UniProtKB - P32567 (PAH1_YEAST)
Phosphatidic acid phosphohydrolase 1
PAH1
Functioni
Mg2+-dependent phosphatidate (PA) phosphatase which catalyzes the dephosphorylation of PA to yield diacylglycerol (PubMed:16467296, PubMed:16968695, PubMed:17910939, PubMed:17971454, PubMed:20876142, PubMed:21081492, PubMed:29765047).
Required for de novo lipid synthesis and formation of lipid droplets (PubMed:21422231).
Controls transcription of phospholipid biosynthetic genes and nuclear structure by regulating the amount of membrane present at the nuclear envelope (PubMed:15889145).
Involved in plasmid maintenance, in respiration and in cell proliferation (PubMed:8437575).
10 PublicationsMiscellaneous
Catalytic activityi
- EC:3.1.3.44 Publications
Cofactori
Activity regulationi
GO - Molecular functioni
- phosphatidate phosphatase activity Source: SGD
- transcription cis-regulatory region binding Source: SGD
GO - Biological processi
- aerobic respiration Source: SGD
- cellular lipid metabolic process Source: GO_Central
- fatty acid catabolic process Source: GO_Central
- lipid droplet organization Source: SGD
- phospholipid biosynthetic process Source: SGD
- plasmid maintenance Source: SGD
- triglyceride biosynthetic process Source: SGD
- vacuole fusion, non-autophagic Source: SGD
Keywordsi
Molecular function | Hydrolase |
Biological process | Lipid biosynthesis, Lipid metabolism, Transcription, Transcription regulation |
Enzyme and pathway databases
BRENDAi | 3.1.3.4, 984 |
Reactomei | R-SCE-1483191, Synthesis of PC R-SCE-1483213, Synthesis of PE R-SCE-4419969, Depolymerisation of the Nuclear Lamina R-SCE-75109, Triglyceride biosynthesis |
Chemistry databases
SwissLipidsi | SLP:000000045 |
Names & Taxonomyi
Protein namesi | Recommended name: Phosphatidic acid phosphohydrolase 1 (EC:3.1.3.4)Short name: PAP1 Alternative name(s): Protein SMP2 |
Gene namesi | Name:PAH1 Synonyms:PAP1, SMP2 Ordered Locus Names:YMR165C ORF Names:YM8520.14C |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000004775, PAH1 |
VEuPathDBi | FungiDB:YMR165C |
Subcellular locationi
Cytoplasm and Cytosol
Endoplasmic reticulum
Nucleus
Cytosol
- cytosol Source: SGD
Endoplasmic reticulum
- endoplasmic reticulum membrane Source: UniProtKB-SubCell
Nucleus
- nuclear membrane Source: SGD
- nucleus Source: GO_Central
Vacuole
- vacuole Source: SGD
Other locations
- cytoplasm Source: SGD
- extrinsic component of membrane Source: SGD
- lipid droplet Source: SGD
Keywords - Cellular componenti
Cytoplasm, Endoplasmic reticulum, Membrane, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 8 | L → A: Impairs membrane recruitiment; when associated with A-11 and A-15. 1 Publication | 1 | |
Mutagenesisi | 11 | V → A: Impairs membrane recruitiment; when associated with A-8 and A-15. 1 Publication | 1 | |
Mutagenesisi | 15 | W → A: Impairs membrane recruitiment; when associated with A-8 and A-11. 1 Publication | 1 | |
Mutagenesisi | 80 | G → R: Impairs phosphatidate phosphatase activity. 2 Publications | 1 | |
Mutagenesisi | 398 | D → E: Impairs phosphatidate phosphatase activity. 2 Publications | 1 | |
Mutagenesisi | 400 | D → E: Impairs phosphatidate phosphatase activity. 2 Publications | 1 | |
Mutagenesisi | 496 | K → R: Abolished acetylation by ESA1, leading to decreased diacylglycerol synthesis; when associated with R-801. 1 Publication | 1 | |
Mutagenesisi | 801 | K → R: Abolished acetylation by ESA1, leading to decreased diacylglycerol synthesis; when associated with R-496. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000209887 | 1 – 862 | Phosphatidic acid phosphohydrolase 1Add BLAST | 862 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 110 | Phosphoserine1 Publication | 1 | |
