Detail Information for IndEnz0002005430
IED ID IndEnz0002005430
Enzyme Type ID protease005430
Protein Name mRNA-decapping enzyme 1A
EC 3.6.1.62
Smad4-interacting transcriptional co-activator
Transcription factor SMIF
Gene Name DCP1A SMIF
Organism Sus scrofa (Pig)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig)
Enzyme Sequence MESLSRAGQEMSLAALKQHDPYITSIADLTGQVALYTFCPKANQWEKTDIEGTLFVYRRSASPYHGFTIVNRLNMHNLVEPVNKDLEFQLHEPFLLYRNASLSIYSIWFYDKNDCHRIAKLMADVLEEETRRSQQAARDKQSPNQANGCSDHRPIDILEMLSRAKDEYERNQMGDSNISSPGLQPSTQISNLGSTETLEETPSGLQDKSALSGHKHLTVEELFGTSLPKEQPTVVGLESEEVEKLPGDASQKEPSSFLPFSFEPSGGGPQSENMGIRPAAHHSVQPEVTTPVLITPASITQSSEKQAPSYAIPLHPVLSPTLPAEASTAQAPPSLPRSTTMMQAVKTTPRQRSPLSSQPVPELSQASLAASQSPFRAPLNVTNTASTSLPSVDLLQKLRLTQQHDQIQTQSLGKGAVAPSFSPAAGQLATPESFIEPPPKTAAARASASLSNMVLAPLQSMQQNQDPEVFAQPKVLSSAIPVAGPALVTATTSAVSSVLLSPSVFQQTVTRSSDLERKASSPSPLTVGTSENQRKPSIILSKSQLQDTLIHLIKNDSSFLSTLHEVYLQVLTKNKDNHNL
Enzyme Length 580
Uniprot Accession Number I3LHS8
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H(+) + N(7)-methyl-GDP; Xref=Rhea:RHEA:67484, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:63714, ChEBI:CHEBI:138282, ChEBI:CHEBI:156461; EC=3.6.1.62; Evidence={ECO:0000250|UniProtKB:Q9NPI6};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67485; Evidence={ECO:0000250|UniProtKB:Q9NPI6};
DNA Binding
EC Number 3.6.1.62
Enzyme Function FUNCTION: Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Contributes to the transactivation of target genes after stimulation by TGFB1 (By similarity). Essential for embryonic development (By similarity). {ECO:0000250|UniProtKB:Q9NPI6}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Compositional bias (1); Modified residue (16); Region (5); Site (1)
Keywords Cytoplasm;Hydrolase;Methylation;Nonsense-mediated mRNA decay;Nucleus;Phosphoprotein;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9NPI6}. Nucleus {ECO:0000250|UniProtKB:Q9NPI6}. Note=Co-localizes with NANOS3 in the processing bodies (By similarity). Predominantly cytoplasmic, in processing bodies (PB). Nuclear, after TGFB1 treatment. Translocation to the nucleus depends on interaction with SMAD4 (By similarity). {ECO:0000250|UniProtKB:Q91YD3, ECO:0000250|UniProtKB:Q9NPI6}.
Modified Residue MOD_RES 62; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9NPI6; MOD_RES 142; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9NPI6; MOD_RES 179; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q91YD3; MOD_RES 180; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9NPI6; MOD_RES 319; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9NPI6; MOD_RES 334; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9NPI6; MOD_RES 348; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q9NPI6; MOD_RES 353; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9NPI6; MOD_RES 376; /note=Asymmetric dimethylarginine; /evidence=ECO:0000250|UniProtKB:Q9NPI6; MOD_RES 401; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q9NPI6; MOD_RES 422; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9NPI6; MOD_RES 520; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9NPI6; MOD_RES 521; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9NPI6; MOD_RES 523; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9NPI6; MOD_RES 526; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q91YD3; MOD_RES 529; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q9NPI6
Post Translational Modification PTM: (Microbial infection) Cleaved by porcine reproductive and respiratory syndrome virus serine protease nsp4 after Glu-238. The cleavage inhibits DCP1A function. {ECO:0000269|PubMed:30158128}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 62,945
Kinetics
Metal Binding
Rhea ID RHEA:67484; RHEA:67485
Cross Reference Brenda