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Protein

Phosphatidate phosphatase APP1

Gene

APP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mg2+-dependent phosphatidate (PA) phosphatase which catalyzes the dephosphorylation of PA to yield diacylglycerol. May play a role in vesicular trafficking through its PAP activity at cortical actin patches.1 Publication

Catalytic activityi

A 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.1 Publication

Cofactori

Mg2+By similarity

Enzyme regulationi

Inhibited by N-ethylmaleimide.1 Publication

GO - Molecular functioni

  • phosphatidate phosphatase activity Source: SGD

GO - Biological processi

  • actin cytoskeleton organization Source: SGD
  • cellular lipid metabolic process Source: SGD
  • dephosphorylation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid metabolism

Enzyme and pathway databases

BioCyciYEAST:G3O-33122-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidate phosphatase APP1 (EC:3.1.3.4)
Short name:
PAP
Alternative name(s):
Actin patch protein 1
Gene namesi
Name:APP1
Ordered Locus Names:YNL094W
ORF Names:N2219
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIV

Organism-specific databases

CYGDiYNL094w.
EuPathDBiFungiDB:YNL094W.
SGDiS000005038. APP1.

Subcellular locationi

GO - Cellular componenti

  • actin cortical patch Source: SGD
  • actin cytoskeleton Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi281 – 2811D → E: Abolishes PAP activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 587587Phosphatidate phosphatase APP1PRO_0000076180Add
BLAST

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP53933.
PaxDbiP53933.

Interactioni

Subunit structurei

Interacts with ABP1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ABP1P158919EBI-28798,EBI-2036
BBC1P470683EBI-28798,EBI-3437
BZZ1P3882214EBI-28798,EBI-3889
HOF1Q050802EBI-28798,EBI-5412
LSB1P532814EBI-28798,EBI-23329
LSB3P436038EBI-28798,EBI-22980
MYO5Q044392EBI-28798,EBI-11687
PEX13P806672EBI-28798,EBI-13206
PIN3Q064494EBI-28798,EBI-35523
RVS167P397439EBI-28798,EBI-14500
SLA1P327904EBI-28798,EBI-17313
YSC84P327936EBI-28798,EBI-24460

Protein-protein interaction databases

BioGridi35730. 57 interactions.
DIPiDIP-2006N.
IntActiP53933. 28 interactions.
MINTiMINT-385983.

Structurei

3D structure databases

ProteinModelPortaliP53933.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni467 – 48317Interaction with SH3 domain of ABP1Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi281 – 2855DXDXT motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi469 – 4757Poly-Pro

Domaini

Contains one Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic motif essential for phosphatidate phosphatase activity.

Phylogenomic databases

eggNOGiCOG4850.
HOGENOMiHOG000000857.
InParanoidiP53933.
OMAiHLKQYTG.
OrthoDBiEOG7P2Z1R.

Family and domain databases

InterProiIPR017210. APP1.
IPR019236. DUF2183.
[Graphical view]
PfamiPF09949. DUF2183. 1 hit.
[Graphical view]
PIRSFiPIRSF037464. UCP037464_APP1. 1 hit.

Sequencei

Sequence statusi: Complete.

