ID   PIMT_PONAB              Reviewed;         227 AA.
AC   Q5RA89;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Protein-L-isoaspartate(D-aspartate) 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/D-aspartyl methyltransferase;
DE   AltName: Full=Protein-beta-aspartate methyltransferase;
GN   Name=PCMT1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       Acts on EIF4EBP2, microtubule-associated protein 2, calreticulin,
CC       clathrin light chains a and b, Ubiquitin C-terminal hydrolase isozyme
CC       L1, phosphatidylethanolamine-binding protein 1, stathmin, beta-
CC       synuclein and alpha-synuclein (By similarity).
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAH91321.1; Type=Erroneous initiation; Evidence={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; CR859129; CAH91321.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001125781.1; NM_001132309.1.
DR   AlphaFoldDB; Q5RA89; -.
DR   SMR; Q5RA89; -.
DR   STRING; 9601.ENSPPYP00000019138; -.
DR   GeneID; 100172708; -.
DR   KEGG; pon:100172708; -.
DR   CTD; 5110; -.
DR   eggNOG; KOG1661; Eukaryota.
DR   InParanoid; Q5RA89; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0006479; P:protein methylation; ISS: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   2: Evidence at transcript level;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..227
FT                   /note="Protein-L-isoaspartate(D-aspartate) O-
FT                   methyltransferase"
FT                   /id="PRO_0000253634"
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         217
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P22061"
FT   BINDING         222
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P22061"
SQ   SEQUENCE   227 AA;  24622 MW;  58370AADD3C674ED CRC64;
     MGWKSGGASH SELIHNLRKN GIIKTDKVFE VMLATDRSHY AKCNPYMDSP QSIGFQATIS
     APHMHAYALE LLFDQLHEGA KALDVGSGSG ILTACFARMV GCTGKVIGID HIKELVDDSI
     NNVRKDDPTL LSSGRVQLVV GDGRMGYAEE APYDAIHVGA AAPVVPQALI DQLKPGGRLI
     LPVGPAGGNQ MLEQYDKLQD GSVKMKPLMG VIYVPLTDKE KQWSRWK