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Protein

Phosphatidic acid phosphohydrolase 1

Gene

PAH1

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. Required for de novo lipid synthesis and formation of lipid droplets. Controles transcription of phospholipid biosynthetic genes and nuclear structure by regulating the amount of membrane present at the nuclear envelope. Involved in plasmid maintenance, in respiration and in cell proliferation.9 Publications

Catalytic activityi

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

Cofactori

Mg2+1 Publication

Enzyme regulationi

Phenylglyoxal and propranolol inhibit activity in dose-dependent manners with IC50 values of 1.3 mM and 0.2 mM, respectively.1 Publication

GO - Molecular functioni

  • phosphatidate phosphatase activity Source: SGD
  • transcription coactivator activity Source: GO_Central
  • transcription regulatory region DNA binding Source: SGD

GO - Biological processi

  • aerobic respiration Source: SGD
  • fatty acid catabolic process Source: GO_Central
  • lipid particle organization Source: SGD
  • phospholipid biosynthetic process Source: SGD
  • plasmid maintenance Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: GO_Central
  • transcription, DNA-templated Source: UniProtKB-KW
  • triglyceride biosynthetic process Source: SGD
  • vacuole fusion, non-autophagic Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15447.
YEAST:G3O-32855-MONOMER.
YEAST:MONOMER3O-4125.
ReactomeiR-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

SwissLipidsiSLP: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
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR165C.
SGDiS000004775. PAH1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • extrinsic component of membrane Source: SGD
  • lipid particle Source: SGD
  • nuclear membrane Source: SGD
  • vacuole Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81L → A: Impairs membrane recruitiment; when associated with A-11 and A-15. 1 Publication
Mutagenesisi11 – 111V → A: Impairs membrane recruitiment; when associated with A-8 and A-15. 1 Publication
Mutagenesisi15 – 151W → A: Impairs membrane recruitiment; when associated with A-8 and A-11. 1 Publication
Mutagenesisi80 – 801G → R: Impairs phosphatidate phosphatase activity. 2 Publications
Mutagenesisi398 – 3981D → E: Impairs phosphatidate phosphatase activity. 2 Publications
Mutagenesisi400 – 4001D → E: Impairs phosphatidate phosphatase activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 862862Phosphatidic acid phosphohydrolase 1PRO_0000209887Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei110 – 1101Phosphoserine1 Publication
Modified residuei114 – 1141Phosphoserine1 Publication
Modified residuei168 – 1681Phosphoserine1 Publication
Modified residuei511 – 5111PhosphoserineCombined sources
Modified residuei602 – 6021Phosphoserine; by CDC28Combined sources2 Publications
Modified residuei723 – 7231Phosphothreonine; by CDC282 Publications
Modified residuei744 – 7441Phosphoserine; by CDC28Combined sources2 Publications
Modified residuei748 – 7481PhosphoserineCombined sources1 Publication
Modified residuei773 – 7731PhosphoserineCombined sources
Modified residuei774 – 7741PhosphoserineCombined sources
Modified residuei810 – 8101PhosphoserineCombined sources
Modified residuei814 – 8141PhosphoserineCombined sources
Modified residuei816 – 8161PhosphothreonineCombined sources
Modified residuei844 – 8441PhosphoserineCombined sources
Modified residuei847 – 8471PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by CDC28 at the onset of mitosis, and dephosphorylated by the NEM1-SPO7 complex. Phosphorylation regulates recruitment on promoters of lipid biosynthetic enzymes.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32567.

PTM databases

iPTMnetiP32567.

Interactioni

Protein-protein interaction databases

BioGridi35343. 135 interactions.
DIPiDIP-1454N.
IntActiP32567. 10 interactions.
MINTiMINT-394846.

Structurei

3D structure databases

ProteinModelPortaliP32567.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 10486N-LIPAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi398 – 4025DXDXT motif

Domaini

The N-terminal amphipathic helix (residues 1 to 18) is involved in the membrane recruitment.1 Publication
Contains one Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic motif essential for phosphatidate phosphatase activity.1 Publication

Sequence similaritiesi

Belongs to the lipin family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000011286.
InParanoidiP32567.
KOiK15728.
OMAiREHSCEL.
OrthoDBiEOG092C1UDO.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR007651. Lipin_N.
IPR013209. LNS2.
IPR031315. LNS2/PITP.
[Graphical view]
PfamiPF04571. Lipin_N. 1 hit.
PF08235. LNS2. 1 hit.
[Graphical view]
SMARTiSM00775. LNS2. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.

Sequencei

Sequence statusi: Complete.

P32567-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:862
Mass (Da):95,031
Last modified:October 1, 1993 - v1
Checksum:i28132EED1906ACBD
GO

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.
PIRiS30911.
RefSeqiNP_013888.1. NM_001182669.1.

Genome annotation databases

EnsemblFungiiYMR165C; YMR165C; YMR165C.
GeneIDi855201.
KEGGisce:YMR165C.

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.
PIRiS30911.
RefSeqiNP_013888.1. NM_001182669.1.

3D structure databases

ProteinModelPortaliP32567.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35343. 135 interactions.
DIPiDIP-1454N.
IntActiP32567. 10 interactions.
MINTiMINT-394846.

Chemistry

SwissLipidsiSLP:000000045.

PTM databases

iPTMnetiP32567.

Proteomic databases

MaxQBiP32567.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR165C; YMR165C; YMR165C.
GeneIDi855201.
KEGGisce:YMR165C.

Organism-specific databases

EuPathDBiFungiDB:YMR165C.
SGDiS000004775. PAH1.

Phylogenomic databases

GeneTreeiENSGT00390000011286.
InParanoidiP32567.
KOiK15728.
OMAiREHSCEL.
OrthoDBiEOG092C1UDO.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15447.
YEAST:G3O-32855-MONOMER.
YEAST:MONOMER3O-4125.
ReactomeiR-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

PROiP32567.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR007651. Lipin_N.
IPR013209. LNS2.
IPR031315. LNS2/PITP.
[Graphical view]
PfamiPF04571. Lipin_N. 1 hit.
PF08235. LNS2. 1 hit.
[Graphical view]
SMARTiSM00775. LNS2. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPAH1_YEAST
AccessioniPrimary (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: September 7, 2016
This is version 139 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 3910 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

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 one 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.