Q9DAR7 (DCPS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
m7GpppX diphosphatase
EC=3.6.1.59

Alternative name(s):
DCS-1
Decapping scavenger enzyme
Hint-related 7meGMP-directed hydrolase
Histidine triad nucleotide-binding protein 5
Histidine triad protein member 5
Short name=HINT-5
Scavenger mRNA-decapping enzyme DcpS

Gene names

Name:	Dcps
Synonyms:	Dcs1, Hint5

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. 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. Binds to m7GpppG and strongly to m7GDP. Plays a role in first intron splicing of pre-mRNAs. Inhibits activation-induced cell death By similarity.
Catalytic activity	M7G5'ppp5'N(3'ppp5'N)(n) + H2O = 7-methylguanosine 5'-phosphate + pp5'N(3'ppp5'N)(n). 7-methylguanosine 5'-diphosphate + H2O = 7-methylguanosine 5'-phosphate + phosphate.
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 By similarity.
Subunit structure	Homodimer. Associates with components of the exosome multienzyme ribonuclease complex, such as EXOSC3 and EXOSC4. Interacts with NDOR1 By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Note: Predominantly localized in the nucleus. Nucleocytoplasmic shuttling protein that can transiently enter the cytoplasm in mammalian cells in a XPO1/CRM1-dependent manner By similarity.
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 By similarity.
Sequence similarities	Belongs to the HIT family.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to menadione Inferred from sequence or structural similarity. Source: UniProtKB deadenylation-dependent decapping of nuclear-transcribed mRNA Inferred from electronic annotation. Source: InterPro mRNA cis splicing, via spliceosome Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of programmed cell death Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB mitochondrion Inferred from electronic annotation. Source: Compara nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	RNA 7-methylguanosine cap binding Inferred from sequence or structural similarity. Source: UniProtKB m7G(5')pppN diphosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 338

337

m7GpppX diphosphatase

PRO_0000109795

Regions

Region

267 – 278

12

Substrate binding By similarity

Motif

9 – 12

4

nuclear localization signal (NLS) By similarity

Motif

141 – 153

13

nuclear export sequence (NES) By similarity

Motif

274 – 278

5

Histidine triad motif By similarity

Sites

Active site

276

1

Nucleophile By similarity

Binding site

174

1

Substrate By similarity

Binding site

184

1

Substrate By similarity

Binding site

204

1

Substrate By similarity

Binding site

206

1

Substrate By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Modified residue

21

1

Phosphothreonine Ref.4

Modified residue

137

1

N6-acetyllysine By similarity

Modified residue

141

1

N6-acetyllysine By similarity

Experimental info

Sequence conflict

141

1

K → E in BAC37194. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

338

Helix Strand Turn

Details...

