DCPS_CAEEL
ID DCPS_CAEEL Reviewed; 311 AA.
AC G5EFS4;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=m7GpppX diphosphatase;
DE EC=3.6.1.59 {ECO:0000269|PubMed:12871939, ECO:0000269|PubMed:15383679, ECO:0000269|PubMed:22985415};
DE AltName: Full=Decapping scavenger enzyme;
DE AltName: Full=Heat shock-like protein;
DE AltName: Full=Protein DCS-1;
DE AltName: Full=Scavenger mRNA-decapping enzyme DcpS;
GN Name=dcs-1; Synonyms=hsl-1; ORFNames=Y113G7A.9;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, SUBCELLULAR
RP LOCALIZATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12871939; DOI=10.1074/jbc.m306355200;
RA Kwasnicka D.A., Krakowiak A., Thacker C., Brenner C., Vincent S.R.;
RT "Coordinate expression of NADPH-dependent flavin reductase, Fre-1, and
RT Hint-related 7meGMP-directed hydrolase, DCS-1.";
RL J. Biol. Chem. 278:39051-39058(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=15383679; DOI=10.1261/rna.7690504;
RA Cohen L.S., Mikhli C., Friedman C., Jankowska-Anyszka M., Stepinski J.,
RA Darzynkiewicz E., Davis R.E.;
RT "Nematode m7GpppG and m3(2,2,7)GpppG decapping: activities in Ascaris
RT embryos and characterization of C. elegans scavenger DcpS.";
RL RNA 10:1609-1624(2004).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND ACTIVITY
RP REGULATION.
RX PubMed=22985415; DOI=10.1021/bi300781g;
RA Wypijewska A., Bojarska E., Lukaszewicz M., Stepinski J., Jemielity J.,
RA Davis R.E., Darzynkiewicz E.;
RT "7-Methylguanosine diphosphate (m(7)GDP) is not hydrolyzed but strongly
RT bound by decapping scavenger (dcpS) enzymes and potently inhibits their
RT activity.";
RL Biochemistry 51:8003-8013(2012).
CC -!- FUNCTION: Decapping scavenger enzyme that catalyzes the cleavage of a
CC residual cap structure following the degradation of mRNAs of the 3'->5'
CC exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures
CC like 7-methylguanosine nucleoside triphosphate (m7GpppG) and tri-methyl
CC guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with up to 2
CC nucleotide substrates (small capped oligoribonucleotides) and
CC specifically releases 5'-phosphorylated RNA fragments and 7-
CC methylguanosine monophosphate (m7GMP). Does not hydrolyze unmethylated
CC cap analog (GpppG) and shows no decapping activity on intact m7GpppG-
CC capped mRNA molecules. Does not hydrolyze 7-methylguanosine diphosphate
CC (m7GDP) and tri-methylguanosine diphosphate (m3(2,2,7)GDP) to m(7)GMP
CC and m3(2,2,7)GMP, respectively (PubMed:22985415). May also play a role
CC in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released
CC by the 5'->3' mRNA mediated decapping activity, may be also converted
CC by dcs-1 to m7GMP. Binds to m7GpppG and strongly to m7GDP.
CC {ECO:0000269|PubMed:12871939, ECO:0000269|PubMed:15383679,
CC ECO:0000269|PubMed:22985415}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + 2 H(+) +
CC N(7)-methyl-GMP; Xref=Rhea:RHEA:65388, Rhea:RHEA-COMP:17165,
CC Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58285, ChEBI:CHEBI:156461, ChEBI:CHEBI:167616;
CC EC=3.6.1.59; Evidence={ECO:0000269|PubMed:12871939,
CC ECO:0000269|PubMed:15383679, ECO:0000269|PubMed:22985415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(2),N(2),N(7)-trimethyl 5'-triphosphoguanosine)-
CC (ribonucleoside) in mRNA + H2O = (N(2),N(2),N(7))-trimethyl-GMP + a
CC 5'-end diphospho-ribonucleoside in mRNA + 2 H(+);
CC Xref=Rhea:RHEA:65384, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17171,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74434,
CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167623; EC=3.6.1.59;
CC Evidence={ECO:0000269|PubMed:15383679};
CC -!- ACTIVITY REGULATION: The hydrolytic product 7-methylguanosine
CC diphosphate (m7GDP) efficiently inhibits the decapping scavenger
CC activity and acts as a competitive inhibitor in vitro.
