DCP2_CAEEL
ID DCP2_CAEEL Reviewed; 786 AA.
AC O62255; A0A061ACN4; A0A061ADX7; B3VKU3; O62257; Q2YS49; Q2YS50; Q45F95;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 4.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=m7GpppN-mRNA hydrolase dcap-2 {ECO:0000305};
DE EC=3.6.1.62 {ECO:0000269|PubMed:16199859};
DE AltName: Full=Nudix hydrolase 5 {ECO:0000305};
DE AltName: Full=mRNA-decapping enzyme 2 {ECO:0000312|WormBase:F52G2.1b};
GN Name=dcap-2 {ECO:0000312|WormBase:F52G2.1b};
GN Synonyms=dcp-2 {ECO:0000303|PubMed:16199859,
GN ECO:0000312|WormBase:F52G2.1b}, ndx-5 {ECO:0000312|WormBase:F52G2.1b};
GN ORFNames=F52G2.1 {ECO:0000312|WormBase:F52G2.1b};
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] (ISOFORM A), FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, AND MUTAGENESIS OF GLU-291.
RX PubMed=16199859; DOI=10.1128/mcb.25.20.8779-8791.2005;
RA Cohen L.S., Mikhli C., Jiao X., Kiledjian M., Kunkel G., Davis R.E.;
RT "Dcp2 Decaps m2,2,7GpppN-capped RNAs, and its activity is sequence and
RT context dependent.";
RL Mol. Cell. Biol. 25:8779-8791(2005).
RN [2] {ECO:0000312|EMBL:ACE88255.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RA Boag P.R., Robida S., Blackwell T.K.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18439994; DOI=10.1016/j.ydbio.2008.02.059;
RA Jud M.C., Czerwinski M.J., Wood M.P., Young R.A., Gallo C.M., Bickel J.S.,
RA Petty E.L., Mason J.M., Little B.A., Padilla P.A., Schisa J.A.;
RT "Large P body-like RNPs form in C. elegans oocytes in response to arrested
RT ovulation, heat shock, osmotic stress, and anoxia and are regulated by the
RT major sperm protein pathway.";
RL Dev. Biol. 318:38-51(2008).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25061667; DOI=10.1371/journal.pone.0103365;
RA Rousakis A., Vlanti A., Borbolis F., Roumelioti F., Kapetanou M.,
RA Syntichaki P.;
RT "Diverse functions of mRNA metabolism factors in stress defense and aging
RT of Caenorhabditis elegans.";
RL PLoS ONE 9:e103365-e103365(2014).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF ARG-287.
RX PubMed=28887031; DOI=10.1016/j.bbrc.2017.09.014;
RA Adachi T., Nagahama K., Izumi S.;
RT "The C. elegans mRNA decapping enzyme shapes morphology of cilia.";
RL Biochem. Biophys. Res. Commun. 493:382-387(2017).
RN [7]
RP FUNCTION.
RX PubMed=31983639; DOI=10.1016/j.cub.2019.12.061;
RA Tang N.H., Kim K.W., Xu S., Blazie S.M., Yee B.A., Yeo G.W., Jin Y.,
RA Chisholm A.D.;
RT "The mRNA Decay Factor CAR-1/LSM14 Regulates Axon Regeneration via
RT Mitochondrial Calcium Dynamics.";
RL Curr. Biol. 30:865-876(2020).
CC -!- FUNCTION: Decapping metalloenzyme that catalyzes the cleavage of the
CC cap structure on mRNAs (PubMed:16199859). Removes the 7-methyl guanine
CC cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA
CC fragment and 7m-GDP (PubMed:16199859). RNA-decapping enzyme although it
CC does not bind the RNA cap (PubMed:16199859). May contribute to gene
CC regulation in multiple RNA pathways including monomethylguanosine- and
CC trimethylguanosine-capped RNAs (PubMed:16199859). In oocytes, may play
CC a role in the response to stress induced by heat shock, osmotic stress
CC and anoxia (PubMed:18439994). Required for the developmental axon
CC guidance and regrowth of PLM touch receptor neurons (PubMed:31983639).
CC Early in embryogenesis, plays a role in ciliary shape formation in
CC sensory neurons (PubMed:28887031). Promotes survival at high
CC temperatures (PubMed:25061667). {ECO:0000269|PubMed:16199859,
CC ECO:0000269|PubMed:18439994, ECO:0000269|PubMed:25061667,
CC ECO:0000269|PubMed:28887031, ECO:0000269|PubMed:31983639}.
