DPP1_SCHPO
ID DPP1_SCHPO Reviewed; 279 AA.
AC Q9UUA6;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Probable diacylglycerol pyrophosphate phosphatase 1;
DE Short=DGPP phosphatase;
DE EC=3.1.3.81;
DE AltName: Full=Phosphatidate phosphatase;
DE EC=3.1.3.4;
GN Name=dpp1; ORFNames=SPBC409.18;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Catalyzes the dephosphorylation of diacylglycerol phosphate
CC (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA
CC to diacylglycerol (DAG). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-
CC sn-glycero-3-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:27449,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58608, ChEBI:CHEBI:59996; EC=3.1.3.81;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-
CC glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
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DR EMBL; CU329671; CAB52620.1; -; Genomic_DNA.
DR PIR; T40445; T40445.
DR RefSeq; NP_595468.1; NM_001021378.2.
DR AlphaFoldDB; Q9UUA6; -.
DR BioGRID; 277593; 8.
DR STRING; 4896.SPBC409.18.1; -.
DR MaxQB; Q9UUA6; -.
DR PaxDb; Q9UUA6; -.
DR EnsemblFungi; SPBC409.18.1; SPBC409.18.1:pep; SPBC409.18.
DR GeneID; 2541078; -.
DR KEGG; spo:SPBC409.18; -.
DR PomBase; SPBC409.18; -.
DR VEuPathDB; FungiDB:SPBC409.18; -.
DR eggNOG; KOG3030; Eukaryota.
DR HOGENOM; CLU_021458_6_1_1; -.
DR InParanoid; Q9UUA6; -.
DR OMA; WFSYRRY; -.
DR PhylomeDB; Q9UUA6; -.
DR Reactome; R-SPO-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-SPO-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-SPO-419408; Lysosphingolipid and LPA receptors.
DR PRO; PR:Q9UUA6; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000329; C:fungal-type vacuole membrane; ISO:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000810; F:diacylglycerol diphosphate phosphatase activity; ISO:PomBase.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IBA:GO_Central.
DR GO; GO:0006644; P:phospholipid metabolic process; ISO:PomBase.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043216; PA_PP_rel.
DR PANTHER; PTHR10165; PTHR10165; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Hydrolase; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..279
FT /note="Probable diacylglycerol pyrophosphate phosphatase 1"
FT /id="PRO_0000358314"
FT TOPO_DOM 1..17
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..86
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..187
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..279
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 111..119
FT /note="Phosphatase sequence motif I"
FT REGION 159..162
FT /note="Phosphatase sequence motif II"
FT REGION 209..220
FT /note="Phosphatase sequence motif III"
SQ 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