CC {ECO:0000269|PubMed:22985415}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 uM for m7GpppBODIPY {ECO:0000269|PubMed:12871939};
CC KM=8.52 uM for GpppBODIPY {ECO:0000269|PubMed:12871939};
CC KM=5.04 uM for ApppBODIPY {ECO:0000269|PubMed:12871939};
CC Note=kcat is 0.174 sec(-1) with m7GpppBODIPY as substrate. The
CC catalytic efficiency with m7GpppBODIPY is at least 35- to 75-fold
CC higher than with ApppBODIPY and GpppBODIPY as substrates,
CC respectively.;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in neurons in the ventral cord, the nerve
CC ring and the pharynx. {ECO:0000269|PubMed:12871939}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryo during all developmental
CC stages. {ECO:0000269|PubMed:12871939}.
CC -!- INDUCTION: Up-regulated by heat schock. {ECO:0000269|PubMed:12871939}.
CC -!- SIMILARITY: Belongs to the HIT family. {ECO:0000305}.
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DR EMBL; AL132858; CAB60481.1; -; Genomic_DNA.
DR EMBL; AY079166; AAL86013.1; -; mRNA.
DR RefSeq; NP_001256897.1; NM_001269968.1.
DR AlphaFoldDB; G5EFS4; -.
DR SMR; G5EFS4; -.
DR BioGRID; 45275; 7.
DR STRING; 6239.Y113G7A.9a; -.
DR EPD; G5EFS4; -.
DR PaxDb; G5EFS4; -.
DR PeptideAtlas; G5EFS4; -.
DR EnsemblMetazoa; Y113G7A.9a.1; Y113G7A.9a.1; WBGene00000940.
DR GeneID; 180315; -.
DR KEGG; cel:CELE_Y113G7A.9; -.
DR CTD; 180315; -.
DR WormBase; Y113G7A.9a; CE23280; WBGene00000940; dcs-1.
DR eggNOG; KOG3969; Eukaryota.
DR GeneTree; ENSGT00390000003924; -.
DR HOGENOM; CLU_041045_2_0_1; -.
DR InParanoid; G5EFS4; -.
DR OMA; WVYNCLE; -.
DR OrthoDB; 930557at2759; -.
DR PhylomeDB; G5EFS4; -.
DR BRENDA; 3.6.1.59; 1045.
DR Reactome; R-CEL-429958; mRNA decay by 3' to 5' exoribonuclease.
DR PRO; PR:G5EFS4; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000940; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; G5EFS4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0047627; F:adenylylsulfatase activity; IDA:WormBase.
DR GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IDA:UniProtKB.
DR GO; GO:0004780; F:sulfate adenylyltransferase (ADP) activity; IDA:WormBase.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR GO; GO:0110156; P:methylguanosine-cap decapping; IDA:WormBase.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:WormBase.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; TAS:UniProtKB.
DR GO; GO:0009150; P:purine ribonucleotide metabolic process; IDA:WormBase.
DR GO; GO:0009408; P:response to heat; IDA:UniProtKB.
DR GO; GO:0006401; P:RNA catabolic process; IDA:WormBase.
DR GO; GO:0006790; P:sulfur compound metabolic process; IDA:WormBase.
DR Gene3D; 3.30.200.40; -; 1.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR008594; DcpS/DCS2.
DR InterPro; IPR036265; HIT-like_sf.
DR InterPro; IPR011145; Scavenger_mRNA_decap_enz_N.
DR PANTHER; PTHR12978; PTHR12978; 1.
DR Pfam; PF05652; DcpS; 1.
DR PIRSF; PIRSF028973; Scavenger_mRNA_decap_enz; 1.
DR SUPFAM; SSF102860; SSF102860; 1.
DR SUPFAM; SSF54197; SSF54197; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Nucleus; Reference proteome; Stress response.
FT CHAIN 1..311
FT /note="m7GpppX diphosphatase"
FT /id="PRO_0000420574"
FT MOTIF 249..253
FT /note="Histidine triad motif"
FT /evidence="ECO:0000250"
FT ACT_SITE 251
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 242..253
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 311 AA; 36477 MW; CDA66CEF8052E63F CRC64;
MKRIADEELV REERAEESTQ KWLQDAKFQE ILGADSSHKS LFVLLSHPDG SQGILLANKS
PFSEEKSDIE KLLATAQLQE ISRNDIFGSY NIEIDPKLNL LKSQLIYPIN DRLIAKYRQE
EKFVIRETPE LYETVTRPYI EKYQLNLNWV YNCLEKRSEV DKIVFEDPDN ENGFVLLQDI
KWDGKTLENL YVLAICHRHG LKSVRDLTGD DLEMLYNMRD KSLEAINQKY GLKTDQIKCY
FHYQPSFYHL HVHFINLKYD APASTTMSAI LLDDVINNLE LNPEHYKKST LTFTRKNGDK
LMEMFREALK N
