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MT000977

UniProt Annotations

Entry Information

Gene Name	decapping enzyme, scavenger
Protein Entry	DCPS_HUMAN
UniProt ID	Q96C86
Species	Human

Comments

Comment type	Description
Catalytic Activity	A 5'-(N(7)-methyl 5'-triphosphoguanosine)- (mRNA) + H(2)O = N(7)-methylguanosine 5'-phosphate + a 5'- diphospho-(mRNA). {ECO:0000269\|PubMed:15273322, ECO:0000269\|PubMed:15383679, ECO:0000269\|PubMed:18839960, ECO:0000269\|PubMed:22985415}.
Domain	The C-terminal histidine triad (HIT) motif and the N- terminal domain are required for the decapping activity. The N- terminus is necessary but not sufficient for binding cap structures. {ECO:0000269\|PubMed:15273322}.
Enzyme Regulation	The hydrolytic product 7-methylguanosine diphosphate (m7GDP) efficiently inhibits the decapping scavenger activity and acts as a competitive inhibitor in vitro. Inhibited by 2,4-diaminoquinazoline. {ECO:0000269\|PubMed:18839960, ECO:0000269\|PubMed:22985415}.
Function	Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Cleaves cap analog structures like tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with very poor efficiency. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) to m7GMP (PubMed:22985415). May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCPS to m7GMP (PubMed:14523240). Binds to m7GpppG and strongly to m7GDP. Plays a role in first intron splicing of pre- mRNAs. Inhibits activation-induced cell death. {ECO:0000269\|PubMed:11747811, ECO:0000269\|PubMed:12198172, ECO:0000269\|PubMed:12871939, ECO:0000269\|PubMed:14523240, ECO:0000269\|PubMed:15273322, ECO:0000269\|PubMed:15383679, ECO:0000269\|PubMed:15769464, ECO:0000269\|PubMed:16140270, ECO:0000269\|PubMed:18426921, ECO:0000269\|PubMed:22985415}.
Induction	Up-regulated by menadione. Up-regulated by the transcription factor LTF isoform delta-lactoferrin (at protein level). {ECO:0000269\|PubMed:16140270, ECO:0000269\|PubMed:18725266}.
Similarity	Belongs to the HIT family. {ECO:0000305}.
Subcellular Location	Cytoplasm. Nucleus. Note=Predominantly localized in the nucleus. Nucleocytoplasmic shuttling protein that can transiently enter the cytoplasm in mammalian cells in a XPO1/CRM1-dependent manner.
Subunit	Homodimer. Associates with components of the exosome multienzyme ribonuclease complex, such as EXOSC3 and EXOSC4. Interacts with NDOR1. {ECO:0000269\|PubMed:11747811, ECO:0000269\|PubMed:12198172, ECO:0000269\|PubMed:15068804, ECO:0000269\|PubMed:15769464, ECO:0000269\|PubMed:16140270, ECO:0000269\|PubMed:18839960}.
Tissue Specificity	Detected in liver, brain, kidney, testis and prostate. {ECO:0000269\|PubMed:12871939}.