ID   APP1_YEAST              Reviewed;         587 AA.
AC   P53933; D6W186;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-NOV-2023, entry version 150.
DE   RecName: Full=Phosphatidate phosphatase APP1;
DE            Short=PAP;
DE            EC=3.1.3.4;
DE   AltName: Full=Actin patch protein 1;
GN   Name=APP1; OrderedLocusNames=YNL094W; ORFNames=N2219;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8771715;
RX   DOI=10.1002/(sici)1097-0061(199605)12:6<599::aid-yea938>3.0.co;2-9;
RA   Garcia-Cantalejo J.M., Boskovic J., Jimenez A.;
RT   "Sequence analysis of a 14.2 kb fragment of Saccharomyces cerevisiae
RT   chromosome XIV that includes the ypt53, tRNALeu and gsr m2 genes and four
RT   new open reading frames.";
RL   Yeast 12:599-608(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11489916; DOI=10.1083/jcb.200104057;
RA   Drees B.L., Sundin B.A., Brazeau E., Caviston J.P., Chen G.-C., Guo W.,
RA   Kozminski K.G., Lau M.W., Moskow J.J., Tong A., Schenkman L.R.,
RA   McKenzie A. III, Brennwald P.J., Longtine M., Bi E., Chan C., Novick P.,
RA   Boone C., Pringle J.R., Davis T.N., Fields S., Drubin D.G.;
RT   "A protein interaction map for cell polarity development.";
RL   J. Cell Biol. 154:549-571(2001).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   INTERACTION WITH ABP1.
RX   PubMed=14737190; DOI=10.1371/journal.pbio.0020014;
RA   Landgraf C., Panni S., Montecchi-Palazzi L., Castagnoli L.,
RA   Schneider-Mergener J., Volkmer-Engert R., Cesareni G.;
RT   "Protein interaction networks by proteome peptide scanning.";
RL   PLoS Biol. 2:94-103(2004).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX   PubMed=19756047; DOI=10.1038/msb.2009.64;
RA   Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT   "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT   new roles for protein glycosylation in eukaryotes.";
RL   Mol. Syst. Biol. 5:308-308(2009).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP   ASP-281.
RX   PubMed=23071111; DOI=10.1074/jbc.m112.421776;
RA   Chae M., Han G.S., Carman G.M.;
RT   "The Saccharomyces cerevisiae actin patch protein App1p is a phosphatidate
RT   phosphatase enzyme.";
RL   J. Biol. Chem. 287:40186-40196(2012).
RN   [10]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP   SUBUNIT.
RX   PubMed=23335564; DOI=10.1074/jbc.m112.449629;
RA   Chae M., Carman G.M.;
RT   "Characterization of the yeast actin patch protein App1p phosphatidate
RT   phosphatase.";
RL   J. Biol. Chem. 288:6427-6437(2013).
CC   -!- FUNCTION: Mg(2+)-dependent phosphatidate (PA) phosphatase which
CC       catalyzes the dephosphorylation of PA to yield diacylglycerol. May play
CC       a role in vesicular trafficking through its PAP activity at cortical
CC       actin patches (PubMed:23071111, PubMed:23335564). Can also utilize
CC       diacylglycerol pyrophosphate and lyso-PA as substrates with specificity
CC       constants 4- and 7-fold lower, respectively, when compared with PA
CC       (PubMed:23335564). {ECO:0000269|PubMed:23071111,
CC       ECO:0000269|PubMed:23335564}.
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         Evidence={ECO:0000269|PubMed:23071111};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-
CC         di-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43244,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52333,
CC         ChEBI:CHEBI:74546; Evidence={ECO:0000269|PubMed:23335564};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245;
CC         Evidence={ECO:0000305|PubMed:23335564};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:23335564};
CC   -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide.
CC       {ECO:0000269|PubMed:23071111}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=577 umol/min/mg enzyme {ECO:0000269|PubMed:23335564};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:23335564};
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.
CC         {ECO:0000269|PubMed:23335564};
CC   -!- SUBUNIT: Monomer (PubMed:23335564). Interacts with ABP1
CC       (PubMed:14737190). {ECO:0000269|PubMed:14737190,
CC       ECO:0000269|PubMed:23335564}.
CC   -!- INTERACTION:
CC       P53933; P15891: ABP1; NbExp=11; IntAct=EBI-28798, EBI-2036;
CC       P53933; P47068: BBC1; NbExp=3; IntAct=EBI-28798, EBI-3437;
CC       P53933; P38822: BZZ1; NbExp=14; IntAct=EBI-28798, EBI-3889;
CC       P53933; Q05080: HOF1; NbExp=2; IntAct=EBI-28798, EBI-5412;
CC       P53933; P53281: LSB1; NbExp=4; IntAct=EBI-28798, EBI-23329;
CC       P53933; P43603: LSB3; NbExp=8; IntAct=EBI-28798, EBI-22980;
CC       P53933; Q04439: MYO5; NbExp=2; IntAct=EBI-28798, EBI-11687;
CC       P53933; P80667: PEX13; NbExp=2; IntAct=EBI-28798, EBI-13206;
CC       P53933; Q06449: PIN3; NbExp=4; IntAct=EBI-28798, EBI-35523;
CC       P53933; P39743: RVS167; NbExp=9; IntAct=EBI-28798, EBI-14500;
CC       P53933; P32790: SLA1; NbExp=4; IntAct=EBI-28798, EBI-17313;
CC       P53933; P32793: YSC84; NbExp=6; IntAct=EBI-28798, EBI-24460;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC       {ECO:0000269|PubMed:11489916, ECO:0000269|PubMed:14562095}.
