PIMT2_ARATH
ID PIMT2_ARATH Reviewed; 309 AA.
AC Q64J17; Q64J16; Q8GXQ4; Q9FGS1;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Protein-L-isoaspartate O-methyltransferase 2;
DE Short=AtPIMT2;
DE EC=2.1.1.77;
GN Name=PIMT2; OrderedLocusNames=At5g50240; ORFNames=K6A12.10;
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 [GENOMIC DNA], ALTERNATIVE SPLICING, FUNCTION,
RP CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION, AND MUTAGENESIS OF
RP 23-LYS-LYS-24.
RC STRAIN=cv. Wassilewskija;
RX PubMed=15347786; DOI=10.1104/pp.104.046094;
RA Xu Q., Belcastro M.P., Villa S.T., Dinkins R.D., Clarke S.G., Downie A.B.;
RT "A second protein L-isoaspartyl methyltransferase gene in Arabidopsis
RT produces two transcripts whose products are sequestered in the nucleus.";
RL Plant Physiol. 136:2652-2664(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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] (ISOFORM 3).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21076691; DOI=10.1111/j.1399-3054.2006.00772.x;
RA Villa S.T., Xu Q., Downie A.B., Clarke S.G.;
RT "Arabidopsis protein repair L-isoaspartyl methyltransferases: predominant
RT activities at lethal temperatures.";
RL Physiol. Plantarum 128:581-592(2006).
CC -!- FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl residues
CC in peptides and proteins that result from spontaneous decomposition of
CC normal L-aspartyl and L-asparaginyl residues. It plays a role in the
CC repair and/or degradation of damaged proteins.
CC {ECO:0000269|PubMed:15347786, ECO:0000269|PubMed:21076691}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-L-isoaspartate + S-adenosyl-L-methionine =
CC [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:12705, Rhea:RHEA-COMP:12143, Rhea:RHEA-
CC COMP:12144, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90596,
CC ChEBI:CHEBI:90598; EC=2.1.1.77;
CC Evidence={ECO:0000269|PubMed:15347786};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:21076691};
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q64J17-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q64J17-2; Sequence=VSP_054320;
CC Name=3;
CC IsoId=Q64J17-3; Sequence=VSP_054319;
CC -!- TISSUE SPECIFICITY: Expressed in rosette leaves, stems, cauline leaves,
CC flowers and developing seeds. {ECO:0000269|PubMed:15347786}.
CC -!- INDUCTION: By abscisic acid (ABA), drought and salt stress.
CC {ECO:0000269|PubMed:15347786}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09395.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY496702; AAR97903.1; -; Genomic_DNA.
DR EMBL; AY496702; AAR97904.1; -; Genomic_DNA.
DR EMBL; AY496702; ACL14906.1; -; Genomic_DNA.
DR EMBL; AB024031; BAB09395.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95915.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95916.1; -; Genomic_DNA.
DR EMBL; AK118104; BAC42732.1; -; mRNA.
DR RefSeq; NP_001078740.1; NM_001085271.1. [Q64J17-2]
DR RefSeq; NP_199835.2; NM_124403.2. [Q64J17-1]
DR AlphaFoldDB; Q64J17; -.
DR SMR; Q64J17; -.
DR STRING; 3702.AT5G50240.1; -.
DR PaxDb; Q64J17; -.
DR PRIDE; Q64J17; -.
DR ProteomicsDB; 226174; -. [Q64J17-1]
DR EnsemblPlants; AT5G50240.1; AT5G50240.1; AT5G50240. [Q64J17-1]
DR EnsemblPlants; AT5G50240.2; AT5G50240.2; AT5G50240. [Q64J17-2]
DR GeneID; 835089; -.
DR Gramene; AT5G50240.1; AT5G50240.1; AT5G50240. [Q64J17-1]
DR Gramene; AT5G50240.2; AT5G50240.2; AT5G50240. [Q64J17-2]
DR KEGG; ath:AT5G50240; -.
DR Araport; AT5G50240; -.
DR TAIR; locus:2157767; AT5G50240.
DR eggNOG; KOG1661; Eukaryota.
DR InParanoid; Q64J17; -.
DR OrthoDB; 1138104at2759; -.
DR PhylomeDB; Q64J17; -.
DR BRENDA; 2.1.1.77; 399.
DR PRO; PR:Q64J17; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q64J17; baseline and differential.
DR Genevisible; Q64J17; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IDA:TAIR.
DR GO; GO:0030091; P:protein repair; TAS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR000682; PCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11579; PTHR11579; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00080; pimt; 1.
DR PROSITE; PS01279; PCMT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..309
FT /note="Protein-L-isoaspartate O-methyltransferase 2"
FT /id="PRO_0000428878"
FT MOTIF 23..28
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000305"
FT ACT_SITE 144
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..84
FT /note="MNTNTQTEQQIIREETRIDKIIKKRKKKMRAQVLLCPTITAYGRLYCAPRRL
FT HRYNSSSSSSQFLNLNLSRFSGALFFHMEQFQ -> ME (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_054319"
FT VAR_SEQ 82..84
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054320"
FT MUTAGEN 23..24
FT /note="KK->RR: Loss of nuclear targeting."
FT /evidence="ECO:0000269|PubMed:15347786"
SQ SEQUENCE 309 AA; 33986 MW; E4220BAE9B39656F CRC64;
MNTNTQTEQQ IIREETRIDK IIKKRKKKMR AQVLLCPTIT AYGRLYCAPR RLHRYNSSSS
SSQFLNLNLS RFSGALFFHM EQFQSGTGSS GKRGMVENLK RYGVISSKRV AQVMEALDRG
LFVPVGSSAY VDTPVPIGYN ATISAPHMHA TCLQLLEDKL HPGMRALDVG SGTGYLTGCF
ALMVGAEGRV VGVDHIPELV DMSIKNIEKS VAASFLKKGS LSLHVGDGRK GWQEFAPYDA
IHVGAAASEI PQPLLDQLKP GGRMVIPLGT YFQELKVIDK NEDGSIKVHT ETSVRYVPLT
SRVEQLGGF