Beta strand

42 – 44

3

Beta strand

47 – 55

9

Turn

56 – 59

4

Beta strand

60 – 67

8

Beta strand

77 – 85

9

Helix

90 – 97

8

Beta strand

102 – 108

7

Beta strand

110 – 118

9

Helix

121 – 124

4

Beta strand

126 – 133

8

Helix

136 – 142

7

Beta strand

147 – 152

6

Helix

154 – 159

6

Helix

161 – 168

8

Helix

173 – 179

7

Beta strand

189 – 192

4

Turn

195 – 197

3

Beta strand

199 – 203

5

Beta strand

216 – 224

9

Helix

229 – 231

3

Helix

234 – 236

3

Helix

237 – 255

19

Helix

259 – 261

3

Beta strand

262 – 269

8

Beta strand

271 – 274

4

Beta strand

276 – 281

6

Turn

291 – 293

3

Beta strand

294 – 296

3

Helix

297 – 306

10

Helix

310 – 313

4

Beta strand

316 – 321

6

Helix

325 – 336

12

Sequences

	Sequence		Length	Mass (Da)
	Q9DAR7 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: A9520CBE48293DFC	FASTA	338	38,988
	10 20 30 40 50 60 MADTAPQLKR KREQEAEEAE TPSTEEKEAG VGNGTSAPVR LPFSGFRVQK VLRESARDKI 70 80 90 100 110 120 IFLHGKVNED SGDTHGEDAV VILEKTPFQV EHVAQLLTGS PELKLQFSND IYSTYNLFPP 130 140 150 160 170 180 RHLSDIKTTV VYPATEKHLQ KYMRQDLRLI RETGDDYRTI TLPYLESQSL SIQWVYNILD 190 200 210 220 230 240 KKAEADRIVF ENPDPSDGFV LIPDLKWNQQ QLDDLYLIAI CHRRGIRSLR DLTPEHLPLL 250 260 270 280 290 300 RNILREGQEA ILKRYQVTGD RLRVYLHYLP SYYHLHVHFT ALGFEAPGSG VERAHLLAQV 310 320 330 IENLECDPKH YQQRTLTFAL RTDDPLLQLL QKAQQERN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a novel member of the histidine triad protein family (HINT-5) in different vertebrate species." Huang C.-H., Peng J., Chen H., Chen Y. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Brain.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Olfactory bulb and Testis.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Eye.
[4]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Crystal structure of mRNA decapping enzyme (DCPS) from Mus musculus at 1.83 A resolution." Joint center for structural genomics (JCSG) Submitted (AUG-2004) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY040775 mRNA. Translation: AAK91764.1.
AK005584 mRNA. Translation: BAB24138.1.
AK078253 mRNA. Translation: BAC37194.1.
BC016273 mRNA. Translation: AAH16273.1.

IPI

IPI00459280.

RefSeq

NP_081306.1. NM_027030.2.

UniGene

Mm.229110.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VLR	X-ray	1.83	A/B	1-338	[»]

ProteinModelPortal

Q9DAR7.

SMR

Q9DAR7. Positions 39-337.

ModBase

Search...

PTM databases

PhosphoSite

Q9DAR7.

Proteomic databases

PaxDb

Q9DAR7.

PRIDE

Q9DAR7.

Protocols and materials databases

DNASU

69305.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000034539; ENSMUSP00000034539; ENSMUSG00000032040.

GeneID

69305.

KEGG

mmu:69305.

UCSC

uc009osp.1. mouse.

Organism-specific databases

CTD

28960.

MGI

MGI:1916555. Dcps.

Phylogenomic databases

eggNOG

COG5075.

GeneTree

ENSGT00390000003924.

HOGENOM

HOG000182411.

HOVERGEN

HBG051322.

InParanoid

Q9DAR7.

KO

K12584.

OMA

GADSSHK.

OrthoDB

EOG48D0VP.

Gene expression databases

ArrayExpress

Q9DAR7.

Bgee

Q9DAR7.

CleanEx

MM_DCPS.

Genevestigator

Q9DAR7.

GermOnline

ENSMUSG00000032040. Mus musculus.

Family and domain databases

Gene3D

3.30.428.10. 1 hit.

InterPro

IPR008594. DcpS/DCS2.
IPR019808. Histidine_triad_CS.
IPR011146. HIT-like.
IPR011145. Scavenger_mRNA_decap_enz_N.
[Graphical view]

PANTHER

PTHR12978. PTHR12978. 1 hit.

Pfam

PF05652. DcpS. 1 hit.
[Graphical view]

PIRSF

PIRSF028973. Scavenger_mRNA_decap_enz. 1 hit.

SUPFAM

SSF54197. His_triad-like_motif. 1 hit.
SSF102860. Scavenger_mRNA_decap_enz_N. 1 hit.

PROSITE

PS00892. HIT_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9DAR7.

NextBio

329076.

SOURCE

Search...

Entry information

Entry name

DCPS_MOUSE

Accession

Primary (citable) accession number: Q9DAR7
Secondary accession number(s): Q8C5I7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	June 1, 2001
Last modified:	April 3, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program