PIMT_RAT
ID PIMT_RAT Reviewed; 227 AA.
AC P22062; Q5M7V6;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=2730663; DOI=10.1016/0006-291x(89)91602-1;
RA Sato M., Yoshida T., Tuboi S.;
RT "Primary structure of rat brain protein carboxyl methyltransferase deduced
RT from cDNA sequence.";
RL Biochem. Biophys. Res. Commun. 161:342-347(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8263531; DOI=10.1046/j.1471-4159.1994.62010322.x;
RA Mizobuchi M., Murao K., Takeda R., Kakimoto Y.;
RT "Tissue-specific expression of isoaspartyl protein carboxyl
RT methyltransferase gene in rat brain and testis.";
RL J. Neurochem. 62:322-328(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 5-18; 28-37; 82-98; 106-135; 179-197 AND 205-219, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA02034.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M26686; AAA60742.1; -; mRNA.
DR EMBL; D11475; BAA02034.1; ALT_INIT; mRNA.
DR EMBL; BC088417; AAH88417.1; -; mRNA.
DR PIR; A32449; A32449.
DR RefSeq; NP_037205.2; NM_013073.3.
DR AlphaFoldDB; P22062; -.
DR SMR; P22062; -.
DR IntAct; P22062; 1.
DR MINT; P22062; -.
DR STRING; 10116.ENSRNOP00000019623; -.
DR iPTMnet; P22062; -.
DR PhosphoSitePlus; P22062; -.
DR jPOST; P22062; -.
DR PaxDb; P22062; -.
DR PRIDE; P22062; -.
DR GeneID; 25604; -.
DR KEGG; rno:25604; -.
DR UCSC; RGD:3268; rat.
DR CTD; 5110; -.
DR RGD; 3268; Pcmt1.
DR eggNOG; KOG1661; Eukaryota.
DR HOGENOM; CLU_055432_0_0_1; -.
DR InParanoid; P22062; -.
DR OrthoDB; 1138104at2759; -.
DR PhylomeDB; P22062; -.
DR Reactome; R-RNO-5676934; Protein repair.
DR PRO; PR:P22062; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; P22062; RN.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IDA:RGD.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IMP:RGD.
DR GO; GO:0006479; P:protein methylation; IDA:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0046498; P:S-adenosylhomocysteine metabolic process; IDA:RGD.
DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IDA:RGD.
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_0000111878"
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"
FT CONFLICT 83
FT /note="L -> P (in Ref. 1; AAA60742 and 2; BAA02034)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 24641 MW; 833498527365E24F CRC64;
MAWKSGGASH SELIHNLRKN GIIKTDKVFE VMLATDRSHY AKSNPYMDSP QSIGFQATIS
APHMHAYALE LLFDQLHEGA KALDVGSGSG ILTACFARMV GHSGKVIGID HIKELVDDSI
TNVKKDDPML LSSGRVRLVV GDGRMGFAEE APYDAIHVGA AAPVVPQALI DQLKPGGRLI
LPVGPAGGNQ MLEQYDKLQD GSVKMKPLMG VIYVPLTDKE KQWSRWK
