DCP1A_MOUSE
ID DCP1A_MOUSE Reviewed; 602 AA.
AC Q91YD3; Q6NZE3;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=mRNA-decapping enzyme 1A;
DE EC=3.6.1.62 {ECO:0000250|UniProtKB:Q9NPI6};
DE AltName: Full=MAD homolog 4-interacting transcription coactivator 1;
DE AltName: Full=Smad4-interacting transcriptional co-activator;
DE AltName: Full=Transcription factor SMIF;
GN Name=Dcp1a; Synonyms=Mitc1, Smif;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Swiss Webster;
RX PubMed=11836524; DOI=10.1038/ncb753;
RA Bai R.-Y., Koester C., Ouyang T., Hahn S.A., Hammerschmidt M., Peschel C.,
RA Duyster J.;
RT "SMIF, a Smad4-interacting protein that functions as a co-activator in
RT TGFbeta signalling.";
RL Nat. Cell Biol. 4:181-190(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-481.
RC STRAIN=C57BL/6J; TISSUE=Egg;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543 AND SER-545, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-162; SER-199;
RP SER-200; SER-335; SER-339; SER-372; THR-420; SER-542; SER-543; SER-545 AND
RP THR-548, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=19861488; DOI=10.1530/rep-09-0373;
RA Yamaji M., Tanaka T., Shigeta M., Chuma S., Saga Y., Saitou M.;
RT "Functional reconstruction of NANOS3 expression in the germ cell lineage by
RT a novel transgenic reporter reveals distinct subcellular localizations of
RT NANOS3.";
RL Reproduction 139:381-393(2010).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=33813271; DOI=10.1016/j.bbrc.2021.03.117;
RA Ibayashi M., Aizawa R., Tsukamoto S.;
RT "mRNA decapping factor Dcp1a is essential for embryonic growth in mice.";
RL Biochem. Biophys. Res. Commun. 555:128-133(2021).
CC -!- FUNCTION: Necessary for the degradation of mRNAs, both in normal mRNA
CC turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl
CC guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated
CC mRNA fragment and 7m-GDP. Contributes to the transactivation of target
CC genes after stimulation by TGFB1 (By similarity). Essential for
CC embryonic development (PubMed:11836524). {ECO:0000250|UniProtKB:Q9NPI6,
CC ECO:0000269|PubMed:11836524}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H(+) +
CC N(7)-methyl-GDP; Xref=Rhea:RHEA:67484, Rhea:RHEA-COMP:15692,
CC Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:63714, ChEBI:CHEBI:138282, ChEBI:CHEBI:156461;
CC EC=3.6.1.62; Evidence={ECO:0000250|UniProtKB:Q9NPI6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67485;
CC Evidence={ECO:0000250|UniProtKB:Q9NPI6};
CC -!- SUBUNIT: Forms a complex with EDC3, DCP2, DDX6 and EDC4/HEDLS, within
CC this complex directly interacts with EDC3. Part of a cytoplasmic
CC complex containing proteins involved in mRNA decay, including XRN1 and
CC LSM1. Interacts with DCP1B. Interacts with DCP2. Interacts with DDX17
CC in an RNA-independent manner. Interacts with PNRC2. Interacts with
CC SMAD4. Interacts with UPF1. Interacts with ZC3HAV1. Interacts with
CC ZFP36L1. Interacts with NBDY. Interacts with DHX34; the interaction is
CC RNA-independent (By similarity). {ECO:0000250|UniProtKB:Q9NPI6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:19861488,
CC ECO:0000269|PubMed:33813271}. Nucleus {ECO:0000250|UniProtKB:Q9NPI6}.
CC Note=Predominantly cytoplasmic, in processing bodies (PB). Nuclear,
CC after TGFB1 treatment. Translocation to the nucleus depends on
CC interaction with SMAD4 (By similarity). Colocalizes with NANOS3 in the
CC processing bodies (PubMed:19861488). {ECO:0000250|UniProtKB:Q9NPI6,
CC ECO:0000269|PubMed:19861488}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with highest expression in the spleen
CC and testis (at protein level). {ECO:0000269|PubMed:33813271}.
CC -!- DEVELOPMENTAL STAGE: Expression detectable at 9.5 dpc and progressively
CC increases from 11.5 dpc onwards (at protein level).
CC {ECO:0000269|PubMed:33813271}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality around embryonic day 10.5
CC concomitant with massive growth retardation and cardiac developmental
CC defects seen. {ECO:0000269|PubMed:33813271}.
CC -!- SIMILARITY: Belongs to the DCP1 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-21 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AJ344447; CAC69875.1; -; mRNA.
DR EMBL; BC066173; AAH66173.1; -; mRNA.
DR CCDS; CCDS36848.1; -.
DR RefSeq; NP_598522.3; NM_133761.3.
DR AlphaFoldDB; Q91YD3; -.
DR SMR; Q91YD3; -.
DR BioGRID; 217832; 3.
DR IntAct; Q91YD3; 6.
DR MINT; Q91YD3; -.
DR STRING; 10090.ENSMUSP00000022535; -.
DR iPTMnet; Q91YD3; -.
DR PhosphoSitePlus; Q91YD3; -.
DR EPD; Q91YD3; -.
DR jPOST; Q91YD3; -.
DR MaxQB; Q91YD3; -.
DR PaxDb; Q91YD3; -.
DR PeptideAtlas; Q91YD3; -.
DR PRIDE; Q91YD3; -.
DR ProteomicsDB; 279315; -.
DR Antibodypedia; 73473; 389 antibodies from 34 providers.
DR DNASU; 75901; -.
DR Ensembl; ENSMUST00000022535; ENSMUSP00000022535; ENSMUSG00000021962.
DR Ensembl; ENSMUST00000225196; ENSMUSP00000152897; ENSMUSG00000021962.
DR GeneID; 75901; -.
DR KEGG; mmu:75901; -.
DR UCSC; uc007sva.1; mouse.
DR CTD; 55802; -.
DR MGI; MGI:1923151; Dcp1a.
DR VEuPathDB; HostDB:ENSMUSG00000021962; -.
DR eggNOG; KOG2868; Eukaryota.
DR GeneTree; ENSGT00940000158818; -.
DR HOGENOM; CLU_030030_0_0_1; -.
DR InParanoid; Q91YD3; -.
DR OMA; TPQHDQM; -.
DR OrthoDB; 1509316at2759; -.
DR PhylomeDB; Q91YD3; -.
DR TreeFam; TF320504; -.
DR Reactome; R-MMU-430039; mRNA decay by 5' to 3' exoribonuclease.
DR Reactome; R-MMU-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-MMU-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 75901; 19 hits in 73 CRISPR screens.
DR ChiTaRS; Dcp1a; mouse.
DR PRO; PR:Q91YD3; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q91YD3; protein.
DR Bgee; ENSMUSG00000021962; Expressed in secondary oocyte and 239 other tissues.
DR ExpressionAtlas; Q91YD3; baseline and differential.
DR Genevisible; Q91YD3; MM.
DR GO; GO:0005737; C:cytoplasm; ISA:MGI.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; ISA:MGI.
DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019894; F:kinesin binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR GO; GO:0110156; P:methylguanosine-cap decapping; ISO:MGI.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISA:MGI.
DR GO; GO:1903608; P:protein localization to cytoplasmic stress granule; ISO:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISA:MGI.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR010334; Dcp1.
DR InterPro; IPR031953; mRNA_decap_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR16290; PTHR16290; 1.
DR Pfam; PF06058; DCP1; 1.
DR Pfam; PF16741; mRNA_decap_C; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Methylation; Nonsense-mediated mRNA decay; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..602
FT /note="mRNA-decapping enzyme 1A"
FT /id="PRO_0000189633"
FT REGION 152..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 367
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI6"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 395
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI6"
FT MOD_RES 420
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI6"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 548
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 551
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI6"
FT VARIANT 481
FT /note="Q -> R (in strain: C57BL/6J)"
FT /evidence="ECO:0000269|PubMed:15489334"
SQ SEQUENCE 602 AA; 65219 MW; 55BC9C32BCA86CFD CRC64;
MALSCSTVRP RRRGSALRSK MELLSRAEQE MSLAALKQHD PYITSIADLT GQVALYTFCP
KANQWEKTDI EGTLFVYRRS ASPYHGFTIV NRLNMHNLVE PVNKDLEFQL HEPFLLYRNA
SLSIYSIWFY DKNDCHRIAK LMADVVEEET RRSQQAARDK QSPSQANGCS DQRPIDILEM
LSRAKDEYER NQMGGSNISS PGLQPSTQLS NLGSTETLEE TPSGSQDKSA PSGHKHLTVE
ELFGTSLPKE QPTAMGLESE DTDKLLGDAS QKEPSSFLPF PFEQSGGAPQ SENLGIHSAA
HHTVQPEVST PVLITPASIA QSGDKHPPSY TLPLSPVLSP TLPAEAPTTQ VPHLPRNSTM
IQAVKTTPRQ KSPLLNQPVP ELSHSSLVAS QSPFRAPVSL ANPAGTALPS VDLLQKLRLT
PQHDQIQAQP LGKGTMAPSF SSAAGQLATP ESFIEPSSKT AAARAAVSAS LSNMVLAPTL
QSMQQNQDPE VFSQPKVLPS AIPIAGSPLV PATTTAVSSV LLSPSVFQQT VPRAADLERK
ASSPSPLTVG TAESQRKPSI ILSKSQLQDT LIHLIKNDSS FLSTLHAVYL QVLTKNKDNH
NL
