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Protein

m7GpppN-mRNA hydrolase

Gene

DCP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay (PubMed:10508173, PubMed:11139489, PubMed:11741542). Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (PubMed:12554866). Decapping is the major pathway of mRNA degradation in yeast and occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body (PubMed:10508173, PubMed:11139489, PubMed:11741542). Blocks autophagy in nutrient-rich conditions by repressing the expression of ATG-related genes through degration of their transcripts (PubMed:19779198).4 Publications

Miscellaneous

Present with 8530 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

5'-(N7-methylguanosine 5'-triphospho)-[mRNA] + H2O = N7-methylguanosine 5'-diphosphate + 5'-phospho-[mRNA].1 Publication

Cofactori

Mn2+1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi149ManganeseBy similarity1
Metal bindingi153ManganeseBy similarity1

GO - Molecular functioni

  • chromatin binding Source: SGD
  • hydrolase activity Source: SGD
  • m7G(5')pppN diphosphatase activity Source: SGD
  • manganese ion binding Source: InterPro
  • mRNA binding Source: SGD

GO - Biological processi

  • deadenylation-dependent decapping of nuclear-transcribed mRNA Source: SGD
  • deadenylation-independent decapping of nuclear-transcribed mRNA Source: SGD
  • mRNA processing Source: UniProtKB-KW
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB-KW
  • positive regulation of transcription initiation from RNA polymerase II promoter Source: SGD
  • stress granule assembly Source: SGD

Keywordsi

Molecular functionHydrolase, RNA-binding
Biological processmRNA processing, Nonsense-mediated mRNA decay
LigandManganese, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33140-MONOMER
BRENDAi3.6.1.62 984

Names & Taxonomyi

Protein namesi
Recommended name:
m7GpppN-mRNA hydrolaseCurated (EC:3.6.1.621 Publication)
Alternative name(s):
Protein PSU1
mRNA-decapping enzyme subunit 21 Publication
Gene namesi
Name:DCP21 Publication
Synonyms:PSU1
Ordered Locus Names:YNL118CImported
ORF Names:N1917
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL118C
SGDiS000005062 DCP2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Increases autophagy activity through accumulation of autophagy-related proteins in nutrient-replete conditions (PubMed:19779198).

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi60N → D in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with V-68 and V-142. 1 Publication1
Mutagenesisi68I → V in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with D-60 and V-142. 1 Publication1
Mutagenesisi142D → V in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with D-60 and V-68. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000570541 – 970m7GpppN-mRNA hydrolaseAdd BLAST970

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei116PhosphoserineCombined sources1
Modified residuei439PhosphoserineCombined sources1
Modified residuei677PhosphothreonineCombined sources1
Modified residuei679PhosphoserineCombined sources1
Modified residuei682PhosphoserineCombined sources1
Modified residuei751PhosphoserineCombined sources1
Modified residuei771PhosphoserineCombined sources1
Modified residuei773PhosphoserineCombined sources1
Modified residuei778PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53550
PaxDbiP53550
PRIDEiP53550

PTM databases

iPTMnetiP53550

Interactioni

Subunit structurei

Component of the decapping complex composed of DCP1 and DCP2 (PubMed:10508173, PubMed:11741542, PubMed:14758354). Interacts with mRNA, LSM2, LSM4 and LSM8 (PubMed:10900456). Interacts with EDC3 (PubMed:18678652).6 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi35708, 629 interactors
ComplexPortaliCPX-1628 Decapping complex, DCP1-DCP2
DIPiDIP-969N
IntActiP53550, 45 interactors
MINTiP53550
STRINGi4932.YNL118C

Structurei

Secondary structure

1970
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi105 – 112Combined sources8
Beta strandi117 – 125Combined sources9
Beta strandi132 – 135Combined sources4
Beta strandi138 – 140Combined sources3
Helixi142 – 154Combined sources13
Turni159 – 161Combined sources3
Beta strandi167 – 172Combined sources6
Beta strandi175 – 185Combined sources11
Beta strandi187 – 189Combined sources3
Beta strandi194 – 206Combined sources13
Helixi207 – 213Combined sources7
Helixi214 – 216Combined sources3
Beta strandi221 – 223Combined sources3
Helixi224 – 227Combined sources4
Helixi228 – 237Combined sources10
Helixi242 – 244Combined sources3
Helixi440 – 449Combined sources10
Helixi485 – 496Combined sources12
Helixi958 – 967Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JVBNMR-A100-245[»]
4K6EX-ray2.10A102-245[»]
4KG3X-ray1.70A/B/C100-245[»]
4KG4X-ray1.80A/B100-245[»]
5LM5X-ray2.60C/D437-450[»]
5LMFX-ray2.15C/D484-500[»]
5LMGX-ray1.89C/D957-970[»]
ProteinModelPortaliP53550
SMRiP53550
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53550

