PAH1_ARATH
ID PAH1_ARATH Reviewed; 904 AA.
AC Q9SF47; D8L210; Q0WNF2;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Phosphatidate phosphatase PAH1;
DE EC=3.1.3.4;
DE AltName: Full=Phosphatidic acid phosphohydrolase 1;
DE Short=AtPAH1;
GN Name=PAH1; OrderedLocusNames=At3g09560; ORFNames=F11F8.14;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20699392; DOI=10.1105/tpc.109.071423;
RA Eastmond P.J., Quettier A.L., Kroon J.T., Craddock C., Adams N.,
RA Slabas A.R.;
RT "Phosphatidic acid phosphohydrolase 1 and 2 regulate phospholipid synthesis
RT at the endoplasmic reticulum in Arabidopsis.";
RL Plant Cell 22:2796-2811(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP FUNCTION, COFACTOR, AND DISRUPTION PHENOTYPE.
RX PubMed=19923426; DOI=10.1073/pnas.0907173106;
RA Nakamura Y., Koizumi R., Shui G., Shimojima M., Wenk M.R., Ito T., Ohta H.;
RT "Arabidopsis lipins mediate eukaryotic pathway of lipid metabolism and cope
RT critically with phosphate starvation.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:20978-20983(2009).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, DXDXT MOTIF, AND MUTAGENESIS OF GLY-83;
RP ASP-707; ASP-709 AND SER-752.
RX PubMed=21205207; DOI=10.1111/j.1742-4658.2010.07995.x;
RA Mietkiewska E., Siloto R.M., Dewald J., Shah S., Brindley D.N.,
RA Weselake R.J.;
RT "Lipins from plants are phosphatidate phosphatases that restore lipid
RT synthesis in a pah1Delta mutant strain of Saccharomyces cerevisiae.";
RL FEBS J. 278:764-775(2011).
CC -!- FUNCTION: Magnesium-dependent phosphatidate phosphatase which catalyzes
CC the dephosphorylation of phosphatidate to yield diacylglycerol. Acts
CC redundantly with PAH2 to repress phospholipid biosynthesis at the
CC endoplasmic reticulum (ER). May function indirectly as repressor of
CC multiple enzymes involved in phospholipid biosynthesis. Is involved in
CC the pathway of galactolipid synthesis in the ER, which is required for
CC the membrane lipid remodeling, an essential adaptation mechanism to
CC cope with phosphate starvation. {ECO:0000269|PubMed:19923426,
CC ECO:0000269|PubMed:20699392, ECO:0000269|PubMed:21205207}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19923426, ECO:0000269|PubMed:20699392};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:20699392};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers,
CC siliques, embryos and mature seeds. {ECO:0000269|PubMed:20699392,
CC ECO:0000269|PubMed:21205207}.
CC -!- DOMAIN: Contains 1 Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic motif
CC essential for phosphatidate phosphatase activity.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutants pah1 and pah2-1 show reduced growth.
CC {ECO:0000269|PubMed:19923426, ECO:0000269|PubMed:20699392}.
CC -!- SIMILARITY: Belongs to the lipin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACT37431.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; FJ591133; ACT37431.1; ALT_SEQ; mRNA.
DR EMBL; AC016661; AAF23287.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74780.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74781.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74782.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64193.1; -; Genomic_DNA.
DR EMBL; AK229489; BAF01347.1; -; mRNA.
DR RefSeq; NP_001118604.1; NM_001125132.1.
DR RefSeq; NP_001326239.1; NM_001337827.1.
DR RefSeq; NP_187567.1; NM_111790.4.
DR RefSeq; NP_974268.1; NM_202539.2.
DR AlphaFoldDB; Q9SF47; -.
DR SMR; Q9SF47; -.
DR STRING; 3702.AT3G09560.1; -.
DR iPTMnet; Q9SF47; -.
DR PaxDb; Q9SF47; -.
DR PRIDE; Q9SF47; -.
DR ProMEX; Q9SF47; -.
DR ProteomicsDB; 248653; -.
DR EnsemblPlants; AT3G09560.1; AT3G09560.1; AT3G09560.
DR EnsemblPlants; AT3G09560.2; AT3G09560.2; AT3G09560.
