DCPS_BOVIN
ID DCPS_BOVIN Reviewed; 337 AA.
AC Q8MJJ7;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang C.-H., Chen H., Peng J., Chen Y.;
RT "A novel member of the histidine triad protein family with differential
RT polyadenylation (Bovine HINT-5).";
RL Submitted (JUL-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 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; AF398237; AAM90585.1; -; mRNA.
DR AlphaFoldDB; Q8MJJ7; -.
DR SMR; Q8MJJ7; -.
DR STRING; 9913.ENSBTAP00000003732; -.
DR PaxDb; Q8MJJ7; -.
DR PeptideAtlas; Q8MJJ7; -.
DR PRIDE; Q8MJJ7; -.
DR eggNOG; KOG3969; Eukaryota.
DR InParanoid; Q8MJJ7; -.
DR Proteomes; UP000009136; 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: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: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..337
FT /note="m7GpppX diphosphatase"
FT /id="PRO_0000109793"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 10..13
FT /note="nuclear localization signal (NLS)"
FT /evidence="ECO:0000250"
FT MOTIF 142..154
FT /note="nuclear export sequence (NES)"
FT /evidence="ECO:0000250"
FT MOTIF 275..279
FT /note="Histidine triad motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 277
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 268..279
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96C86"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96C86"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DAR7"
FT MOD_RES 138
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96C86"
FT MOD_RES 142
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96C86"
SQ SEQUENCE 337 AA; 38402 MW; 9DB7C72959B0B860 CRC64;
MAELAHQQSK RKRELDAEEA EASSTEGEEA GVGNGTSAPV RLPFSGFRVK KVLRESARDK
IIFLHGKVNE ASGDGDGEDA VVILEKTPFQ VDQVAQLLKG SPELQLQFSN DVYSTYHLFP
PRQLSDVKTT VVYPATEKHL QKYLRQDLHL VRETGSDYRN VTLPHLESQS LSIQWVYNIL
DKKAEADRIV FENPDPSDGF VLIPDLKWNQ QQLDDLYLIA ICHRRGIKSL RDLTAEHLPL
LRNILREGQE AILRRYQVAA DRLRVYLHYL PSYYHLHVHF TALGFEAPGA GVERAHLLAE
VIDNLEQDPE HYQRRTLTFA LRADDPLLAL LQEAQRS