Modified residuei | 114 | Phosphoserine1 Publication | 1 | |
Modified residuei | 168 | Phosphoserine1 Publication | 1 | |
Modified residuei | 496 | N6-acetyllysine1 Publication | 1 | |
Modified residuei | 511 | PhosphoserineCombined sources | 1 | |
Modified residuei | 602 | Phosphoserine; by CDC28Combined sources2 Publications | 1 | |
Modified residuei | 723 | Phosphothreonine; by CDC282 Publications | 1 | |
Modified residuei | 744 | Phosphoserine; by CDC28Combined sources2 Publications | 1 | |
Modified residuei | 748 | PhosphoserineCombined sources1 Publication | 1 | |
Modified residuei | 773 | PhosphoserineCombined sources | 1 | |
Modified residuei | 774 | PhosphoserineCombined sources | 1 | |
Modified residuei | 801 | N6-acetyllysine1 Publication | 1 | |
Modified residuei | 810 | PhosphoserineCombined sources | 1 | |
Modified residuei | 814 | PhosphoserineCombined sources | 1 | |
Modified residuei | 816 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 844 | PhosphoserineCombined sources | 1 | |
Modified residuei | 847 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
MaxQBi | P32567 |
PaxDbi | P32567 |
PRIDEi | P32567 |
PTM databases
iPTMneti | P32567 |
Interactioni
Protein-protein interaction databases
BioGRIDi | 35343, 223 interactors |
DIPi | DIP-1454N |
IntActi | P32567, 10 interactors |
MINTi | P32567 |
STRINGi | 4932.YMR165C |
Miscellaneous databases
RNActi | P32567, protein |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 19 – 104 | N-LIPAdd BLAST | 86 | |
Regioni | 104 – 183 | DisorderedSequence analysisAdd BLAST | 80 | |
Regioni | 300 – 341 | DisorderedSequence analysisAdd BLAST | 42 | |
Regioni | 648 – 732 | DisorderedSequence analysisAdd BLAST | 85 | |
Regioni | 757 – 780 | DisorderedSequence analysisAdd BLAST | 24 | |
Regioni | 807 – 862 | DisorderedSequence analysisAdd BLAST | 56 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 398 – 402 | DXDXT motif | 5 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 104 – 120 | Polar residuesSequence analysisAdd BLAST | 17 | |
Compositional biasi | 128 – 147 | Basic and acidic residuesSequence analysisAdd BLAST | 20 | |
Compositional biasi | 153 – 180 | Polar residuesSequence analysisAdd BLAST | 28 | |
Compositional biasi | 300 – 316 | Polar residuesSequence analysisAdd BLAST | 17 | |
Compositional biasi | 317 – 341 | Basic and acidic residuesSequence analysisAdd BLAST | 25 | |
Compositional biasi | 662 – 732 | Polar residuesSequence analysisAdd BLAST | 71 | |
Compositional biasi | 845 – 862 | Acidic residuesSequence analysisAdd BLAST | 18 |
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG2116, Eukaryota |
GeneTreei | ENSGT00940000168260 |
HOGENOMi | CLU_002546_3_1_1 |
InParanoidi | P32567 |
OMAi | MLDMTGF |
Family and domain databases
Gene3Di | 3.40.50.1000, 1 hit |
InterProi | View protein in InterPro IPR036412, HAD-like_sf IPR023214, HAD_sf IPR026058, LIPIN IPR007651, Lipin_N IPR013209, LNS2 IPR031315, LNS2/PITP |
PANTHERi | PTHR12181, PTHR12181, 2 hits |
Pfami | View protein in Pfam PF04571, Lipin_N, 1 hit PF08235, LNS2, 1 hit |
SMARTi | View protein in SMART SM00775, LNS2, 1 hit |
SUPFAMi | SSF56784, SSF56784, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MQYVGRALGS VSKTWSSINP ATLSGAIDVI VVEHPDGRLS CSPFHVRFGK
60 70 80 90 100
FQILKPSQKK VQVFINEKLS NMPMKLSDSG EAYFVFEMGD QVTDVPDELL
110 120 130 140 150
VSPVMSATSS PPQSPETSIL EGGTEGEGEG ENENKKKEKK VLEEPDFLDI
160 170 180 190 200