P53933-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSQGYDESS SSTAATSGPT SGDPRMGKKQ RFMNLIRTTK DVYIPNLTSS
60 70 80 90 100
ISQKTMDGIR STTNSFEGYN DLPMELPHNT TITYFPTYTT TNLVDPDGLS
110 120 130 140 150
APRKDFETTV RCAVSYPGNP TSRRNRWLLS LCKQYLRTGT AEADVAPVVP
160 170 180 190 200
PHLEEDSGDL NDSQSSIESS LSSKSENRYS HMGIQEEDVL NERIQGFLSK
210 220 230 240 250
KVPNTPVVVD LLPKDKLRGD TASFFGTTDS YGNLLIKAET DFLPSKINIT
260 270 280 290 300
LDTPIEGHAD PISETFPANY VSPYGIGLIS DIDDTIKHTG VTGDRRSMFR
310 320 330 340 350
NVFIHDVQSW VIDGVPLWYK TLHDVADVDF FYVSNSPIQT FTLLKQYICA
360 370 380 390 400
NFPPGPIFLK QYSGNFFSTI MTSSANRKIQ PIANILKDFP KKKFILVGDS
410 420 430 440 450
GEHDLEAYTT TALQFPNQIL AIYIRCCSNS MSDVPSHDEE VMNEVNNIIE
460 470 480 490 500
LQQRPMQMTK STVRTRRRPP PPPIPSTQKP SLTEEQTESI RMSRRNKDEN
510 520 530 540 550
NAKRVAPPPL PNRQLPNLDA NTYYVPSSQN DYGMYGAFMD KKADEWKRRV
560 570 580
MDSIQKLSNQ DTTLMFFSDP ALSLEDSIRR IREKYSN
Length:587
Mass (Da):66,134
Last modified:October 1, 1996 - v1
Checksum:iB85C525548BA34BC
GO

Sequence cautioni

The sequence CAA59823.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85811 Genomic DNA. Translation: CAA59823.1. Different initiation.
Z71370 Genomic DNA. Translation: CAA95970.1.
BK006947 Genomic DNA. Translation: DAA10452.1.
PIRiS63033.
RefSeqiNP_014305.1. NM_001182932.1.

Genome annotation databases

EnsemblFungiiYNL094W; YNL094W; YNL094W.
GeneIDi855630.
KEGGisce:YNL094W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85811 Genomic DNA. Translation: CAA59823.1. Different initiation.
Z71370 Genomic DNA. Translation: CAA95970.1.
BK006947 Genomic DNA. Translation: DAA10452.1.
PIRiS63033.
RefSeqiNP_014305.1. NM_001182932.1.

3D structure databases

ProteinModelPortaliP53933.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35730. 57 interactions.
DIPiDIP-2006N.
IntActiP53933. 28 interactions.
MINTiMINT-385983.

Proteomic databases

MaxQBiP53933.
PaxDbiP53933.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL094W; YNL094W; YNL094W.
GeneIDi855630.
KEGGisce:YNL094W.

Organism-specific databases

CYGDiYNL094w.
EuPathDBiFungiDB:YNL094W.
SGDiS000005038. APP1.

Phylogenomic databases

eggNOGiCOG4850.
HOGENOMiHOG000000857.
InParanoidiP53933.
OMAiHLKQYTG.
OrthoDBiEOG7P2Z1R.

Enzyme and pathway databases

BioCyciYEAST:G3O-33122-MONOMER.

Miscellaneous databases

NextBioi979839.
PROiP53933.

Family and domain databases

InterProiIPR017210. APP1.
IPR019236. DUF2183.
[Graphical view]
PfamiPF09949. DUF2183. 1 hit.
[Graphical view]
PIRSFiPIRSF037464. UCP037464_APP1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of a 14.2 kb fragment of Saccharomyces cerevisiae chromosome XIV that includes the ypt53, tRNALeu and gsr m2 genes and four new open reading frames."
    Garcia-Cantalejo J.M., Boskovic J., Jimenez A.
    Yeast 12:599-608(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: SUBCELLULAR LOCATION.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: INTERACTION WITH ABP1.
  8. "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes."
    Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.
    Mol. Syst. Biol. 5:308-308(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS].
  9. "The Saccharomyces cerevisiae actin patch protein App1p is a phosphatidate phosphatase enzyme."
    Chae M., Han G.S., Carman G.M.
    J. Biol. Chem. 287:40186-40196(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, MUTAGENESIS OF ASP-281.

Entry informationi

Entry nameiAPP1_YEAST
AccessioniPrimary (citable) accession number: P53933
Secondary accession number(s): D6W186
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 22, 2015
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2289 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.