P53933 · APP1_YEAST
- ProteinPhosphatidate phosphatase APP1
- GeneAPP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids587 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 (PubMed:23071111, PubMed:23335564).
Can also utilize diacylglycerol pyrophosphate and lyso-PA as substrates with specificity constants 4- and 7-fold lower, respectively, when compared with PA (PubMed:23335564).
Can also utilize diacylglycerol pyrophosphate and lyso-PA as substrates with specificity constants 4- and 7-fold lower, respectively, when compared with PA (PubMed:23335564).
Miscellaneous
Present with 2289 molecules/cell in log phase SD medium.
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
- 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-di-(9Z-octadecenoyl)-sn-glycerol + phosphateThis reaction proceeds in the forward direction.
Cofactor
Activity regulation
Inhibited by N-ethylmaleimide.
Kinetics
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
577 μmol/min/mg |
pH Dependence
Optimum pH is 7.5.
Temperature Dependence
Optimum temperature is 30 degrees Celsius.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | actin cortical patch | |
Molecular Function | phosphatidate phosphatase activity | |
Biological Process | cellular lipid metabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended namePhosphatidate phosphatase APP1
- EC number
- Short namesPAP
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP53933
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 281 | Abolishes PAP activity. | ||||
Sequence: D → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 8 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000076180 | 1-587 | Phosphatidate phosphatase APP1 | |||
Sequence: MNSQGYDESSSSTAATSGPTSGDPRMGKKQRFMNLIRTTKDVYIPNLTSSISQKTMDGIRSTTNSFEGYNDLPMELPHNTTITYFPTYTTTNLVDPDGLSAPRKDFETTVRCAVSYPGNPTSRRNRWLLSLCKQYLRTGTAEADVAPVVPPHLEEDSGDLNDSQSSIESSLSSKSENRYSHMGIQEEDVLNERIQGFLSKKVPNTPVVVDLLPKDKLRGDTASFFGTTDSYGNLLIKAETDFLPSKINITLDTPIEGHADPISETFPANYVSPYGIGLISDIDDTIKHTGVTGDRRSMFRNVFIHDVQSWVIDGVPLWYKTLHDVADVDFFYVSNSPIQTFTLLKQYICANFPPGPIFLKQYSGNFFSTIMTSSANRKIQPIANILKDFPKKKFILVGDSGEHDLEAYTTTALQFPNQILAIYIRCCSNSMSDVPSHDEEVMNEVNNIIELQQRPMQMTKSTVRTRRRPPPPPIPSTQKPSLTEEQTESIRMSRRNKDENNAKRVAPPPLPNRQLPNLDANTYYVPSSQNDYGMYGAFMDKKADEWKRRVMDSIQKLSNQDTTLMFFSDPALSLEDSIRRIREKYSN |
Post-translational modification
N-glycosylated.
Keywords
- PTM
Proteomic databases
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P53933 | ABP1 P15891 | 12 | EBI-28798, EBI-2036 | |
BINARY | P53933 | BBC1 P47068 | 3 | EBI-28798, EBI-3437 | |
BINARY | P53933 | BZZ1 P38822 | 14 | EBI-28798, EBI-3889 | |
BINARY | P53933 | HOF1 Q05080 | 2 | EBI-28798, EBI-5412 | |
BINARY | P53933 | LSB1 P53281 | 4 | EBI-28798, EBI-23329 | |
BINARY | P53933 | LSB3 P43603 | 8 | EBI-28798, EBI-22980 | |
BINARY | P53933 | MYO5 Q04439 | 2 | EBI-28798, EBI-11687 | |
BINARY | P53933 | PEX13 P80667 | 2 | EBI-28798, EBI-13206 | |
BINARY | P53933 | PIN3 Q06449 | 4 | EBI-28798, EBI-35523 | |
BINARY | P53933 | RVS167 P39743 | 9 | EBI-28798, EBI-14500 | |
BINARY | P53933 | SLA1 P32790 | 4 | EBI-28798, EBI-17313 | |
BINARY | P53933 | YSC84 P32793 | 6 | EBI-28798, EBI-24460 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-20 | Polar residues | ||||
Sequence: MNSQGYDESSSSTAATSGPT | ||||||
Region | 1-28 | Disordered | ||||
Sequence: MNSQGYDESSSSTAATSGPTSGDPRMGK | ||||||
Region | 150-178 | Disordered | ||||
Sequence: PPHLEEDSGDLNDSQSSIESSLSSKSENR | ||||||
Compositional bias | 160-178 | Polar residues | ||||
Sequence: LNDSQSSIESSLSSKSENR | ||||||
Motif | 281-285 | DXDXT motif | ||||
Sequence: DIDDT | ||||||
Region | 452-521 | Disordered | ||||
Sequence: QQRPMQMTKSTVRTRRRPPPPPIPSTQKPSLTEEQTESIRMSRRNKDENNAKRVAPPPLPNRQLPNLDAN | ||||||
Region | 467-483 | Interaction with SH3 domain of ABP1 | ||||
Sequence: RRPPPPPIPSTQKPSLT | ||||||
Compositional bias | 488-502 | Basic and acidic residues | ||||
Sequence: ESIRMSRRNKDENNA |
Domain
Contains one Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic motif essential for phosphatidate phosphatase activity.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length587
- Mass (Da)66,134
- Last updated1996-10-01 v1
- ChecksumB85C525548BA34BC
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-20 | Polar residues | ||||
Sequence: MNSQGYDESSSSTAATSGPT | ||||||
Compositional bias | 160-178 | Polar residues | ||||
Sequence: LNDSQSSIESSLSSKSENR | ||||||
Compositional bias | 488-502 | Basic and acidic residues | ||||
Sequence: ESIRMSRRNKDENNA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X85811 EMBL· GenBank· DDBJ | CAA59823.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
Z71370 EMBL· GenBank· DDBJ | CAA95970.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006947 EMBL· GenBank· DDBJ | DAA10452.1 EMBL· GenBank· DDBJ | Genomic DNA |