PIMT_BOVIN
ID PIMT_BOVIN Reviewed; 227 AA.
AC P15246; Q32LB2;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 147.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-227 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=2777770; DOI=10.1016/s0021-9258(18)71564-0;
RA Henzel W.J., Stults J.T., Hsu C.-A., Aswad D.W.;
RT "The primary structure of a protein carboxyl methyltransferase from bovine
RT brain that selectively methylates L-isoaspartyl sites.";
RL J. Biol. Chem. 264:15905-15911(1989).
RN [3]
RP PROTEIN SEQUENCE OF 5-17; 37-62; 106-133 AND 136-221.
RX PubMed=3167043; DOI=10.1021/bi00414a042;
RA Gilbert J.M., Fowler A., Bleibaum J., Clarke S.;
RT "Purification of homologous protein carboxyl methyltransferase isozymes
RT from human and bovine erythrocytes.";
RL Biochemistry 27:5227-5233(1988).
RN [4]
RP PROTEIN SEQUENCE OF 5-11; 48-65; 74-83; 106-136; 144-195 AND 200-225
RP (ISOFORM 2).
RX PubMed=1627573; DOI=10.1021/bi00142a025;
RA Potter S.M., Johnson B.A., Henschen A., Aswad D.W., Guzzetta A.W.;
RT "The type II isoform of bovine brain protein L-isoaspartyl
RT methyltransferase has an endoplasmic reticulum retention signal (RDEL) at
RT its C-terminus.";
RL Biochemistry 31:6339-6347(1992).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P15246-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P15246-2; Sequence=VSP_012044;
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family. {ECO:0000305}.
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DR EMBL; BC109663; AAI09664.1; -; mRNA.
DR PIR; A43292; A43292.
DR RefSeq; NP_001073085.1; NM_001079617.2.
DR AlphaFoldDB; P15246; -.
DR SMR; P15246; -.
DR STRING; 9913.ENSBTAP00000055150; -.
DR PaxDb; P15246; -.
DR PeptideAtlas; P15246; -.
DR PRIDE; P15246; -.
DR GeneID; 613854; -.
DR KEGG; bta:613854; -.
DR CTD; 5110; -.
DR eggNOG; KOG1661; Eukaryota.
DR HOGENOM; CLU_055432_0_4_1; -.
DR InParanoid; P15246; -.
DR OrthoDB; 1138104at2759; -.
DR Proteomes; UP000009136; Unplaced.
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; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW 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_0000111874"
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 VAR_SEQ 226..227
FT /note="WK -> DEL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_012044"
FT CONFLICT 133
FT /note="S -> T (in Ref. 1; AAI09664)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 24565 MW; 8566921A7B7AFE37 CRC64;
MAWKSGGASH SELIHNLRKN GIIKTDKVFE VMLATDRSHY AKCNPYMDSP QSIGFQATIS
APHMHAYALE LLFDQLNEGA KALDVGSGSG ILTACFARMV GPSGKVIGID HIKELVDDSI
NNVRKDDPML LSSGRVQLVV GDGRMGYAAE APYDAIHVGA AAPVVPQALI DQLKPGGRLI
LPVGPAGGNQ MLEQYDKLQD GSVKMKPLMG VIYVPLTDKE KQWSRWK
