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Probable diacylglycerol pyrophosphate phosphatase 1 (DGPP phosphatase) (EC 3.1.3.81) (Phosphatidate phosphatase) (EC 3.1.3.4)

 DPP1_SCHPO              Reviewed;         279 AA.
Q9UUA6;
16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 105.
RecName: Full=Probable diacylglycerol pyrophosphate phosphatase 1;
Short=DGPP phosphatase;
EC=3.1.3.81;
AltName: Full=Phosphatidate phosphatase;
EC=3.1.3.4;
Name=dpp1; ORFNames=SPBC409.18;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
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.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=16823372; DOI=10.1038/nbt1222;
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the
fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
-!- FUNCTION: Catalyzes the dephosphorylation of diacylglycerol
phosphate (DGPP) to phosphatidate (PA) and the subsequent
dephosphorylation of PA to diacylglycerol (DAG). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: 1,2-diacyl-sn-glycerol 3-diphosphate + H(2)O =
1,2-diacyl-sn-glycerol 3-phosphate + phosphate.
-!- CATALYTIC ACTIVITY: A 1,2-diacylglycerol 3-phosphate + H(2)O = a
1,2-diacyl-sn-glycerol + phosphate.
-!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
{ECO:0000269|PubMed:16823372}.
-!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CU329671; CAB52620.1; -; Genomic_DNA.
PIR; T40445; T40445.
RefSeq; NP_595468.1; NM_001021378.2.
ProteinModelPortal; Q9UUA6; -.
SMR; Q9UUA6; -.
BioGrid; 277593; 8.
MINT; MINT-4711516; -.
STRING; 4896.SPBC409.18.1; -.
MaxQB; Q9UUA6; -.
PRIDE; Q9UUA6; -.
EnsemblFungi; SPBC409.18.1; SPBC409.18.1:pep; SPBC409.18.
GeneID; 2541078; -.
KEGG; spo:SPBC409.18; -.
EuPathDB; FungiDB:SPBC409.18; -.
PomBase; SPBC409.18; -.
HOGENOM; HOG000215098; -.
InParanoid; Q9UUA6; -.
KO; K18693; -.
OMA; IQYPFAV; -.
OrthoDB; EOG092C29DM; -.
PhylomeDB; Q9UUA6; -.
Reactome; R-SPO-2029485; Role of phospholipids in phagocytosis.
PRO; PR:Q9UUA6; -.
Proteomes; UP000002485; Chromosome II.
GO; GO:0005783; C:endoplasmic reticulum; IDA:PomBase.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0000329; C:fungal-type vacuole membrane; ISO:PomBase.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0000810; F:diacylglycerol diphosphate phosphatase activity; ISO:PomBase.
GO; GO:0008195; F:phosphatidate phosphatase activity; IBA:GO_Central.
GO; GO:0006644; P:phospholipid metabolic process; ISO:PomBase.
InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
Pfam; PF01569; PAP2; 1.
SMART; SM00014; acidPPc; 1.
SUPFAM; SSF48317; SSF48317; 1.
3: Inferred from homology;
Complete proteome; Endoplasmic reticulum; Hydrolase; Membrane;
Reference proteome; Transmembrane; Transmembrane helix; Vacuole.
CHAIN 1 279 Probable diacylglycerol pyrophosphate
phosphatase 1.
/FTId=PRO_0000358314.
TOPO_DOM 1 17 Lumenal. {ECO:0000255}.
TRANSMEM 18 38 Helical. {ECO:0000255}.
TOPO_DOM 39 58 Cytoplasmic. {ECO:0000255}.
TRANSMEM 59 79 Helical. {ECO:0000255}.
TOPO_DOM 80 86 Lumenal. {ECO:0000255}.
TRANSMEM 87 107 Helical. {ECO:0000255}.
TOPO_DOM 108 163 Cytoplasmic. {ECO:0000255}.
TRANSMEM 164 184 Helical. {ECO:0000255}.
TOPO_DOM 185 187 Lumenal. {ECO:0000255}.
TRANSMEM 188 208 Helical. {ECO:0000255}.
TOPO_DOM 209 220 Cytoplasmic. {ECO:0000255}.
TRANSMEM 221 241 Helical. {ECO:0000255}.
TOPO_DOM 242 279 Lumenal. {ECO:0000255}.
REGION 111 119 Phosphatase sequence motif I.
REGION 159 162 Phosphatase sequence motif II.
REGION 209 220 Phosphatase sequence motif III.
SEQUENCE 279 AA; 31192 MW; 0AEF99E6565ED985 CRC64;
MEAVGKHVKL FWNVYSDYAV LIAISLSYFV FDVLMLPFTR QFSLEDITIS HPFALHEQVP
TKYLGIICVF FPALVLYGFG KLRNNSLLFW KSLMGLLYST MVCGLCVSLL KNAVGRPRPD
FLARCQPFES TPKTGLVDVL SCSVPWSDKV LQDGFRSFPS GHTSFSFAGL GFLAIFLAGQ
LKMFRNKTSS WKVVVPLVPL SIASWIGLSR SQDYRHHKED IAVGALFGFA IAYVVYRQLF
PPLDHHNADI LYVQAELDEG YTNVHSAGNS SATNAEQMV


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