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Q9UUA6 (DPP1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length279 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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 1,2-diacylglycerol 3-phosphate + 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 Ref.2.

Sequence similarities

Belongs to the PA-phosphatase related phosphoesterase family.

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

Sequences

Sequence LengthMass (Da)Tools
Q9UUA6 [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

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: 972 / ATCC 24843.
[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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329671 Genomic DNA. Translation: CAB52620.1.
PIRT40445.
RefSeqNP_595468.1. NM_001021378.1.

3D structure databases

ProteinModelPortalQ9UUA6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC409.18.1; SPBC409.18.1:pep; SPBC409.18.
GeneID2541078.
GenomeReviewsGene locus dpp1 in contig CU329671_GR.
KEGGspo:SPBC409.18.
NMPDRfig|4896.1.peg.1334.

Organism-specific databases

GeneDB_SpombeSPBC409.18.

Phylogenomic databases

eggNOGfuNOG04236.
GeneTreeEFGT00050000001908.
HOGENOMHBG395619.
OMAHTIQTHG.
OrthoDBEOG43NBNX.

Gene expression databases

ArrayExpressQ9UUA6.

Family and domain databases

InterProIPR016118. P_Acid_Pase/Cl_peroxidase_N.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
Gene3DG3DSA:1.20.144.10. P_Acid_Pase/Cl_peroxidase_N. 1 hit.
PfamPF01569. PAP2. 1 hit.
[Graphical view]
SMARTSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMSSF48317. AcPase_VanPerase. 1 hit.
ProtoNetSearch...

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: December 14, 2011
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents