DCP1A_PIG
ID DCP1A_PIG Reviewed; 580 AA.
AC I3LHS8;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=mRNA-decapping enzyme 1A;
DE EC=3.6.1.62 {ECO:0000250|UniProtKB:Q9NPI6};
DE AltName: Full=Smad4-interacting transcriptional co-activator;
DE AltName: Full=Transcription factor SMIF;
GN Name=DCP1A; Synonyms=SMIF;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP CLEAVAGE BY PORCINE REPRODUCTIVE AND RESPIRATORY SYNDROME VIRUS SERINE
RP PROTEASE NSP4 (MICROBIAL INFECTION).
RX PubMed=30158128; DOI=10.4049/jimmunol.1701773;
RA Tao R., Fang L., Bai D., Ke W., Zhou Y., Wang D., Xiao S.;
RT "Porcine Reproductive and Respiratory Syndrome Virus Nonstructural Protein
RT 4 Cleaves Porcine DCP1a To Attenuate Its Antiviral Activity.";
RL J. Immunol. 201:2345-2353(2018).
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 (By similarity). {ECO:0000250|UniProtKB:Q9NPI6}.
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:0000250|UniProtKB:Q9NPI6}.
CC Nucleus {ECO:0000250|UniProtKB:Q9NPI6}. Note=Co-localizes with NANOS3
CC in the processing bodies (By similarity). Predominantly cytoplasmic, in
CC processing bodies (PB). Nuclear, after TGFB1 treatment. Translocation
CC to the nucleus depends on interaction with SMAD4 (By similarity).
CC {ECO:0000250|UniProtKB:Q91YD3, ECO:0000250|UniProtKB:Q9NPI6}.
CC -!- PTM: (Microbial infection) Cleaved by porcine reproductive and
CC respiratory syndrome virus serine protease nsp4 after Glu-238. The
CC cleavage inhibits DCP1A function. {ECO:0000269|PubMed:30158128}.
CC -!- SIMILARITY: Belongs to the DCP1 family. {ECO:0000305}.
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DR EMBL; AEMK02000086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3LHS8; -.
DR SMR; I3LHS8; -.
DR STRING; 9823.ENSSSCP00000023625; -.
DR PaxDb; I3LHS8; -.
DR PeptideAtlas; I3LHS8; -.
DR PRIDE; I3LHS8; -.
DR Ensembl; ENSSSCT00000023022; ENSSSCP00000023625; ENSSSCG00000022616.
DR VGNC; VGNC:97960; DCP1A.
DR eggNOG; KOG2868; Eukaryota.
DR GeneTree; ENSGT00940000158818; -.
DR HOGENOM; CLU_030030_0_0_1; -.
DR InParanoid; I3LHS8; -.
DR OMA; TPQHDQM; -.
DR TreeFam; TF320504; -.
DR Reactome; R-SSC-430039; mRNA decay by 5' to 3' exoribonuclease.
DR Reactome; R-SSC-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-SSC-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR Proteomes; UP000008227; Chromosome 13.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000022616; Expressed in stomach and 43 other tissues.
DR ExpressionAtlas; I3LHS8; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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: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 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..580
FT /note="mRNA-decapping enzyme 1A"
FT /id="PRO_0000445605"
FT REGION 132..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 238..239
FT /note="(Microbial infection) Cleavage; by porcine
FT reproductive and respiratory syndrome virus serine protease
FT nsp4"
FT /evidence="ECO:0000269|PubMed:30158128"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI6"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI6"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YD3"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI6"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI6"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI6"
FT MOD_RES 348
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI6"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI6"
FT MOD_RES 376
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI6"
FT MOD_RES 401
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI6"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI6"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI6"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI6"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI6"
FT MOD_RES 526
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q91YD3"
FT MOD_RES 529
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI6"
SQ SEQUENCE 580 AA; 62945 MW; E999A4DD4D14434A CRC64;
MESLSRAGQE MSLAALKQHD PYITSIADLT GQVALYTFCP KANQWEKTDI EGTLFVYRRS
ASPYHGFTIV NRLNMHNLVE PVNKDLEFQL HEPFLLYRNA SLSIYSIWFY DKNDCHRIAK
LMADVLEEET RRSQQAARDK QSPNQANGCS DHRPIDILEM LSRAKDEYER NQMGDSNISS
PGLQPSTQIS NLGSTETLEE TPSGLQDKSA LSGHKHLTVE ELFGTSLPKE QPTVVGLESE
EVEKLPGDAS QKEPSSFLPF SFEPSGGGPQ SENMGIRPAA HHSVQPEVTT PVLITPASIT
QSSEKQAPSY AIPLHPVLSP TLPAEASTAQ APPSLPRSTT MMQAVKTTPR QRSPLSSQPV
PELSQASLAA SQSPFRAPLN VTNTASTSLP SVDLLQKLRL TQQHDQIQTQ SLGKGAVAPS
FSPAAGQLAT PESFIEPPPK TAAARASASL SNMVLAPLQS MQQNQDPEVF AQPKVLSSAI
PVAGPALVTA TTSAVSSVLL SPSVFQQTVT RSSDLERKAS SPSPLTVGTS ENQRKPSIIL
SKSQLQDTLI HLIKNDSSFL STLHEVYLQV LTKNKDNHNL