CC   -!- DOMAIN: Contains one Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic
CC       motif essential for phosphatidate phosphatase activity.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC   -!- MISCELLANEOUS: Present with 2289 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA59823.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X85811; CAA59823.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z71370; CAA95970.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10452.1; -; Genomic_DNA.
DR   PIR; S63033; S63033.
DR   RefSeq; NP_014305.1; NM_001182932.1.
DR   AlphaFoldDB; P53933; -.
DR   BioGRID; 35730; 127.
DR   DIP; DIP-2006N; -.
DR   IntAct; P53933; 44.
DR   MINT; P53933; -.
DR   STRING; 4932.YNL094W; -.
DR   SwissLipids; SLP:000001946; -.
DR   MaxQB; P53933; -.
DR   PaxDb; 4932-YNL094W; -.
DR   PeptideAtlas; P53933; -.
DR   EnsemblFungi; YNL094W_mRNA; YNL094W; YNL094W.
DR   GeneID; 855630; -.
DR   KEGG; sce:YNL094W; -.
DR   AGR; SGD:S000005038; -.
DR   SGD; S000005038; APP1.
DR   VEuPathDB; FungiDB:YNL094W; -.
DR   eggNOG; ENOG502QT5E; Eukaryota.
DR   HOGENOM; CLU_022324_0_0_1; -.
DR   InParanoid; P53933; -.
DR   OMA; IYIRCCK; -.
DR   OrthoDB; 1709418at2759; -.
DR   BioCyc; YEAST:G3O-33122-MONOMER; -.
DR   BioGRID-ORCS; 855630; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P53933; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53933; Protein.
DR   GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; IDA:SGD.
DR   GO; GO:0044255; P:cellular lipid metabolic process; IMP:SGD.
DR   InterPro; IPR017210; APP1.
DR   InterPro; IPR019236; APP1_cat.
DR   PANTHER; PTHR28208; PHOSPHATIDATE PHOSPHATASE APP1; 1.
DR   PANTHER; PTHR28208:SF3; PHOSPHATIDATE PHOSPHATASE APP1; 1.
DR   Pfam; PF09949; APP1_cat; 1.
DR   PIRSF; PIRSF037464; UCP037464_APP1; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Glycoprotein; Hydrolase; Lipid metabolism;
KW   Reference proteome.
FT   CHAIN           1..587
FT                   /note="Phosphatidate phosphatase APP1"
FT                   /id="PRO_0000076180"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          150..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          467..483
FT                   /note="Interaction with SH3 domain of ABP1"
FT   MOTIF           281..285
FT                   /note="DXDXT motif"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..502
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         281
FT                   /note="D->E: Abolishes PAP activity."
FT                   /evidence="ECO:0000269|PubMed:23071111"
SQ   SEQUENCE   587 AA;  66134 MW;  B85C525548BA34BC CRC64;
     MNSQGYDESS SSTAATSGPT SGDPRMGKKQ RFMNLIRTTK DVYIPNLTSS ISQKTMDGIR
     STTNSFEGYN DLPMELPHNT TITYFPTYTT TNLVDPDGLS APRKDFETTV RCAVSYPGNP
     TSRRNRWLLS LCKQYLRTGT AEADVAPVVP PHLEEDSGDL NDSQSSIESS LSSKSENRYS
     HMGIQEEDVL NERIQGFLSK KVPNTPVVVD LLPKDKLRGD TASFFGTTDS YGNLLIKAET
     DFLPSKINIT LDTPIEGHAD PISETFPANY VSPYGIGLIS DIDDTIKHTG VTGDRRSMFR
     NVFIHDVQSW VIDGVPLWYK TLHDVADVDF FYVSNSPIQT FTLLKQYICA NFPPGPIFLK
     QYSGNFFSTI MTSSANRKIQ PIANILKDFP KKKFILVGDS GEHDLEAYTT TALQFPNQIL
     AIYIRCCSNS MSDVPSHDEE VMNEVNNIIE LQQRPMQMTK STVRTRRRPP PPPIPSTQKP
     SLTEEQTESI RMSRRNKDEN NAKRVAPPPL PNRQLPNLDA NTYYVPSSQN DYGMYGAFMD
     KKADEWKRRV MDSIQKLSNQ DTTLMFFSDP ALSLEDSIRR IREKYSN
//