ID A0A3P8WI04_CYNSE Unreviewed; 390 AA.
AC A0A3P8WI04;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 28-JAN-2026, entry version 33.
DE RecName: Full=m7GpppN-mRNA hydrolase {ECO:0000256|ARBA:ARBA00068566};
DE EC=3.6.1.62 {ECO:0000256|ARBA:ARBA00026102};
DE AltName: Full=mRNA-decapping enzyme 2 {ECO:0000256|ARBA:ARBA00078183};
OS Cynoglossus semilaevis (Tongue sole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC Cynoglossinae; Cynoglossus.
OX NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000026369.1, ECO:0000313|Proteomes:UP000265120};
RN [1] {ECO:0000313|Ensembl:ENSCSEP00000026369.1, ECO:0000313|Proteomes:UP000265120}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24487278; DOI=10.1038/ng.2890;
RA Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA Zhao Y., Schartl M., Tang Q., Wang J.;
RT "Whole-genome sequence of a flatfish provides insights into ZW sex
RT chromosome evolution and adaptation to a benthic lifestyle.";
RL Nat. Genet. 46:253-260(2014).
RN [2] {ECO:0000313|Ensembl:ENSCSEP00000026369.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSCSEP00000026369.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Decapping metalloenzyme that catalyzes the cleavage of the
CC cap structure on mRNAs. Removes the 7-methyl guanine cap structure from
CC mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP.
CC Necessary for the degradation of mRNAs, both in normal mRNA turnover
CC and in nonsense-mediated mRNA decay. Plays a role in replication-
CC dependent histone mRNA degradation. Has higher activity towards mRNAs
CC that lack a poly(A) tail. Has no activity towards a cap structure
CC lacking an RNA moiety. The presence of a N(6)-methyladenosine
CC methylation at the second transcribed position of mRNAs (N(6),2'-O-
CC dimethyladenosine cap; m6A(m)) provides resistance to DCP2-mediated
CC decapping. Blocks autophagy in nutrient-rich conditions by repressing
CC the expression of ATG-related genes through degradation of their
CC transcripts. {ECO:0000256|ARBA:ARBA00060003}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + H2O = N(7)-methyl-GDP + a 5'-end phospho-ribonucleoside in
CC mRNA + 2 H(+); Xref=Rhea:RHEA:67484, Rhea:RHEA-COMP:15692, Rhea:RHEA-
CC COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:63714,
CC ChEBI:CHEBI:138282, ChEBI:CHEBI:156461; EC=3.6.1.62;
CC Evidence={ECO:0000256|ARBA:ARBA00047661};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67485;
CC Evidence={ECO:0000256|ARBA:ARBA00047661};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC {ECO:0000256|ARBA:ARBA00004201}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DCP2 subfamily.
CC {ECO:0000256|ARBA:ARBA00005279}.
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DR RefSeq; XP_008322581.1; XM_008324359.3.
DR AlphaFoldDB; A0A3P8WI04; -.
DR SMR; A0A3P8WI04; -.
DR FunCoup; A0A3P8WI04; 569.
DR STRING; 244447.ENSCSEP00000026369; -.
DR Ensembl; ENSCSET00000026723.1; ENSCSEP00000026369.1; ENSCSEG00000016855.1.
DR GeneID; 103389093; -.
DR KEGG; csem:103389093; -.
DR CTD; 167227; -.
DR GeneTree; ENSGT00390000018878; -.
DR InParanoid; A0A3P8WI04; -.
DR OMA; RQDSPCV; -.
DR OrthoDB; 18996at2759; -.
DR Proteomes; UP000265120; Chromosome 14.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0140933; F:5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity; IEA:UniProtKB-EC.
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; IEA:InterPro.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:InterPro.
DR CDD; cd03672; NUDIX_Dcp2p_Nudt20; 1.
DR FunFam; 1.10.10.1050:FF:000001; M7GpppN-mRNA hydrolase isoform 2; 1.
DR FunFam; 3.90.79.10:FF:000003; M7GpppN-mRNA hydrolase isoform 2; 1.
DR Gene3D; 1.10.10.1050; Dcp2, box A domain; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 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 PANTHER; PTHR23114; M7GPPPN-MRNA HYDROLASE; 1.
DR PANTHER; PTHR23114:SF17; M7GPPPN-MRNA HYDROLASE; 1.
DR Pfam; PF05026; DCP2; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SMART; SM01125; DCP2; 1.
DR SUPFAM; SSF140586; Dcp2 domain-like; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000265120};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 95..226
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT REGION 249..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 390 AA; 44656 MW; D41D012836BB5F41 CRC64;
MESKRVDIPS DVLDDLCSRF ILHIPSEERD NAIRVCFQIE LAHWFYLDFC MQNTPGAPHC
GIRDFAKAVF HHCPFLLPHG EDVQKVLEQW KEYKMGVPTY GAIILNESLE NVLLVQGYLA
KSGWGFPKGK VNEDEAPHDC AVREVLEETG FDIKNRICKD VFIEQKINDQ LVRLYIIPGV
SKDTKFYPKT RKEIRNIEWF PIEKLPCHRN DMTPKSKLGL APNRFFMAIP FIRPLREWIN
KLKGECTDSD DDLTSNSSTP GKPSDNHRSK SQRLLGTETF VGNGWSKHTQ QKGQLVEVNQ
NSSSKVNGKK GQDLPCVKKE ANESGANGHQ KEDRRLQPRK LLESFDQDSA SCSSKGHHTV
NKRDVEQLLS SKTFLNFKFD RDAIMKCFDC
//
