DCPS_RAT
ID DCPS_RAT Reviewed; 336 AA.
AC Q8K4F7;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=m7GpppX diphosphatase;
DE EC=3.6.1.59 {ECO:0000250|UniProtKB:Q96C86};
DE AltName: Full=DCS-1;
DE AltName: Full=Decapping scavenger enzyme;
DE AltName: Full=Hint-related 7meGMP-directed hydrolase;
DE AltName: Full=Histidine triad nucleotide-binding protein 5;
DE AltName: Full=Histidine triad protein member 5;
DE Short=HINT-5;
DE AltName: Full=Scavenger mRNA-decapping enzyme DcpS;
GN Name=Dcps; Synonyms=Dcs1, Hint5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Huang C.-H., Peng J., Chen H., Chen Y.;
RT "Cloning and characterization of a novel member of the histidine triad
RT protein family (HINT-5) in different vertebrate species.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Decapping scavenger enzyme that catalyzes the cleavage of a
CC residual cap structure following the degradation of mRNAs by the 3'->5'
CC exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures
CC like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10
CC nucleotide substrates (small capped oligoribonucleotides) and
CC specifically releases 5'-phosphorylated RNA fragments and 7-
CC methylguanosine monophosphate (m7GMP). Cleaves cap analog structures
CC like tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with
CC very poor efficiency. Does not hydrolyze unmethylated cap analog
CC (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA
CC molecules longer than 25 nucleotides. Does not hydrolyze 7-
CC methylguanosine diphosphate (m7GDP) to m7GMP. May also play a role in
CC the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by
CC the 5'->3' mRNA mediated decapping activity, may be also converted by
CC DCPS to m7GMP. Binds to m7GpppG and strongly to m7GDP. Plays a role in
CC first intron splicing of pre-mRNAs. Inhibits activation-induced cell
CC death. {ECO:0000250}.
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:0000250|UniProtKB:Q96C86};
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. Inhibited by
CC 2,4-diaminoquinazoline. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Associates with components of the exosome
CC multienzyme ribonuclease complex, such as EXOSC3 and EXOSC4. Interacts
CC with NDOR1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Predominantly localized in the nucleus. Nucleocytoplasmic
CC shuttling protein that can transiently enter the cytoplasm in mammalian
CC cells in a XPO1/CRM1-dependent manner. {ECO:0000250}.
CC -!- DOMAIN: The C-terminal histidine triad (HIT) motif and the N-terminal
CC domain are required for the decapping activity. The N-terminus is
CC necessary but not sufficient for binding cap structures. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HIT family. {ECO:0000305}.
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DR EMBL; AF411249; AAN03664.1; -; mRNA.
DR RefSeq; NP_695214.1; NM_153302.1.
DR AlphaFoldDB; Q8K4F7; -.
DR SMR; Q8K4F7; -.
DR BioGRID; 251757; 1.
DR STRING; 10116.ENSRNOP00000013763; -.
DR iPTMnet; Q8K4F7; -.
DR PhosphoSitePlus; Q8K4F7; -.
DR jPOST; Q8K4F7; -.
DR PaxDb; Q8K4F7; -.
DR PRIDE; Q8K4F7; -.
DR GeneID; 266605; -.
DR KEGG; rno:266605; -.
DR UCSC; RGD:628887; rat.
DR CTD; 28960; -.
DR RGD; 628887; Dcps.
DR eggNOG; KOG3969; Eukaryota.
DR InParanoid; Q8K4F7; -.
DR OrthoDB; 930557at2759; -.
DR PhylomeDB; Q8K4F7; -.
DR Reactome; R-RNO-429958; mRNA decay by 3' to 5' exoribonuclease.
DR PRO; PR:Q8K4F7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; ISS:UniProtKB.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; ISS:UniProtKB.
DR GO; GO:0036245; P:cellular response to menadione; ISS:UniProtKB.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR GO; GO:0110156; P:methylguanosine-cap decapping; ISO:RGD.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0043069; P:negative regulation of programmed cell death; ISS:UniProtKB.
DR Gene3D; 3.30.200.40; -; 1.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR008594; DcpS/DCS2.
DR InterPro; IPR019808; Histidine_triad_CS.
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.
DR PROSITE; PS00892; HIT_1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Hydrolase; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96C86"
FT CHAIN 2..336
FT /note="m7GpppX diphosphatase"
FT /id="PRO_0000109797"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 9..12
FT /note="nuclear localization signal (NLS)"
FT /evidence="ECO:0000250"
FT MOTIF 141..153
FT /note="nuclear export sequence (NES)"
FT /evidence="ECO:0000250"
FT MOTIF 274..278
FT /note="Histidine triad motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 276
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 267..278
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96C86"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96C86"
FT MOD_RES 137
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96C86"
FT MOD_RES 141
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96C86"
SQ SEQUENCE 336 AA; 38714 MW; AEFA4D106FC5B6AE CRC64;
MADTAPQLKR KREQEAEEAE TPSTEEKEAG VGNGTSAPVR LPFSGFRVQK VLRESARDKI
IFLHGKVNED SGDTHGEDAV VILEKTPFQV EHVAQLLTGN PELKLQFSND IYSTYNLFPP
RHLSDIKTTV VYPASEKHLQ KYMRQDLRLI RETGDDYRSL TLPYLESQSL SIQWVYNILD
KKAEADRIVF ENPDPSDGFV LIPDLKWNQQ QLDDLYLIAI CHRRGIRSLR DLTPEHLPLL
RNILREGQEA ILKRYQVTGD RLRVYLHYLP SYYHLHVHFT ALGFEAPGSG VERAHLLAEV
IENLECDPKH YQRRTLTFAL RTDDPLLQLL QKAQQP
