ID A0A2Y9DLS7_TRIMA Unreviewed; 422 AA.
AC A0A2Y9DLS7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, 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};
GN Name=DCP2 {ECO:0000313|RefSeq:XP_004377045.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004377045.1};
RN [1] {ECO:0000313|RefSeq:XP_004377045.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_004377045.1; XM_004376988.2.
DR AlphaFoldDB; A0A2Y9DLS7; -.
DR FunCoup; A0A2Y9DLS7; 1854.
DR STRING; 127582.A0A2Y9DLS7; -.
DR GeneID; 101361864; -.
DR KEGG; tmu:101361864; -.
DR CTD; 167227; -.
DR InParanoid; A0A2Y9DLS7; -.
DR OrthoDB; 18996at2759; -.
DR Proteomes; UP000248480; Unplaced.
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:UniProtKB-KW.
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 ECO:0000313|RefSeq:XP_004377045.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nonsense-mediated mRNA decay {ECO:0000256|ARBA:ARBA00023161};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 95..226
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT REGION 319..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 48658 MW; 1A7FF3D91C55BF45 CRC64;
METKRVEIPG SVLDDLCSRF ILHIPSEERD NAIRVCFQIE LAHWFYLDFY MQNTPGLPQC
GIRDFAKAVF SHCPFLLPQG EDVEKVLDEW KEYKMGVPTY GAIILDETLE NVLLVQGYLA
KSGWGFPKGK VNKEEAPHDC AAREVFEETG FDIKDYICKD DYIELRINDQ LARLYIIPGV
PKDTKFNPKT RREIRNIEWF SIEKLPCHRN DMTPKSKLGL APNKFFMAIP FIRPLRDWLS
RRFGDSSDSD NGFSSAGSTP AKPTVEKLSR TKFRHGQQLF PEGSPGDQWV KHRQPLQQKP
YNNHSEMSDL LKAKNQNMRG NGRKQYQDSP NQKKRTNGVH SQSAKQQNPL MKCEKKFHPR
KLQDNFETDA VYDSPCSGED QLLEHAEGQS VTCNGHCKFP FSSRTFLSFK FDHNAIMKIL
DL
//