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini101 – 228Nudix hydrolasePROSITE-ProRule annotationAdd BLAST128

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi134 – 155Nudix boxAdd BLAST22

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi345 – 430Pro-richAdd BLAST86
Compositional biasi436 – 439Poly-Ser4

Sequence similaritiesi

Belongs to the Nudix hydrolase family. DCP2 subfamily.Curated

Phylogenomic databases

GeneTreeiENSGT00390000018878
InParanoidiP53550
KOiK12613
OrthoDBiEOG092C10K0

Family and domain databases

Gene3Di1.10.10.1050, 1 hit
InterProiView protein in InterPro
IPR007722 DCP2_BoxA
IPR036189 DCP2_BoxA_sf
IPR015797 NUDIX_hydrolase-like_dom_sf
IPR020084 NUDIX_hydrolase_CS
IPR000086 NUDIX_hydrolase_dom
PfamiView protein in Pfam
PF05026 DCP2, 1 hit
PF00293 NUDIX, 1 hit
SMARTiView protein in SMART
SM01125 DCP2, 1 hit
SUPFAMiSSF140586 SSF140586, 1 hit
SSF55811 SSF55811, 1 hit
PROSITEiView protein in PROSITE
PS51462 NUDIX, 1 hit
PS00893 NUDIX_BOX, 1 hit

Sequencei

Sequence statusi: Complete.

