APP1_YEAST
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 03-AUG-2022, entry version 145.
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; 126.
DR DIP; DIP-2006N; -.
DR IntAct; P53933; 44.
DR MINT; P53933; -.
DR STRING; 4932.YNL094W; -.
DR SwissLipids; SLP:000001946; -.
DR MaxQB; P53933; -.
DR PaxDb; P53933; -.
DR PRIDE; P53933; -.
DR EnsemblFungi; YNL094W_mRNA; YNL094W; YNL094W.
DR GeneID; 855630; -.
DR KEGG; sce:YNL094W; -.
DR SGD; S000005038; APP1.
DR VEuPathDB; FungiDB:YNL094W; -.
DR eggNOG; ENOG502QT5E; Eukaryota.
DR HOGENOM; CLU_022324_0_0_1; -.
DR InParanoid; P53933; -.
DR OMA; MSLWYNT; -.
DR BioCyc; YEAST:G3O-33122-MON; -.
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 Pfam; PF09949; DUF2183; 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
