PIMT_PIG
ID PIMT_PIG Reviewed; 227 AA.
AC P80895; Q8SQ35;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 90.
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 {ECO:0000250|UniProtKB:P22061};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Koh E., Hong S.;
RT "Cloning and characterization of porcine brain PCMT.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 6-33.
RA Hong S.;
RL Submitted (FEB-1997) to UniProtKB.
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}.
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DR EMBL; AF239700; AAL83718.1; -; mRNA.
DR RefSeq; NP_001182709.1; NM_001195780.1.
DR AlphaFoldDB; P80895; -.
DR SMR; P80895; -.
DR STRING; 9823.ENSSSCP00000004436; -.
DR PaxDb; P80895; -.
DR PeptideAtlas; P80895; -.
DR PRIDE; P80895; -.
DR Ensembl; ENSSSCT00005006359; ENSSSCP00005003680; ENSSSCG00005004278.
DR GeneID; 100502562; -.
DR KEGG; ssc:100502562; -.
DR CTD; 5110; -.
DR eggNOG; KOG1661; Eukaryota.
DR HOGENOM; CLU_055432_0_0_1; -.
DR InParanoid; P80895; -.
DR OrthoDB; 1138104at2759; -.
DR Reactome; R-SSC-5676934; Protein repair.
DR SABIO-RK; P80895; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P80895; SS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P22061"
FT CHAIN 2..227
FT /note="Protein-L-isoaspartate(D-aspartate) O-
FT methyltransferase"
FT /id="PRO_0000111877"
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"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P22061"
SQ SEQUENCE 227 AA; 24646 MW; F7619EB7BD1A9F9D CRC64;
MAWKSGGASH SELIHNLRKN GIIKTDKVFE VMLATDRSHY AKCNPYMDSP QSIGFQATIS
APHMHAYALE LLFDQLHEGA KALDVGSGSG ILTACFARMV GPSGKVIGID HIKELVDDSI
NNVRKDDPML LSSGRVQLVV GDGRMGYAEE APYDAIHVGA AAPVVPQALI DQLKPGGRLI
LPVGPAGGNQ MLEQYDKLQD GSVKMKPLMG VIYVPLTDKE KQWSRWK
