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Protein

mRNA-decapping enzyme subunit 1

Gene

DCP1

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

Functioni

Component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body. DCP1 is activated by the DEAD-box helicase DHH1 and destabilizes the eIF-4F cap-binding complex from the mRNA.16 Publications

Miscellaneous

Present with 2880 molecules/cell in log phase SD medium.1 Publication

GO - Molecular functioni

  • enzyme activator activity Source: SGD
  • mRNA binding Source: SGD

GO - Biological processi

Keywordsi

Molecular functionRNA-binding
Biological processmRNA processing, Nonsense-mediated mRNA decay

Enzyme and pathway databases

BioCyciYEAST:G3O-33539-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA-decapping enzyme subunit 1
Gene namesi
Name:DCP1
Ordered Locus Names:YOL149W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL149W
SGDiS000005509 DCP1

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi16 – 20EFYRK → AFYAA in DCP1-17; partial loss of mRNA-decapping activity. 1 Publication5
Mutagenesisi29 – 31RYD → AYA in DCP1-2; strong loss of mRNA decapping activity at 36 degrees Celsius. 2 Publications3
Mutagenesisi32 – 34PKI → AKA: Partial loss of mRNA-decapping activity. 1 Publication3
Mutagenesisi37 – 38LL → AA: Strong loss of mRNA-decapping activity; when associated with A-217 and A-221. 1 Publication2
Mutagenesisi47Y → A in DCP1-32; partial loss of mRNA decapping activity. 1 Publication1
Mutagenesisi47Y → F in DCP1-35; partial loss of mRNA decapping activity. 1 Publication1
Mutagenesisi48 – 50KWD → AWA in DCP1-4; partial loss of mRNA decapping activity. In DCP1-43; strong loss of mRNA-decapping activity; when associated with A-187 and A-188. In DCP1-44; strong loss of mRNA-decapping activity; when associated with A-216 and A-219. 1 Publication3
Mutagenesisi56W → A in DCP1-31; partial loss of mRNA decapping activity. 3 Publications1
Mutagenesisi70R → A in DCP1-33; strong loss of mRNA decapping activity. 2 Publications1
Mutagenesisi156G → D in DCP1-1; strong loss of mRNA decapping activity. 1 Publication1
Mutagenesisi187 – 188KD → AA in DCP1-19; partial loss of mRNA decapping activity. In DCP1-43; strong loss of mRNA-decapping activity; when associated with A-48 and A-50. 1 Publication2
Mutagenesisi204W → A in DCP1-33; partial loss of mRNA decapping activity. 1 Publication1
Mutagenesisi216 – 219ELIK → ALIA in DCP1-25; partial loss of mRNA-decapping activity. In DCP1-44; strong loss of mRNA-decapping activity; when associated with A-48 and A-50. 1 Publication4
Mutagenesisi217L → A: Strong loss of mRNA-decapping activity; when associated with A-37; A-38 and A-221. 1 Publication1
Mutagenesisi221L → A: Strong loss of mRNA-decapping activity; when associated with A-37; A-38 and A-217. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002329981 – 231mRNA-decapping enzyme subunit 1Add BLAST231

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12517
PaxDbiQ12517
PRIDEiQ12517

Interactioni

Subunit structurei

Component of the decapping complex composed of DCP1 and DCP2. Interacts with mRNAs, DHH1, LSM1, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, and the cap-binding proteins PAB1 and TIF4632/eIF-4G.8 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi34268, 392 interactors
ComplexPortaliCPX-1628 Decapping complex, DCP1-DCP2
DIPiDIP-1288N
IntActiQ12517, 25 interactors
MINTiQ12517
STRINGi4932.YOL149W

Structurei

Secondary structure

1231
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi24 – 30Combined sources7
Beta strandi34 – 50Combined sources17
Turni51 – 54Combined sources4
Beta strandi55 – 70Combined sources16
Beta strandi139 – 150Combined sources12
Beta strandi152 – 157Combined sources6
Helixi160 – 169Combined sources10
Helixi171 – 176Combined sources6
Beta strandi183 – 187Combined sources5
Beta strandi190 – 194Combined sources5
Beta strandi200 – 207Combined sources8
Helixi208 – 223Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q67X-ray2.30A/B1-231[»]
ProteinModelPortaliQ12517
SMRiQ12517
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12517

Family & Domainsi

Sequence similaritiesi

Belongs to the DCP1 family.Curated

Phylogenomic databases

HOGENOMiHOG000246588
InParanoidiQ12517
KOiK12612
OMAiKQLLFHT
OrthoDBiEOG092C4W9A

Family and domain databases

Gene3Di2.30.29.30, 2 hits
InterProiView protein in InterPro
IPR010334 Dcp1
IPR011993 PH-like_dom_sf
PANTHERiPTHR16290 PTHR16290, 1 hit
PfamiView protein in Pfam
PF06058 DCP1, 2 hits

Sequencei

Sequence statusi: Complete.

Q12517-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGAATAAEN SATQLEFYRK ALNFNVIGRY DPKIKQLLFH TPHASLYKWD
60 70 80 90 100
FKKDEWNKLE YQGVLAIYLR DVSQNTNLLP VSPQEVDIFD SQNGSNNIQV
110 120 130 140 150
NNGSDNSNRN SSGNGNSYKS NDSLTYNCGK TLSGKDIYNY GLIILNRINP
160 170 180 190 200
DNFSMGIVPN SVVNKRKVFN AEEDTLNPLE CMGVEVKDEL VIIKNLKHEV
210 220 230
YGIWIHTVSD RQNIYELIKY LLENEPKDSF A
Length:231
Mass (Da):26,266
Last modified:November 1, 1996 - v1
Checksum:i8456B1C96C121C4D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48239 Genomic DNA Translation: CAA88278.1
Z74891 Genomic DNA Translation: CAA99170.1
AY558431 Genomic DNA Translation: AAS56757.1
BK006948 Genomic DNA Translation: DAA10636.1
PIRiS60387
RefSeqiNP_014492.1, NM_001183403.1

Genome annotation databases

EnsemblFungiiYOL149W; YOL149W; YOL149W
GeneIDi854016
KEGGisce:YOL149W

Similar proteinsi

Entry informationi

Entry nameiDCP1_YEAST
AccessioniPrimary (citable) accession number: Q12517
Secondary accession number(s): D6W1S0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: November 1, 1996
Last modified: June 20, 2018
This is version 139 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, Direct protein sequencing, 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

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