NDTGDSGSKN SETTGSLSPT ESSTTTPPDS VEERKLVEQR TKNFQQKLNK
210 220 230 240 250
KLTEIHIPSK LDNNGDLLLD TEGYKPNKNM MHDTDIQLKQ LLKDEFGNDS
260 270 280 290 300
DISSFIKEDK NGNIKIVNPY EHLTDLSPPG TPPTMATSGS VLGLDAMESG
310 320 330 340 350
STLNSLSSSP SGSDTEDETS FSKEQSSKSE KTSKKGTAGS GETEKRYIRT
360 370 380 390 400
IRLTNDQLKC LNLTYGENDL KFSVDHGKAI VTSKLFVWRW DVPIVISDID
410 420 430 440 450
GTITKSDALG HVLAMIGKDW THLGVAKLFS EISRNGYNIL YLTARSAGQA
460 470 480 490 500
DSTRSYLRSI EQNGSKLPNG PVILSPDRTM AALRREVILK KPEVFKIACL
510 520 530 540 550
NDIRSLYFED SDNEVDTEEK STPFFAGFGN RITDALSYRT VGIPSSRIFT
560 570 580 590 600
INTEGEVHME LLELAGYRSS YIHINELVDH FFPPVSLDSV DLRTNTSMVP
610 620 630 640 650
GSPPNRTLDN FDSEITSGRK TLFRGNQEEK FTDVNFWRDP LVDIDNLSDI
660 670 680 690 700
SNDDSDNIDE DTDVSQQSNI SRNRANSVKT AKVTKAPQRN VSGSTNNNEV
710 720 730 740 750
LAASSDVENA SDLVSSHSSS GSTPNKSTMS KGDIGKQIYL ELGSPLASPK
760 770 780 790 800
LRYLDDMDDE DSNYNRTKSR RASSAAATSI DKEFKKLSVS KAGAPTRIVS
810 820 830 840 850
KINVSNDVHS LGNSDTESRR EQSVNETGRN QLPHNSMDDK DLDSRVSDEF
860
DDDEFDEDEF ED
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D01095 Genomic DNA Translation: BAA00880.1 Z49705 Genomic DNA Translation: CAA89801.1 BK006946 Genomic DNA Translation: DAA10061.1 |
PIRi | S30911 |
RefSeqi | NP_013888.1, NM_001182669.1 |
Genome annotation databases
EnsemblFungii | YMR165C_mRNA; YMR165C; YMR165C |
GeneIDi | 855201 |
KEGGi | sce:YMR165C |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D01095 Genomic DNA Translation: BAA00880.1 Z49705 Genomic DNA Translation: CAA89801.1 BK006946 Genomic DNA Translation: DAA10061.1 |
PIRi | S30911 |
RefSeqi | NP_013888.1, NM_001182669.1 |
3D structure databases
SMRi | P32567 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 35343, 223 interactors |
DIPi | DIP-1454N |
IntActi | P32567, 10 interactors |
MINTi | P32567 |
STRINGi | 4932.YMR165C |
Chemistry databases
SwissLipidsi | SLP:000000045 |
PTM databases
iPTMneti | P32567 |
Proteomic databases
MaxQBi | P32567 |
PaxDbi | P32567 |
PRIDEi | P32567 |
Genome annotation databases
EnsemblFungii | YMR165C_mRNA; YMR165C; YMR165C |
GeneIDi | 855201 |
KEGGi | sce:YMR165C |
Organism-specific databases
SGDi | S000004775, PAH1 |
VEuPathDBi | FungiDB:YMR165C |
Phylogenomic databases
eggNOGi | KOG2116, Eukaryota |
GeneTreei | ENSGT00940000168260 |
HOGENOMi | CLU_002546_3_1_1 |
InParanoidi | P32567 |
OMAi | MLDMTGF |
Enzyme and pathway databases
BRENDAi | 3.1.3.4, 984 |
Reactomei | R-SCE-1483191, Synthesis of PC R-SCE-1483213, Synthesis of PE R-SCE-4419969, Depolymerisation of the Nuclear Lamina R-SCE-75109, Triglyceride biosynthesis |
Miscellaneous databases
PROi | PR:P32567 |
RNActi | P32567, protein |
Family and domain databases
Gene3Di | 3.40.50.1000, 1 hit |
InterProi | View protein in InterPro IPR036412, HAD-like_sf IPR023214, HAD_sf IPR026058, LIPIN IPR007651, Lipin_N IPR013209, LNS2 IPR031315, LNS2/PITP |
PANTHERi | PTHR12181, PTHR12181, 2 hits |
Pfami | View protein in Pfam PF04571, Lipin_N, 1 hit PF08235, LNS2, 1 hit |
SMARTi | View protein in SMART SM00775, LNS2, 1 hit |
SUPFAMi | SSF56784, SSF56784, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PAH1_YEAST | |
Accessioni | P32567Primary (citable) accession number: P32567 Secondary accession number(s): D6VZY7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1993 |
Last sequence update: | October 1, 1993 | |
Last modified: | February 23, 2022 | |
This is version 174 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome XIII
Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names - SIMILARITY comments
Index of protein domains and families