ID   PIMT_MACFA              Reviewed;         227 AA.
AC   Q4R5H0;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Protein-L-isoaspartate(D-aspartate) O-methyltransferase;
DE            Short=PIMT;
DE            EC=2.1.1.77;
DE   AltName: Full=Protein-beta-aspartate methyltransferase;
DE   AltName: Full=Protein L-isoaspartyl/D-aspartyl methyltransferase;
DE   AltName: Full=L-isoaspartyl protein carboxyl methyltransferase;
GN   Name=PCMT1; ORFNames=QnpA-11118;
OS   Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Parietal cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl and
CC       D-aspartyl residues in peptides and proteins that result from
CC       spontaneous decomposition of normal L-aspartyl and L-asparaginyl
CC       residues. It plays a role in the repair and/or degradation of
CC       damaged proteins. Acts on microtubule-associated protein 2,
CC       calreticulin, clathrin light chains a and b, Ubiquitin carboxyl-
CC       terminal hydrolase isozyme L1, phosphatidylethanolamine-binding
CC       protein 1, stathmin, beta-synuclein and alpha-synuclein (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + protein L-
CC       isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate
CC       alpha-methyl ester.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the L-isoaspartyl/D-aspartyl protein
CC       methyltransferase family.
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DR   EMBL; AB169573; BAE01655.1; ALT_INIT; mRNA.
DR   SMR; Q4R5H0; 3-226.
DR   HOVERGEN; Q4R5H0; -.
DR   BRENDA; 2.1.1.77; 3438.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-meth...; IEA:EC.
DR   GO; GO:0006464; P:protein modification process; IEA:InterPro.
DR   InterPro; IPR000682; PCMT.
DR   PANTHER; PTHR11579; PCMT; 1.
DR   Pfam; PF01135; PCMT; 1.
DR   TIGRFAMs; TIGR00080; pimt; 1.
DR   PROSITE; PS01279; PCMT; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    227       Protein-L-isoaspartate(D-aspartate) O-
FT                                methyltransferase.
FT                                /FTId=PRO_0000253633.
FT   ACT_SITE     60     60       By similarity.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
SQ   SEQUENCE   227 AA;  24637 MW;  8EAAA2EC606402A8 CRC64;
     MAWKSGGASH SELIHNLRKN GIIKTDKVFE VMLATDRSHY AECNPYMDSP QSIGFQATIS
     APHMHAYALE LLFDQLHEGA KALDVGSGSG ILTACFARMV GCTGKVIGID HIKELVDDSI
     NNVRKDDPTL LSSGRVQLVV GDGRMGYAEE APYDAIHVGA AAPVVPQALI DQLKPGGRLI
     LPVGPAGGNQ MLEQYDKLQD GSVKMKPLMG VIYVPLTDKE KQWSRWK
//