PIMT_CAEEL
ID PIMT_CAEEL Reviewed; 225 AA.
AC Q27873;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Protein-L-isoaspartate O-methyltransferase {ECO:0000250|UniProtKB:P23506};
DE Short=PIMT;
DE EC=2.1.1.77 {ECO:0000250|UniProtKB:P23506};
DE AltName: Full=L-isoaspartyl protein carboxyl methyltransferase;
DE AltName: Full=Protein L-isoaspartyl methyltransferase;
DE AltName: Full=Protein-beta-aspartate methyltransferase;
GN Name=pcm-1; ORFNames=C10F3.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Bristol N2;
RX PubMed=7662659; DOI=10.1021/bi00034a012;
RA Kagan R.M., Clarke S.;
RT "Protein L-isoaspartyl methyltransferase from the nematode Caenorhabditis
RT elegans: genomic structure and substrate specificity.";
RL Biochemistry 34:10794-10806(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Initiates the repair of damaged proteins by catalyzing methyl
CC esterification of L-isoaspartyl and D-aspartyl residues produced by
CC spontaneous isomerization and racemization of L-aspartyl and L-
CC asparaginyl residues in aging peptides and proteins.
CC {ECO:0000250|UniProtKB:P23506}.
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:0000250|UniProtKB:P23506};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12706;
CC Evidence={ECO:0000250|UniProtKB:P23506};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P22061}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P22061}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U15129; AAB60240.1; -; Genomic_DNA.
DR EMBL; U09669; AAA82166.1; -; mRNA.
DR EMBL; FO080493; CCD64125.1; -; Genomic_DNA.
DR PIR; T32150; T32150.
DR RefSeq; NP_504551.3; NM_072150.5.
DR AlphaFoldDB; Q27873; -.
DR SMR; Q27873; -.
DR BioGRID; 44029; 4.
DR DIP; DIP-25593N; -.
DR STRING; 6239.C10F3.5a; -.
DR EPD; Q27873; -.
DR PaxDb; Q27873; -.
DR EnsemblMetazoa; C10F3.5a.1; C10F3.5a.1; WBGene00003954.
DR GeneID; 178981; -.
DR UCSC; C10F3.5a; c. elegans.
DR CTD; 178981; -.
DR WormBase; C10F3.5a; CE08070; WBGene00003954; pcm-1.
DR eggNOG; KOG1661; Eukaryota.
DR GeneTree; ENSGT00950000183032; -.
DR HOGENOM; CLU_055432_0_4_1; -.
DR InParanoid; Q27873; -.
DR OMA; TISAIHM; -.
DR OrthoDB; 1138104at2759; -.
DR PhylomeDB; Q27873; -.
DR Reactome; R-CEL-5676934; Protein repair.
DR SignaLink; Q27873; -.
DR PRO; PR:Q27873; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003954; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q27873; baseline and differential.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IDA:WormBase.
DR GO; GO:0033555; P:multicellular organismal response to stress; IDA:WormBase.
DR GO; GO:0018197; P:peptidyl-aspartic acid modification; IDA:WormBase.
DR GO; GO:0006479; P:protein methylation; IDA:WormBase.
DR GO; GO:0010506; P:regulation of autophagy; IMP:WormBase.
DR GO; GO:0042594; P:response to starvation; IMP:WormBase.
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 2: Evidence at transcript level;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..225
FT /note="Protein-L-isoaspartate O-methyltransferase"
FT /id="PRO_0000111880"
FT ACT_SITE 60
FT /evidence="ECO:0000250|UniProtKB:Q27869"
FT BINDING 57..60
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P22061"
FT BINDING 65
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P22061"
FT BINDING 89
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P22061"
FT BINDING 110..111
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P22061"
FT BINDING 142..143
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P22061"
FT BINDING 216
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P22061"
FT BINDING 221
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P22061"
SQ SEQUENCE 225 AA; 24767 MW; 004E7D7BBF9D3B85 CRC64;
MAWRSSGSTN SELIDNLRNN RVFASQRAYD AMKSVDRGDF APRAPYEDAP QRIGYNATVS
APHMHAAALD YLQNHLVAGA KALDVGSGSG YLTVCMAMMV GRNGTVVGIE HMPQLVELSE
KNIRKHHSEQ LERGNVIIIE GDGRQGFAEK APYNAIHVGA ASKGVPKALT DQLAEGGRMM
IPVEQVDGNQ VFMQIDKING KIEQKIVEHV IYVPLTSREE QWNRN
