DCPS_MOUSE
ID DCPS_MOUSE Reviewed; 338 AA.
AC Q9DAR7; Q8C5I7;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
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 (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of mRNA decapping enzyme (DCPS) from Mus musculus at
RT 1.83 A resolution.";
RL Submitted (AUG-2004) to the PDB data bank.
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; AY040775; AAK91764.1; -; mRNA.
DR EMBL; AK005584; BAB24138.1; -; mRNA.
DR EMBL; AK078253; BAC37194.1; -; mRNA.
DR EMBL; BC016273; AAH16273.1; -; mRNA.
DR CCDS; CCDS22957.1; -.
DR RefSeq; NP_081306.1; NM_027030.2.
DR PDB; 1VLR; X-ray; 1.83 A; A/B=1-338.
DR PDBsum; 1VLR; -.
DR AlphaFoldDB; Q9DAR7; -.
DR SMR; Q9DAR7; -.
DR BioGRID; 213348; 13.
DR IntAct; Q9DAR7; 1.
DR MINT; Q9DAR7; -.
DR STRING; 10090.ENSMUSP00000034539; -.
DR ChEMBL; CHEMBL4105708; -.
DR iPTMnet; Q9DAR7; -.
DR PhosphoSitePlus; Q9DAR7; -.
DR SwissPalm; Q9DAR7; -.
DR EPD; Q9DAR7; -.
DR jPOST; Q9DAR7; -.
DR MaxQB; Q9DAR7; -.
DR PaxDb; Q9DAR7; -.
DR PeptideAtlas; Q9DAR7; -.
DR PRIDE; Q9DAR7; -.
DR ProteomicsDB; 279393; -.
DR Antibodypedia; 32998; 233 antibodies from 24 providers.
DR DNASU; 69305; -.
DR Ensembl; ENSMUST00000034539; ENSMUSP00000034539; ENSMUSG00000032040.
DR GeneID; 69305; -.
DR KEGG; mmu:69305; -.
DR UCSC; uc009osp.1; mouse.
DR CTD; 28960; -.
DR MGI; MGI:1916555; Dcps.
DR VEuPathDB; HostDB:ENSMUSG00000032040; -.
DR eggNOG; KOG3969; Eukaryota.
DR GeneTree; ENSGT00390000003924; -.
DR HOGENOM; CLU_041045_2_0_1; -.
DR InParanoid; Q9DAR7; -.
DR OMA; LIYPCTD; -.
DR OrthoDB; 930557at2759; -.
DR PhylomeDB; Q9DAR7; -.
DR TreeFam; TF105622; -.
DR BRENDA; 3.6.1.59; 3474.
DR Reactome; R-MMU-429958; mRNA decay by 3' to 5' exoribonuclease.
DR BioGRID-ORCS; 69305; 22 hits in 77 CRISPR screens.
DR ChiTaRS; Dcps; mouse.
DR EvolutionaryTrace; Q9DAR7; -.
DR PRO; PR:Q9DAR7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9DAR7; protein.
DR Bgee; ENSMUSG00000032040; Expressed in spinal cord lateral wall and 243 other tissues.
DR ExpressionAtlas; Q9DAR7; baseline and differential.
DR Genevisible; Q9DAR7; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:MGI.
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:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96C86"
FT CHAIN 2..338
FT /note="m7GpppX diphosphatase"
FT /id="PRO_0000109795"
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 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 137
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 141
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96C86"
FT CONFLICT 141
FT /note="K -> E (in Ref. 2; BAC37194)"
FT /evidence="ECO:0000305"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1VLR"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:1VLR"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:1VLR"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:1VLR"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:1VLR"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:1VLR"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:1VLR"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:1VLR"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:1VLR"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:1VLR"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:1VLR"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:1VLR"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:1VLR"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:1VLR"
FT HELIX 173..179
FT /evidence="ECO:0007829|PDB:1VLR"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:1VLR"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:1VLR"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:1VLR"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:1VLR"
FT STRAND 216..224
FT /evidence="ECO:0007829|PDB:1VLR"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1VLR"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:1VLR"
FT HELIX 237..255
FT /evidence="ECO:0007829|PDB:1VLR"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:1VLR"
FT STRAND 262..269
FT /evidence="ECO:0007829|PDB:1VLR"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:1VLR"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:1VLR"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:1VLR"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:1VLR"
FT HELIX 297..306
FT /evidence="ECO:0007829|PDB:1VLR"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:1VLR"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:1VLR"
FT HELIX 325..336
FT /evidence="ECO:0007829|PDB:1VLR"
SQ SEQUENCE 338 AA; 38988 MW; A9520CBE48293DFC CRC64;
MADTAPQLKR KREQEAEEAE TPSTEEKEAG VGNGTSAPVR LPFSGFRVQK VLRESARDKI
IFLHGKVNED SGDTHGEDAV VILEKTPFQV EHVAQLLTGS PELKLQFSND IYSTYNLFPP
RHLSDIKTTV VYPATEKHLQ KYMRQDLRLI RETGDDYRTI TLPYLESQSL SIQWVYNILD
KKAEADRIVF ENPDPSDGFV LIPDLKWNQQ QLDDLYLIAI CHRRGIRSLR DLTPEHLPLL
RNILREGQEA ILKRYQVTGD RLRVYLHYLP SYYHLHVHFT ALGFEAPGSG VERAHLLAQV
IENLECDPKH YQQRTLTFAL RTDDPLLQLL QKAQQERN
