PIMT1_ARATH
ID PIMT1_ARATH Reviewed; 230 AA.
AC Q42539; A0JQ02; Q9STL3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein-L-isoaspartate O-methyltransferase 1;
DE Short=AtPIMT1;
DE EC=2.1.1.77;
DE AltName: Full=L-isoaspartyl protein carboxyl methyltransferase;
DE AltName: Full=Protein L-isoaspartyl methyltransferase;
DE AltName: Full=Protein-beta-aspartate methyltransferase;
GN Name=PIMT1; Synonyms=PCM; OrderedLocusNames=At3g48330; ORFNames=T29H11.150;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=8624405; DOI=10.1007/bf00019007;
RA Mudgett M.B., Clarke S.;
RT "A distinctly regulated protein repair L-isoaspartylmethyltransferase from
RT Arabidopsis thaliana.";
RL Plant Mol. Biol. 30:723-737(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [6]
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).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=19011119; DOI=10.1105/tpc.108.058479;
RA Oge L., Bourdais G., Bove J., Collet B., Godin B., Granier F., Boutin J.P.,
RA Job D., Jullien M., Grappin P.;
RT "Protein repair L-isoaspartyl methyltransferase 1 is involved in both seed
RT longevity and germination vigor in Arabidopsis.";
RL Plant Cell 20:3022-3037(2008).
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. Contributes to seed
CC longevity and germination vigor by limiting the abnormal accumulation
CC of the L-isoaspartyl residues in seed proteins.
CC {ECO:0000269|PubMed:15347786, ECO:0000269|PubMed:19011119,
CC 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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15347786}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, stems, cauline
CC leaves, flowers and developing seeds. {ECO:0000269|PubMed:15347786,
CC ECO:0000269|PubMed:8624405}.
CC -!- INDUCTION: By abscisic acid (ABA). {ECO:0000269|PubMed:19011119}.
CC -!- MISCELLANEOUS: Seeds over-expressing PIMT1 have reduced accumulation of
CC L-isoaspartyl residues in seed proteins and increased seed longevity
CC and germination vigor. Conversely, reduced PIMT1 expression is
CC associated with an increase in the accumulation of L-isoaspartyl
CC residues in proteins, leading to increased sensitivity to aging
CC treatments and loss of seed vigor under stressful germination
CC conditions (PubMed:19011119). {ECO:0000305|PubMed:19011119}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family. {ECO:0000305}.
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DR EMBL; U31288; AAC49279.1; -; Genomic_DNA.
DR EMBL; AL049659; CAB41165.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78401.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78402.1; -; Genomic_DNA.
DR EMBL; BT029372; ABK32186.1; -; mRNA.
DR PIR; T06709; T06709.
DR RefSeq; NP_680112.2; NM_148859.4.
DR RefSeq; NP_851013.2; NM_180682.4.
DR AlphaFoldDB; Q42539; -.
DR SMR; Q42539; -.
DR STRING; 3702.AT3G48330.1; -.
DR iPTMnet; Q42539; -.
DR PaxDb; Q42539; -.
DR PRIDE; Q42539; -.
DR ProteomicsDB; 234953; -.
DR EnsemblPlants; AT3G48330.1; AT3G48330.1; AT3G48330.
DR EnsemblPlants; AT3G48330.2; AT3G48330.2; AT3G48330.
DR GeneID; 823991; -.
DR Gramene; AT3G48330.1; AT3G48330.1; AT3G48330.
DR Gramene; AT3G48330.2; AT3G48330.2; AT3G48330.
DR KEGG; ath:AT3G48330; -.
DR Araport; AT3G48330; -.
DR TAIR; locus:504955645; AT3G48330.
DR eggNOG; KOG1661; Eukaryota.
DR HOGENOM; CLU_055432_0_2_1; -.
DR InParanoid; Q42539; -.
DR OMA; TISAIHM; -.
DR PhylomeDB; Q42539; -.
DR PRO; PR:Q42539; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q42539; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0007568; P:aging; IMP:TAIR.
DR GO; GO:0030091; P:protein repair; TAS:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
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 Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..230
FT /note="Protein-L-isoaspartate O-methyltransferase 1"
FT /id="PRO_0000111882"
FT ACT_SITE 65
FT /evidence="ECO:0000250"
FT CONFLICT 140
FT /note="G -> R (in Ref. 2; CAB41165)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 230 AA; 24614 MW; AC7E505605A48B13 CRC64;
MKQFWSPSSI NKNKAMVENL QNHGIVTSDE VAKAMEAVDR GVFVTDRSSA YVDSPMSIGY
NVTISAPHMH AMCLQLLEKH LKPGMRVLDV GSGTGYLTAC FAVMVGTEGR AIGVEHIPEL
VASSVKNIEA SAASPFLKEG SLAVHVGDGR QGWAEFAPYD AIHVGAAAPE IPEALIDQLK
PGGRLVIPVG NIFQDLQVVD KNSDGSVSIK DETSVRYVPL TSREAQLRGD
