ID E0CYV0_MOUSE Unreviewed; 286 AA.
AC E0CYV0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Protein-L-isoaspartate O-methyltransferase {ECO:0000256|RuleBase:RU003802};
DE EC=2.1.1.77 {ECO:0000256|RuleBase:RU003802};
GN Name=Pcmt1 {ECO:0000313|Ensembl:ENSMUSP00000123866.3,
GN ECO:0000313|MGI:MGI:97502};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000123866.3, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000123866.3, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000123866.3,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000123866.3}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000123866.3};
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
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:0000256|ARBA:ARBA00035815};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12706;
CC Evidence={ECO:0000256|ARBA:ARBA00035815};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005369, ECO:0000256|RuleBase:RU003802}.
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DR RefSeq; NP_001334157.1; NM_001347228.1.
DR AlphaFoldDB; E0CYV0; -.
DR SMR; E0CYV0; -.
DR SwissPalm; E0CYV0; -.
DR jPOST; E0CYV0; -.
DR MaxQB; E0CYV0; -.
DR PeptideAtlas; E0CYV0; -.
DR ProteomicsDB; 304615; -.
DR Antibodypedia; 759; 312 antibodies from 31 providers.
DR DNASU; 18537; -.
DR Ensembl; ENSMUST00000162606.8; ENSMUSP00000123866.3; ENSMUSG00000019795.18.
DR GeneID; 18537; -.
DR UCSC; uc007ehy.2; mouse.
DR AGR; MGI:97502; -.
DR CTD; 5110; -.
DR MGI; MGI:97502; Pcmt1.
DR VEuPathDB; HostDB:ENSMUSG00000019795; -.
DR OrthoDB; 303909at2759; -.
DR PhylomeDB; E0CYV0; -.
DR BioGRID-ORCS; 18537; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Pcmt1; mouse.
DR Proteomes; UP000000589; Chromosome 10.
DR Bgee; ENSMUSG00000019795; Expressed in spermatocyte and 63 other cell types or tissues.
DR ExpressionAtlas; E0CYV0; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR000682; PCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00080; pimt; 1.
DR PANTHER; PTHR11579; PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11579:SF7; PROTEIN-L-ISOASPARTATE(D-ASPARTATE) O-METHYLTRANSFERASE; 1.
DR Pfam; PF01135; PCMT; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS01279; PCMT; 1.
PE 1: Evidence at protein level;
KW Methyltransferase {ECO:0000256|RuleBase:RU003802};
KW Proteomics identification {ECO:0007829|EPD:E0CYV0,
KW ECO:0007829|MaxQB:E0CYV0};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU003802};
KW Transferase {ECO:0000256|RuleBase:RU003802}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 286 AA; 30441 MW; A77D3B0B86C0E09F CRC64;
MPGARIGGSG SDGSNSGRSS GDTSGAVTVW EVVSLLGKLL GTVAALKVVL YLLRVCFAMA
WKSGGASHSE LIHNLRKNGI IKTDKVFEVM LATDRSHYAK SNPYMDSPQS IGFQATISAP
HMHAYALELL FDQLHEGAKA LDVGSGSGIL TACFARMVGN SGKVIGIDHI KELVDDSITN
VKKDDPMLLS SGRVRLVVGD GRMGYAEEAP YDAIHVGAAA PVVPQALIDQ LKPGGRLILP
VGPAGGNQML EQYDKLQDGS VKMKPLMGVI YVPLTDKEKQ WSRDEL
//