P53550-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLPLRHALE NVTSVDRILE DLLVRFIINC PNEDLSSVER ELFHFEEASW
60 70 80 90 100
FYTDFIKLMN PTLPSLKIKS FAQLIIKLCP LVWKWDIRVD EALQQFSKYK
110 120 130 140 150
KSIPVRGAAI FNENLSKILL VQGTESDSWS FPRGKISKDE NDIDCCIREV
160 170 180 190 200
KEEIGFDLTD YIDDNQFIER NIQGKNYKIF LISGVSEVFN FKPQVRNEID
210 220 230 240 250
KIEWFDFKKI SKTMYKSNIK YYLINSMMRP LSMWLRHQRQ IKNEDQLKSY
260 270 280 290 300
AEEQLKLLLG ITKEEQIDPG RELLNMLHTA VQANSNNNAV SNGQVPSSQE
310 320 330 340 350
LQHLKEQSGE HNQQKDQQSS FSSQQQPSIF PSLSEPFANN KNVIPPTMPM
360 370 380 390 400
ANVFMSNPQL FATMNGQPFA PFPFMLPLTN NSNSANPIPT PVPPNFNAPP
410 420 430 440 450
NPMAFGVPNM HNLSGPAVSQ PFSLPPAPLP RDSGYSSSSP GQLLDILNSK
460 470 480 490 500
KPDSNVQSSK KPKLKILQRG TDLNSIKQNN NDETAHSNSQ ALLDLLKKPT
510 520 530 540 550
SSQKIHASKP DTSFLPNDSV SGIQDAEYED FESSSDEEVE TARDERNSLN
560 570 580 590 600
VDIGVNVMPS EKDSRRSQKE KPRNDASKTN LNASAESNSV EWGPGKSSPS
610 620 630 640 650
TQSKQNSSVG MQNKYRQEIH IGDSDAYEVF ESSSDEEDGK KLEELEQTQD
660 670 680 690 700
NSKLISQDIL KENNFQDGEV PHRDMPTESN KSINETVGLS STTNTVKKVP
710 720 730 740 750
KVKILKRGET FASLANDKKA FDSSSNVSSS KDLLQMLRNP ISSTVSSNQQ
760 770 780 790 800
SPKSQHLSGD EEIMMMLKRN SVSKPQNSEE NASTSSINDA NASELLGMLK
810 820 830 840 850
QKEKDITAPK QPYNVDSYSQ KNSAKGLLNI LKKNDSTGYP RTEGGPSSEM
860 870 880 890 900
STSMKRNDAT NNQELDKNST ELLNYLKPKP LNDGYENISN KDSSHELLNI
910 920 930 940 950
LHGNKNSSAF NNNVYATDGY SLASDNNENS SNKLLNMLQN RSSAINEPNF
960 970
DVRSNGTSGS NELLSILHRK
Length:970
Mass (Da):108,667
Last modified:October 1, 1996 - v1
Checksum:iD53CA2C5A546FA4A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti425P → L in AAA68866 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti188V → A in strain: YJM339. 1 Publication1
Natural varianti288Missing in strain: V1-09, YJM269, YJM270, YJM326, YJM339, YJM627 and YJM1129. 1 Publication1
Natural varianti301L → H in strain: YJM280, YJM 20 and YJM339. 1 Publication1
Natural varianti319S → P in strain: YJM627. 1 Publication1
Natural varianti494D → N in strain: YJM339. 1 Publication1
Natural varianti505I → T in strain: SK1, V1-09, YJM269, YJM270, YJM280, YJM320, YJM326, YJM339, YJM627 and YJM1129. 1 Publication1
Natural varianti522G → D in strain: YJM269, YJM270, YJM326 and YJM1129. 1 Publication1
Natural varianti547N → T in strain: YJM280 and YJM320. 1 Publication1
Natural varianti567S → R in strain: YJM269, YJM270, YJM326 and YJM1129. 1 Publication1
Natural varianti574N → S in strain: YJM269, YJM270, YJM280, YJM320, YJM326 and YJM1129. 1 Publication1
Natural varianti577S → N in strain: V1-09, YJM269, YJM270, YJM280, YJM320, YJM326, YJM339 and YJM1129. 1 Publication1
Natural varianti622G → S in strain: V1-09 and YJM339. 1 Publication1
Natural varianti650D → G in strain: YJM280 and YJM320. 1 Publication1
Natural varianti740P → S in strain: YJM269 and YJM270. 1 Publication1
Natural varianti807T → A in strain: YJM 69, YJM270, YJM326 and YJM1129. 1 Publication1
Natural varianti823S → P in strain: YJM269, YJM270, YJM280, YJM320, YJM326 and YJM1129. 1 Publication1
Natural varianti835D → N in strain: YJM280 and YJM320. 1 Publication1
Natural varianti844G → V in strain: V1-09. 1 Publication1
Natural varianti851S → P in strain: YJM280, YJM320 and YJM627. 1 Publication1
Natural varianti854M → I in strain: YJM269, YJM270, YJM326 and YJM1129. 1 Publication1
Natural varianti864E → Q in strain: YJM269 and YJM270. 1 Publication1
Natural varianti865L → S in strain: YJM269, YJM270, YJM326 and YJM1129. 1 Publication1
Natural varianti866D → A in strain: YJM627. 1
Natural varianti909A → T in strain: YJM280 and YJM320. 1 Publication1
Natural varianti945I → L in strain: YJM627. 1 Publication1
Natural varianti951D → E in strain: V1-09. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31377 Genomic DNA Translation: AAC99860.1
L43065 Genomic DNA Translation: AAA68866.1
EF125216 Genomic DNA Translation: ABN58539.1
EF125217 Genomic DNA Translation: ABN58548.1
EF125218 Genomic DNA Translation: ABN58557.1
EF125219 Genomic DNA Translation: ABN58566.1
EF125220 Genomic DNA Translation: ABN58578.1
EF125221 Genomic DNA Translation: ABN58584.1
EF125222 Genomic DNA Translation: ABN58593.1
EF125223 Genomic DNA Translation: ABN58602.1
EF125224 Genomic DNA Translation: ABN58611.1
EF125225 Genomic DNA Translation: ABN58620.1
EF125226 Genomic DNA Translation: ABN58629.1
EF125228 Genomic DNA Translation: ABN58647.1
Z69382 Genomic DNA Translation: CAA93389.1
Z71394 Genomic DNA Translation: CAA95998.1
BK006947 Genomic DNA Translation: DAA10430.1
PIRiS63059
RefSeqiNP_014281.1, NM_001182956.1

Genome annotation databases

EnsemblFungiiYNL118C; YNL118C; YNL118C
GeneIDi855605
KEGGisce:YNL118C

Similar proteinsi

Entry informationi

Entry nameiDCP2_YEAST
AccessioniPrimary (citable) accession number: P53550
Secondary accession number(s): B0KZS6
, B0KZU4, B0KZW2, B0KZY0, B0KZY9, B0KZZ8, B0L007, D6W164, Q6LCS6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 20, 2018
This is version 169 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

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