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Reviewed, UniProtKB/Swiss-Prot Q9UUA6 (DPP1_SCHPO)

Last modified June 16, 2009. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Probable diacylglycerol pyrophosphate phosphatase 1
      Short name=DGPP phosphatase
    EC=3.1.3.-
Alternative name(s):
    Phosphatidate phosphatase
    EC=3.1.3.4
Gene names
Name: dpp1
ORF Names: SPBC409.18
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

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Protein attributes

Sequence length279 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Catalyzes the dephosphorylation of diacylglycerol phosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG) By similarity.

Catalytic activity

A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.

Diacylglycerol pyrophosphate + H2O = phosphatidate + phosphate.

Subcellular location

Vacuole membrane; Multi-pass membrane protein By similarity. Endoplasmic reticulum membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the PA-phosphatase related phosphoesterase family.

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Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Vacuole
   DomainTransmembrane
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processsecond-messenger-mediated signaling

Inferred by curator. Source: GeneDB_SPombe

   Cellular componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

vacuolar membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionphosphatidate phosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 279279Probable diacylglycerol pyrophosphate phosphatase 1
PRO_0000358314

Regions

Topological domain1 – 1717Lumenal Potential
Transmembrane18 – 3821 Potential
Topological domain39 – 5820Cytoplasmic Potential
Transmembrane59 – 7921 Potential
Topological domain80 – 867Lumenal Potential
Transmembrane87 – 10721 Potential
Topological domain108 – 16356Cytoplasmic Potential
Transmembrane164 – 18421 Potential
Topological domain185 – 1873Lumenal Potential
Transmembrane188 – 20821 Potential
Topological domain209 – 22012Cytoplasmic Potential
Transmembrane221 – 24121 Potential
Topological domain242 – 27938Lumenal Potential
Region111 – 1199Phosphatase sequence motif I
Region159 – 1624Phosphatase sequence motif II
Region209 – 22012Phosphatase sequence motif III

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Sequences

Sequence LengthMass (Da)Tools
Q9UUA6-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 0AEF99E6565ED985

FASTA27931,192
        10         20         30         40         50         60 
MEAVGKHVKL FWNVYSDYAV LIAISLSYFV FDVLMLPFTR QFSLEDITIS HPFALHEQVP 

        70         80         90        100        110        120 
TKYLGIICVF FPALVLYGFG KLRNNSLLFW KSLMGLLYST MVCGLCVSLL KNAVGRPRPD 

       130        140        150        160        170        180 
FLARCQPFES TPKTGLVDVL SCSVPWSDKV LQDGFRSFPS GHTSFSFAGL GFLAIFLAGQ 

       190        200        210        220        230        240 
LKMFRNKTSS WKVVVPLVPL SIASWIGLSR SQDYRHHKED IAVGALFGFA IAYVVYRQLF 

       250        260        270 
PPLDHHNADI LYVQAELDEG YTNVHSAGNS SATNAEQMV

« Hide

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References

[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. expand/collapse author list , 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: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.
[2]"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: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

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Cross-references

Sequence databases

CU329671 Genomic DNA. Translation: CAB52620.1.
PIRT40445.
RefSeqNP_595468.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2541078.
KEGGspo:SPBC409.18.
NMPDRfig|4896.1.peg.1334.

Organism-specific databases

GeneDB_SpombeSPBC409.18.

Phylogenomic databases

OMAQ9UUA6. WATMTHD.

Gene expression databases

ArrayExpressQ9UUA6.

Family and domain databases

InterProIPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamPF01569. PAP2. 1 hit.
[Graphical view]
SMARTSM00014. acidPPc. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameDPP1_SCHPO
AccessionPrimary (citable) accession number: Q9UUA6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: May 1, 2000
Last modified: June 16, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents