Q12517 (DCP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
mRNA-decapping enzyme subunit 1

Gene names

Name:	DCP1
Ordered Locus Names:	YOL149W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	231 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17 Ref.18 Ref.20 Ref.21 Ref.24 Ref.26
Subunit structure	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. Ref.9 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.27
Subcellular location	Cytoplasm › P-body. Note: Is concentrated in several cytoplasmic foci called P bodies (or cytoplasmic processing bodies) which represent sites of mRNA decapping and 5' to 3' exonucleotidic decay. Ref.15 Ref.22 Ref.25
Post-translational modification	Phosphorylated. Ref.7
Miscellaneous	Present with 2880 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the DCP1 family.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay mRNA processing
Cellular component	Cytoplasm
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	deadenylation-dependent decapping of nuclear-transcribed mRNA Inferred from direct assay Ref.17. Source: SGD mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasmic mRNA processing body Inferred from mutant phenotype Ref.25. Source: SGD
Molecular_function	enzyme activator activity Inferred from direct assay PubMed 16341225. Source: SGD mRNA binding Inferred from physical interaction Ref.17. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DCP2	P53550	5	EBI-38519,EBI-270
EDC3	P39998	5	EBI-38519,EBI-22300

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 231

231

mRNA-decapping enzyme subunit 1

PRO_0000232998

Experimental info

Mutagenesis

16 – 20

5

EFYRK → AFYAA in DCP1-17; partial loss of mRNA-decapping activity. Ref.10

Mutagenesis

29 – 31

3

RYD → AYA in DCP1-2; strong loss of mRNA decapping activity at 36 degrees Celsius. Ref.10 Ref.27

Mutagenesis

32 – 34

3

PKI → AKA: Partial loss of mRNA-decapping activity. Ref.27

Mutagenesis

37 – 38

2

LL → AA: Strong loss of mRNA-decapping activity; when associated with A-217 and A-221.

Mutagenesis

47

1

Y → A in DCP1-32; partial loss of mRNA decapping activity. Ref.10

Mutagenesis

47

1

Y → F in DCP1-35; partial loss of mRNA decapping activity. Ref.10

Mutagenesis

48 – 50

3

KWD → 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. Ref.10

Mutagenesis

56

1

W → A in DCP1-31; partial loss of mRNA decapping activity. Ref.5 Ref.10 Ref.27

Mutagenesis

70

1

R → A in DCP1-33; strong loss of mRNA decapping activity. Ref.10 Ref.27

Mutagenesis

156

1

G → D in DCP1-1; strong loss of mRNA decapping activity. Ref.10

Mutagenesis

187 – 188

2

KD → 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.

Mutagenesis

204

1

W → A in DCP1-33; partial loss of mRNA decapping activity. Ref.10

Mutagenesis

216 – 219

4

ELIK → 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. Ref.10

Mutagenesis

217

1

L → A: Strong loss of mRNA-decapping activity; when associated with A-37; A-38 and A-221. Ref.27

Mutagenesis

221

1

L → A: Strong loss of mRNA-decapping activity; when associated with A-37; A-38 and A-217. Ref.27

Secondary structure

1

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231

Helix Strand Turn

Details...