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:0000269|PubMed:16199859};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67485;
CC Evidence={ECO:0000269|PubMed:16199859};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(2),N(2),N(7)-trimethyl 5'-triphosphoguanosine)-
CC (ribonucleoside) in mRNA + H2O = a 5'-end phospho-ribonucleoside in
CC mRNA + 2 H(+) + N(2),N(2),N(7)-trimethyl-GDP; Xref=Rhea:RHEA:67612,
CC Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17171, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:138282, ChEBI:CHEBI:156463,
CC ChEBI:CHEBI:167623; Evidence={ECO:0000269|PubMed:16199859};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67613;
CC Evidence={ECO:0000269|PubMed:16199859};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8IU60};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8IU60};
CC -!- ACTIVITY REGULATION: Inhibited by capped and uncapped RNA
CC (PubMed:16199859). Not inhibited by dinucleotide cap or methylated
CC nucleotide analogs (PubMed:16199859). {ECO:0000269|PubMed:16199859}.
CC -!- SUBUNIT: May be a component of the decapping complex composed of dcap-1
CC and dcap-2. {ECO:0000250|UniProtKB:P53550}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule
CC {ECO:0000269|PubMed:18439994}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:18439994}. Note=Localizes to perinuclear puncta in
CC pachytene-stage germ cells (PubMed:18439994). Diffusely localized to
CC cytoplasmic puncta in maturing oocytes (PubMed:18439994).
CC {ECO:0000269|PubMed:18439994}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=b {ECO:0000312|WormBase:F52G2.1b};
CC IsoId=O62255-2; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F52G2.1a};
CC IsoId=O62255-1; Sequence=VSP_014286;
CC Name=c {ECO:0000312|WormBase:F52G2.1c};
CC IsoId=O62255-3; Sequence=VSP_060859;
CC Name=d {ECO:0000312|WormBase:F52G2.1d};
CC IsoId=O62255-4; Sequence=VSP_060858;
CC -!- TISSUE SPECIFICITY: Expressed in sensory neurons.
CC {ECO:0000305|PubMed:28887031}.
CC -!- DISRUPTION PHENOTYPE: Double RNAi-mediated knockdown with dcap-1
CC reduces survival at 20 degrees Celsius. {ECO:0000269|PubMed:25061667}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DCP2 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACE88255.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ143943; AAZ73241.1; -; mRNA.
DR EMBL; EU760346; ACE88255.1; ALT_INIT; mRNA.
DR EMBL; BX284604; CAB05204.2; -; Genomic_DNA.
DR EMBL; AL021488; CAB05204.2; JOINED; Genomic_DNA.
DR EMBL; BX284604; CAB05206.4; -; Genomic_DNA.
DR EMBL; AL021488; CAB05206.4; JOINED; Genomic_DNA.
DR EMBL; BX284604; CDR32703.1; -; Genomic_DNA.
DR EMBL; BX284604; CDR32704.1; -; Genomic_DNA.
DR PIR; E88886; E88886.
DR PIR; T22515; T22515.
DR RefSeq; NP_001293937.1; NM_001307008.1. [O62255-3]
DR RefSeq; NP_001293938.1; NM_001307009.1. [O62255-4]
DR RefSeq; NP_502608.3; NM_070207.5. [O62255-1]
DR RefSeq; NP_502609.2; NM_070208.3. [O62255-2]
DR AlphaFoldDB; O62255; -.
DR SMR; O62255; -.
DR BioGRID; 43406; 1.
DR STRING; 6239.F52G2.1b; -.
DR iPTMnet; O62255; -.
DR PaxDb; O62255; -.
DR PeptideAtlas; O62255; -.
DR PRIDE; O62255; -.
DR EnsemblMetazoa; F52G2.1a.1; F52G2.1a.1; WBGene00003582. [O62255-1]
DR EnsemblMetazoa; F52G2.1b.1; F52G2.1b.1; WBGene00003582. [O62255-2]
DR EnsemblMetazoa; F52G2.1c.1; F52G2.1c.1; WBGene00003582. [O62255-3]
DR EnsemblMetazoa; F52G2.1d.1; F52G2.1d.1; WBGene00003582. [O62255-4]
DR GeneID; 178321; -.
DR KEGG; cel:CELE_F52G2.1; -.
DR UCSC; F52G2.1b; c. elegans. [O62255-2]
DR CTD; 178321; -.
DR WormBase; F52G2.1a; CE42539; WBGene00003582; dcap-2. [O62255-1]
DR WormBase; F52G2.1b; CE39374; WBGene00003582; dcap-2. [O62255-2]
DR WormBase; F52G2.1c; CE49837; WBGene00003582; dcap-2. [O62255-3]
DR WormBase; F52G2.1d; CE49931; WBGene00003582; dcap-2. [O62255-4]
DR eggNOG; KOG2937; Eukaryota.
