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Protein

mRNA-decapping enzyme subunit 1

Gene

dcp1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.1 Publication

GO - Molecular functioni

  • m7G(5')pppN diphosphatase activator activity Source: PomBase
  • RNA binding Source: UniProtKB-KW

GO - Biological processi

  • 7-methylguanosine catabolic process Source: PomBase
  • deadenylation-dependent decapping of nuclear-transcribed mRNA Source: PomBase
  • deadenylation-independent decapping of nuclear-transcribed mRNA Source: PomBase
  • mRNA processing Source: UniProtKB-KW
  • nuclear-transcribed mRNA catabolic process, exonucleolytic, 5'-3' Source: PomBase
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

mRNA processing, Nonsense-mediated mRNA decay

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-SPO-450385. Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA-decapping enzyme subunit 1
Gene namesi
Name:dcp1
ORF Names:SPBC3B9.21
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC3B9.21.
PomBaseiSPBC3B9.21. dcp1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic mRNA processing body Source: PomBase
  • cytoplasmic stress granule Source: PomBase
  • cytosol Source: PomBase
  • Dcp1-Dcp2 complex Source: PomBase
  • mRNA cap binding complex Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 127127mRNA-decapping enzyme subunit 1PRO_0000339336Add
BLAST

Proteomic databases

MaxQBiQ9P805.

Interactioni

Subunit structurei

Component of the decapping complex composed of dcp1 and dcp2.By similarity

Protein-protein interaction databases

BioGridi277548. 11 interactions.
DIPiDIP-29008N.
IntActiQ9P805. 2 interactions.
MINTiMINT-4706793.

Structurei

Secondary structure

1
127
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1917Combined sources
Beta strandi23 – 3614Combined sources
Turni40 – 434Combined sources
Beta strandi47 – 5913Combined sources
Beta strandi64 – 7411Combined sources
Beta strandi77 – 815Combined sources
Helixi84 – 863Combined sources
Beta strandi87 – 904Combined sources
Beta strandi93 – 986Combined sources
Turni99 – 1013Combined sources
Beta strandi102 – 1109Combined sources
Helixi112 – 12413Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QKLX-ray2.33A1-127[»]
2QKMX-ray2.80A/C/E/G1-127[»]
ProteinModelPortaliQ9P805.
SMRiQ9P805. Positions 1-127.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P805.

Family & Domainsi

Sequence similaritiesi

Belongs to the DCP1 family.Curated

Phylogenomic databases

InParanoidiQ9P805.
OMAiRESAQNT.
OrthoDBiEOG7JT790.
PhylomeDBiQ9P805.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR010334. Dcp1.
IPR011993. PH_dom-like.
[Graphical view]
PANTHERiPTHR16290. PTHR16290. 1 hit.
PfamiPF06058. DCP1. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9P805-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDENILRNA VNLQVLKFHY PEIESIIDIA SHVAVYQFDV GSQKWLKTSI
60 70 80 90 100
EGTFFLVKDQ RARVGYVILN RNSPENLYLF INHPSNVHLV DRYLIHRTEN
110 120
QHVVGLWMFD PNDMSRIFNI VKESLLR
Length:127
Mass (Da):14,983
Last modified:October 1, 2000 - v1
Checksum:iDD593F646C61EEC0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB69661.1.
RefSeqiNP_596662.1. NM_001022584.2.

Genome annotation databases

EnsemblFungiiSPBC3B9.21.1; SPBC3B9.21.1:pep; SPBC3B9.21.
GeneIDi2541033.
KEGGispo:SPBC3B9.21.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB69661.1.
RefSeqiNP_596662.1. NM_001022584.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QKLX-ray2.33A1-127[»]
2QKMX-ray2.80A/C/E/G1-127[»]
ProteinModelPortaliQ9P805.
SMRiQ9P805. Positions 1-127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277548. 11 interactions.
DIPiDIP-29008N.
IntActiQ9P805. 2 interactions.
MINTiMINT-4706793.

Proteomic databases

MaxQBiQ9P805.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC3B9.21.1; SPBC3B9.21.1:pep; SPBC3B9.21.
GeneIDi2541033.
KEGGispo:SPBC3B9.21.

Organism-specific databases

EuPathDBiFungiDB:SPBC3B9.21.
PomBaseiSPBC3B9.21. dcp1.

Phylogenomic databases

InParanoidiQ9P805.
OMAiRESAQNT.
OrthoDBiEOG7JT790.
PhylomeDBiQ9P805.

Enzyme and pathway databases

ReactomeiR-SPO-450385. Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.

Miscellaneous databases

EvolutionaryTraceiQ9P805.
NextBioi20802147.
PROiQ9P805.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR010334. Dcp1.
IPR011993. PH_dom-like.
[Graphical view]
PANTHERiPTHR16290. PTHR16290. 1 hit.
PfamiPF06058. DCP1. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Decapping reaction of mRNA requires Dcp1 in fission yeast: its characterization in different species from yeast to human."
    Sakuno T., Araki Y., Ohya Y., Kofuji S., Takahashi S., Hoshino S., Katada T.
    J. Biochem. 136:805-812(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  3. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDCP1_SCHPO
AccessioniPrimary (citable) accession number: Q9P805
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: October 1, 2000
Last modified: May 11, 2016
This is version 89 of the entry and version 1 of the sequence. [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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.