Helix

24 – 30

7

Beta strand

34 – 50

17

Turn

51 – 54

4

Beta strand

55 – 70

16

Beta strand

139 – 150

12

Beta strand

152 – 157

6

Helix

160 – 169

10

Helix

171 – 176

6

Beta strand

183 – 187

5

Beta strand

190 – 194

5

Beta strand

200 – 207

8

Helix

208 – 223

16

Sequences

	Sequence		Length	Mass (Da)
	Q12517 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 8456B1C96C121C4D	FASTA	231	26,266
	10 20 30 40 50 60 MTGAATAAEN SATQLEFYRK ALNFNVIGRY DPKIKQLLFH TPHASLYKWD FKKDEWNKLE 70 80 90 100 110 120 YQGVLAIYLR DVSQNTNLLP VSPQEVDIFD SQNGSNNIQV NNGSDNSNRN SSGNGNSYKS 130 140 150 160 170 180 NDSLTYNCGK TLSGKDIYNY GLIILNRINP DNFSMGIVPN SVVNKRKVFN AEEDTLNPLE 190 200 210 220 230 CMGVEVKDEL VIIKNLKHEV YGIWIHTVSD RQNIYELIKY LLENEPKDSF A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequence analysis of a 13 kbp fragment of the left arm of yeast chromosome XV containing seven new open reading frames." Casamayor A., Aldea M., Casas C., Herrero E., Gamo F.-J., Lafuente M.J., Gancedo C., Arino J. Yeast 11:1281-1288(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"An essential component of the decapping enzyme required for normal rates of mRNA turnover." Beelman C.A., Stevens A., Caponigro G., LaGrandeur T.E., Hatfield L., Fortner D.M., Parker R. Nature 382:642-646(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-14, FUNCTION, MUTAGENESIS OF TRP-56.
[6]	"Mutations in trans-acting factors affecting mRNA decapping in Saccharomyces cerevisiae." Hatfield L., Beelman C.A., Stevens A., Parker R. Mol. Cell. Biol. 16:5830-5838(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Isolation and characterization of Dcp1p, the yeast mRNA decapping enzyme." LaGrandeur T.E., Parker R. EMBO J. 17:1487-1496(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION.
[8]	"The 3' to 5' degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3' to 5' exonucleases of the exosome complex." Anderson J.S.J., Parker R.P. EMBO J. 17:1497-1506(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif." Dunckley T., Parker R. EMBO J. 18:5411-5422(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH DCP2.
[10]	"Analysis of mutations in the yeast mRNA decapping enzyme." Tharun S., Parker R. Genetics 151:1273-1285(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF 16-GLU--LYS-20; 29-ARG--ASP-31; TYR-47; 48-LYS--ASP-50; TRP-56; ARG-70; GLY-156; 187-LYS-ASP-188; TRP-204 AND 216-GLU--LYS-219.
[11]	"Monitoring mRNA decapping activity." Zhang S., Williams C.J., Wormington M., Stevens A., Peltz S.W. Methods 17:46-51(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Recognition of yeast mRNAs as 'nonsense containing' leads to both inhibition of mRNA translation and mRNA degradation: implications for the control of mRNA decapping." Muhlrad D., Parker R. Mol. Biol. Cell 10:3971-3978(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Mutations in translation initiation factors lead to increased rates of deadenylation and decapping of mRNAs in Saccharomyces cerevisiae." Schwartz D.C., Parker R. Mol. Cell. Biol. 19:5247-5256(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"The eukaryotic mRNA decapping protein Dcp1 interacts physically and functionally with the eIF4F translation initiation complex." Vilela C., Velasco C., Ptushkina M., McCarthy J.E.G. EMBO J. 19:4372-4382(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PAB1 AND TIF4632.
[15]	"Yeast Sm-like proteins function in mRNA decapping and decay." Tharun S., He W., Mayes A.E., Lennertz P., Beggs J.D., Parker R. Nature 404:515-518(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LSM1; LSM2; LSM3; LSM4; LSM5; LSM6 AND LSM7, SUBCELLULAR LOCATION.
[16]	"Genome-wide protein interaction screens reveal functional networks involving Sm-like proteins." Fromont-Racine M., Mayes A.E., Brunet-Simon A., Rain J.-C., Colley A., Dix I., Decourty L., Joly N., Ricard F., Beggs J.D., Legrain P. Yeast 17:95-110(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LSM4.
[17]	"Two related proteins, Edc1p and Edc2p, stimulate mRNA decapping in Saccharomyces cerevisiae." Dunckley T., Tucker M., Parker R. Genetics 157:27-37(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH EDC1.
[18]	"Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs." Tharun S., Parker R. Mol. Cell 8:1075-1083(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MRNA, FUNCTION OF THE DCP1-DCP2 COMPLEX.
[19]	"The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes." Coller J.M., Tucker M., Sheth U., Valencia-Sanchez M.A., Parker R. RNA 7:1717-1727(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DHH1.
[20]	"The DEAD box protein Dhh1 stimulates the decapping enzyme Dcp1." Fischer N., Weis K. EMBO J. 21:2788-2797(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ACTIVATION BY DHH1.
[21]	"Modulation of eukaryotic mRNA stability via the cap-binding translation complex eIF4F." Ramirez C.V., Vilela C., Berthelot K., McCarthy J.E.G. J. Mol. Biol. 318:951-962(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[22]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[23]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[24]	"Analysis of recombinant yeast decapping enzyme." Steiger M., Carr-Schmid A., Schwartz D.C., Kiledjian M., Parker R. RNA 9:231-238(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE DCP1-DCP2 COMPLEX.
[25]	"Decapping and decay of messenger RNA occur in cytoplasmic processing bodies." Sheth U., Parker R. Science 300:805-808(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[26]	"Loss of translational control in yeast compromised for the major mRNA decay pathway." Holmes L.E.A., Campbell S.G., De Long S.K., Sachs A.B., Ashe M.P. Mol. Cell. Biol. 24:2998-3010(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[27]	"Crystal structure of Dcp1p and its functional implications in mRNA decapping." She M., Decker C.J., Sundramurthy K., Liu Y., Chen N., Parker R., Song H. Nat. Struct. Mol. Biol. 11:249-256(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), INTERACTION WITH DCP2, MUTAGENESIS OF 29-ARG--ASP-31; 32-PRO--ILE-34; 37-LEU-LEU-38; TRP-56; ARG-70; LEU-217 AND LEU-221.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z48239 Genomic DNA. Translation: CAA88278.1.
Z74891 Genomic DNA. Translation: CAA99170.1.
AY558431 Genomic DNA. Translation: AAS56757.1.
BK006948 Genomic DNA. Translation: DAA10636.1.

PIR

S60387.

RefSeq

NP_014492.1. NM_001183403.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Q67	X-ray	2.30	A/B	1-231	[»]

ProteinModelPortal

Q12517.

SMR

Q12517. Positions 17-231.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1288N.

IntAct

Q12517. 23 interactions.

MINT

MINT-390330.

STRING

4932.YOL149W.

Proteomic databases

PaxDb

Q12517.

PeptideAtlas

Q12517.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YOL149W; YOL149W; YOL149W.

GeneID

854016.

KEGG

sce:YOL149W.

Organism-specific databases

CYGD

YOL149w.

SGD

S000005509. DCP1.

Phylogenomic databases

eggNOG

NOG240628.

HOGENOM

HOG000246588.

KO

K12612.

OMA

KLEYQGV.

OrthoDB

EOG4NGKX3.

Gene expression databases

Genevestigator

Q12517.

GermOnline

YOL149W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

2.30.29.30. 2 hits.

InterPro

IPR010334. DCP1.
IPR011993. PH_like_dom.
[Graphical view]

PANTHER

PTHR16290. PTHR16290. 1 hit.

Pfam

PF06058. DCP1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q12517.

NextBio

975538.

Entry information

Entry name

DCP1_YEAST

Accession

Primary (citable) accession number: Q12517
Secondary accession number(s): D6W1S0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2006
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program