DR GeneTree; ENSGT00390000018878; -.
DR HOGENOM; CLU_401282_0_0_1; -.
DR InParanoid; O62255; -.
DR OMA; NDNIRVC; -.
DR OrthoDB; 647130at2759; -.
DR Reactome; R-CEL-430039; mRNA decay by 5' to 3' exoribonuclease.
DR Reactome; R-CEL-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR PRO; PR:O62255; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003582; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; O62255; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IDA:WormBase.
DR GO; GO:0000932; C:P-body; IDA:WormBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; IDA:WormBase.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IDA:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0040012; P:regulation of locomotion; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0009408; P:response to heat; IMP:WormBase.
DR GO; GO:0006979; P:response to oxidative stress; IMP:WormBase.
DR GO; GO:0009411; P:response to UV; IMP:WormBase.
DR CDD; cd03672; Dcp2p; 1.
DR Gene3D; 1.10.10.1050; -; 1.
DR InterPro; IPR007722; DCP2_BoxA.
DR InterPro; IPR036189; DCP2_BoxA_sf.
DR InterPro; IPR044099; Dcp2_NUDIX.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF05026; DCP2; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SMART; SM01125; DCP2; 1.
DR SUPFAM; SSF140586; SSF140586; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase; Magnesium; Manganese;
KW Metal-binding; mRNA processing; Nonsense-mediated mRNA decay;
KW Reference proteome; RNA-binding.
FT CHAIN 1..786
FT /note="m7GpppN-mRNA hydrolase dcap-2"
FT /id="PRO_0000057135"
FT DOMAIN 238..366
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 25..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 273..294
FT /note="Nudix box"
FT COMPBIAS 25..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..190
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_060858"
FT VAR_SEQ 1..100
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_060859"
FT VAR_SEQ 2..25
FT /note="EISTENWCKKPKNRSIFSKNISFQ -> ASNSTNSK (in isoform a)"
FT /evidence="ECO:0000303|PubMed:16199859"
FT /id="VSP_014286"
FT MUTAGEN 287
FT /note="R->E: In var1; defective ADL, ADF, AWB and AWC
FT sensory neuron cilia."
FT /evidence="ECO:0000269|PubMed:28887031"
FT MUTAGEN 291
FT /note="E->Q: Abolishes mRNA decapping activity."
FT /evidence="ECO:0000269|PubMed:16199859"
FT CONFLICT 1..25
FT /note="MEISTENWCKKPKNRSIFSKNISFQ -> MASNSTNSK (in Ref. 2;
FT ACE88255)"
FT /evidence="ECO:0000305"
FT CONFLICT 214..786
FT /note="Missing (in Ref. 2; ACE88255)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 786 AA; 87369 MW; 45753599CA77D9B9 CRC64;
MEISTENWCK KPKNRSIFSK NISFQKQNKS TEEPPSSVQK LLASLQQAQN KSDLSEQPST
SKPKKNEKRK KAVAQAPASA PAPGPEEKKK QPKRASVGAR MQQQAENARI SQTKRPRQVS
TSKGSSRNTT APEQQNYQQQ QQQYKGPRIP TDILDELEFR FISNMVECEI NDNIRVCFHL
ELAHWYYIDH MVEDDKISGC PNVGSRDFNF QMCQHCRVLR KYAHRADEVL AKFREYKSTV
PTYGAILVDP EMDHVVLVQS YFAKGKNWGF PKGKINQAEP PRDAAIRETF EETGFDFGIY
SEKEKKFQRF INDGMVRLYL VKNVPKDFNF QPQTRKEIRK IEWFKIDDLP TDKTDELPAY
LQGNKFYMVM PFVKDIQIYV QKEKEKLRRR KAEAVQSTPS SSIFSQLFPA QPPPPVPEDA
TPTRPMYKRL TSEELFSAFK NPPAGEVARP TLPDMSPAVN GLDTLAVLGI CTPLKPGASL
NEFSGAPQNC PMISEEAGSP ADPSAEIGFA MPMDLKQPVV TSDHPWQHHK ISDSSAPPQT
LESHQGWLDT QLVNTIMHSP NHPLPPTSNS PATPTAVLGH LIGKPIQPQA ILPQAATPTA
LGSAEKPKSS RISLSDNSAF KAISSTQKQS IPKATAAPPS TEKTRSASLS GSSQVVGKPA
RNLFNSVVSP VSSGIQSIQG DGGAWEDVWF REQLAATTTA GTSISSLAAS NQELAMINRE
ETPIEDPYFK QQAYQKAQKA QSLIPACSQW TNSIKLDIDY VVGPLSFWMQ QFSTKSPVSG
TGPQLP
