DCP2_PONAB
ID DCP2_PONAB Reviewed; 385 AA.
AC Q5REQ8;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=m7GpppN-mRNA hydrolase;
DE EC=3.6.1.62 {ECO:0000250|UniProtKB:Q8IU60};
DE AltName: Full=mRNA-decapping enzyme 2;
GN Name=DCP2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q8IU60}.
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:Q8IU60};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67485;
CC Evidence={ECO:0000250|UniProtKB:Q8IU60};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Mn(2+) ion is required for highest activity. Can also utilize
CC magnesium ions. {ECO:0000250};
CC -!- SUBUNIT: Found in a mRNA decay complex with LSM1, LSM3, LSM4, EXOSC2,
CC EXOSC4, EXOSC10, PARN, XRN1, CNOT6, UPF1, UPF2 and UPF3B. Forms a
CC complex with DCP1A, EDC3, DDX6 and EDC4/HEDLS, within this complex
CC directly interacts with EDC4/HEDLS. Interacts with DPC1B, UPF1, UPF2
CC and UPF3B. Associates with polysomes. Interacts (via N-terminus and C-
CC terminus) with TRIM21 (via N-terminus and C-terminus). Interacts with
CC LIMD1, WTIP and AJUBA. Interacts with DDX17 in an RNA-dependent manner.
CC Interacts with ZC3HAV1. Interacts with APOBEC3G in an RNA-dependent
CC manner. Interacts with ZFP36L1 (via N-terminus). Interacts with NBDY.
CC {ECO:0000250|UniProtKB:Q8IU60}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250}. Nucleus
CC {ECO:0000250}. Note=Predominantly cytoplasmic, in processing bodies
CC (PB). A minor amount is nuclear. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DCP2 subfamily.
CC {ECO:0000305}.
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DR EMBL; CR857460; CAH89749.1; -; mRNA.
DR RefSeq; NP_001124545.1; NM_001131073.1.
DR AlphaFoldDB; Q5REQ8; -.
DR SMR; Q5REQ8; -.
DR GeneID; 100127054; -.
DR KEGG; pon:100127054; -.
DR CTD; 167227; -.
DR eggNOG; KOG2937; Eukaryota.
DR InParanoid; Q5REQ8; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; ISS:UniProtKB.
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:0071044; P:histone mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Manganese; Metal-binding;
KW Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT CHAIN 1..385
FT /note="m7GpppN-mRNA hydrolase"
FT /id="PRO_0000057053"
FT DOMAIN 95..226
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 247..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 129..150
FT /note="Nudix box"
FT COMPBIAS 247..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 144
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IU60"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IU60"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IU60"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IU60"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IU60"
SQ SEQUENCE 385 AA; 44427 MW; F4BE8EC7570368DF CRC64;
METKRVEIPG SVLDDLCSRF ILHIPSEERD NAIRVCFQIE LAHWFYLDFY MQNTPGLSQC
GIRDFAKAVF SHCPFLLPEG EDVEKVLDEW KEYKMGVPTY GAIILDETLE NVLLVQGYLA
KSGWGFPKGK VNKEEAPHDC AAREVFEETG FDIKDYICKD DYIELRINDQ LARLYIIPGI
PKDTKFNPKT RREIRNIEWF SIEKLPCHRN DMTPKSKLGL APNKFFMAIP FIRPLRDWLS
RRFGDSSDSD NGFSSTGSTP AKPTVEKLSR TKFRHSQQLF PDGSPGDQWV KHRQPLQQKP
YNNHSEMSDL LKGKKCEKKL HPRKLQDNFE TDAVYDLPSS NEDQLLEHAE GQPVACNGHC
KFPFSSRAFL SFKFDHNAIM KILDL
