION BY
RP BRASSINOSTEROID, AND MUTAGENESIS OF GLU-290.
RX PubMed=21558554; DOI=10.1126/scisignal.2001258;
RA Wu G., Wang X., Li X., Kamiya Y., Otegui M.S., Chory J.;
RT "Methylation of a phosphatase specifies dephosphorylation and degradation
RT of activated brassinosteroid receptors.";
RL Sci. Signal. 4:RA29-RA29(2011).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28741704; DOI=10.1111/pce.13038;
RA Creighton M.T., Kolton A., Kataya A.R.A., Maple-Groedem J., Averkina I.O.,
RA Heidari B., Lillo C.;
RT "Methylation of protein phosphatase 2A-influence of regulators and
RT environmental stress factors.";
RL Plant Cell Environ. 40:2347-2358(2017).
CC -!- FUNCTION: Methylates the carboxyl group of the C-terminal leucine
CC residue of protein phosphatase 2A (PP2A) catalytic subunits to form
CC alpha-leucine ester residues (Probable) (PubMed:21558554). Involved in
CC brassinosteroid (BR) signaling. Plays a negative role in BR signaling
CC pathway. Functions as a positive regulator of BRI1 receptor-kinase
CC degradation. Methylates PP2A, thus facilitating its association with
CC activated BRI1. This leads to receptor dephosphorylation and
CC degradation, and thus to the termination of BR signaling. May act
CC upstream of ASK7/BIN2 (PubMed:21558554). Involved in methylation of
CC PP2A during environemental stress responses (PubMed:28741704).
CC {ECO:0000269|PubMed:21558554, ECO:0000269|PubMed:28741704,
CC ECO:0000305|PubMed:28741704}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-
CC methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl
CC ester + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48544, Rhea:RHEA-
CC COMP:12134, Rhea:RHEA-COMP:12135, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:90516, ChEBI:CHEBI:90517;
CC EC=2.1.1.233; Evidence={ECO:0000269|PubMed:21558554};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21558554}. Membrane
CC {ECO:0000269|PubMed:21558554}; Peripheral membrane protein.
CC -!- INDUCTION: Induced by brassinosteroids. {ECO:0000269|PubMed:21558554}.
CC -!- DISRUPTION PHENOTYPE: Reduced rosette size and early flowering. Reduced
CC length of the main root and reduced number of lateral roots.
CC {ECO:0000269|PubMed:28741704}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC24381.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD95220.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U89959; AAC24381.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27383.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27384.1; -; Genomic_DNA.
DR EMBL; AY074300; AAL66997.1; -; mRNA.
DR EMBL; AY133744; AAM91678.1; -; mRNA.
DR EMBL; AK220671; BAD95220.1; ALT_INIT; mRNA.
DR PIR; H86152; H86152.
DR RefSeq; NP_171712.2; NM_100090.4.
DR RefSeq; NP_973741.1; NM_202012.1.
DR AlphaFoldDB; Q8VY08; -.
DR SMR; Q8VY08; -.
DR STRING; 3702.AT1G02100.1; -.
DR iPTMnet; Q8VY08; -.
DR PaxDb; Q8VY08; -.
DR PRIDE; Q8VY08; -.
DR EnsemblPlants; AT1G02100.1; AT1G02100.1; AT1G02100.
DR EnsemblPlants; AT1G02100.3; AT1G02100.3; AT1G02100.
DR GeneID; 837541; -.
DR Gramene; AT1G02100.1; AT1G02100.1; AT1G02100.
DR Gramene; AT1G02100.3; AT1G02100.3; AT1G02100.
DR KEGG; ath:AT1G02100; -.
DR Araport; AT1G02100; -.
DR TAIR; locus:2205619; AT1G02100.
DR eggNOG; KOG2918; Eukaryota.
DR HOGENOM; CLU_031312_0_0_1; -.
DR InParanoid; Q8VY08; -.
DR OrthoDB; 1094856at2759; -.
DR PhylomeDB; Q8VY08; -.
DR BRENDA; 2.1.1.233; 399.
DR PRO; PR:Q8VY08; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VY08; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IDA:UniProtKB.
DR GO; GO:1900458; P:negative regulation of brassinosteroid mediated signaling pathway; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016651; PPM1.
DR InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13600; PTHR13600; 1.
DR Pfam; PF04072; LCM; 1.
DR PIRSF; PIRSF016305; LCM_mtfrase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Membrane; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Stress response; Transferase.
FT CHAIN 1..332
FT /note="Leucine carboxyl methyltransferase 1 homolog"
FT /id="PRO_0000443354"
FT BINDING 22
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UIC8"
FT BINDING 57
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UIC8"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UIC8"
FT BINDING 107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UIC8"
FT BINDING 153..154
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UIC8"
FT BINDING 180
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UIC8"
FT MUTAGEN 290
FT /note="E->K: In sbi1; early flowering."
FT /evidence="ECO:0000269|PubMed:21558554"
SQ SEQUENCE 332 AA; 37550 MW; 833887B9CDBAAA97 CRC64;
MAESRSNRAA VQATNDDASA SKLSCVKKGY MKDDYVHLFV KRPVRRSPII NRGYFSRWAA
FRKLMSQFLL SGTSSKKQIL SLGAGFDTTY FQLLDEGNGP NLYVELDFKE VTSKKAAVIQ
NSSQLRDKLG ANASISIDEG QVLSDHYKLL PVDLRDIPKL RDVISFADMD LSLPTFIIAE
CVLIYLDPDS SRAIVNWSSK TFSTAVFFLY EQIHPDDAFG HQMIRNLESR GCALLSIDAS
PTLLAKERLF LDNGWQRAVA WDMLKVYGSF VDTQEKRRIE RLELFDEFEE WHMMQEHYCV
TYAVNDAMGI FGDFGFTREG GGERMSSSAS SP