DR EnsemblPlants; AT3G09560.3; AT3G09560.3; AT3G09560.
DR EnsemblPlants; AT3G09560.4; AT3G09560.4; AT3G09560.
DR GeneID; 820113; -.
DR Gramene; AT3G09560.1; AT3G09560.1; AT3G09560.
DR Gramene; AT3G09560.2; AT3G09560.2; AT3G09560.
DR Gramene; AT3G09560.3; AT3G09560.3; AT3G09560.
DR Gramene; AT3G09560.4; AT3G09560.4; AT3G09560.
DR KEGG; ath:AT3G09560; -.
DR Araport; AT3G09560; -.
DR TAIR; locus:2075019; AT3G09560.
DR eggNOG; KOG2116; Eukaryota.
DR HOGENOM; CLU_002546_1_0_1; -.
DR InParanoid; Q9SF47; -.
DR OMA; NFCTEHI; -.
DR OrthoDB; 866929at2759; -.
DR PhylomeDB; Q9SF47; -.
DR BioCyc; ARA:MON-AT3G09560; -.
DR BRENDA; 3.1.3.4; 399.
DR PRO; PR:Q9SF47; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SF47; baseline and differential.
DR Genevisible; Q9SF47; AT.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0032586; C:protein storage vacuole membrane; IDA:UniProtKB.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IBA:GO_Central.
DR GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IGI:TAIR.
DR GO; GO:0019375; P:galactolipid biosynthetic process; IGI:TAIR.
DR GO; GO:0006886; P:intracellular protein transport; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IGI:TAIR.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IGI:TAIR.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR026058; LIPIN.
DR InterPro; IPR031703; Lipin_mid.
DR InterPro; IPR007651; Lipin_N.
DR InterPro; IPR013209; LNS2.
DR InterPro; IPR031315; LNS2/PITP.
DR PANTHER; PTHR12181; PTHR12181; 2.
DR Pfam; PF16876; Lipin_mid; 1.
DR Pfam; PF04571; Lipin_N; 1.
DR Pfam; PF08235; LNS2; 1.
DR SMART; SM00775; LNS2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Lipid biosynthesis; Lipid metabolism;
KW Reference proteome.
FT CHAIN 1..904
FT /note="Phosphatidate phosphatase PAH1"
FT /id="PRO_0000425528"
FT REGION 1..112
FT /note="N-LIP"
FT REGION 254..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..857
FT /note="C-LIP"
FT MOTIF 707..711
FT /note="DXDXT motif"
FT COMPBIAS 309..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 83
FT /note="G->A: Reduces activity 3-fold."
FT /evidence="ECO:0000269|PubMed:21205207"
FT MUTAGEN 707
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:21205207"
FT MUTAGEN 709
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:21205207"
FT MUTAGEN 752
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:21205207"
FT CONFLICT 663
FT /note="Q -> R (in Ref. 4; BAF01347)"
FT /evidence="ECO:0000305"
FT CONFLICT 884
FT /note="L -> F (in Ref. 4; BAF01347)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 904 AA; 101003 MW; A1E9469E71788549 CRC64;
MSLVGRVGSL ISQGVYSVAT PFHPFGGAID VIVVQQQDGS FRSTPWYVRF GKFQGVLKGA
EKFVRISVNG TEADFHMYLD NSGEAYFIRE VDPAANDTNN LISGSENNNG NQNNGVTYRL
EHSLSDSGTG ELREGFDPLS RLERTESDCN RRFYDFQDDP PSPTSEYGSA RFDNLNVESY
GDSQGSDSEV VLVSIDGHIL TAPVSVAEQE AENLRLNTPQ FHLAPGDGTE FCEGNTEFAS
SETPWDTEYI DKVEESSDTA NIASDKVDAI NDERNDLDSH SRDNAEKDSH DAERDLLGSC
LEQSELTKTS ENVKSEEPGP TFEDRNLKEG EFPLRTIMEN DRSEDEVTIE SIDTLVDSFE
SSTTQITIEE VKTTEGSRIS VDSNADSECK DEQTSAETAI LFNNQESSIS VDSNADSECK
DEQPRISAET AILINNQEGG IIESEDQDSE RVSIDSTREE VDKDNEDRKT VVSVGVTSSV
DEGEPDTDQR YELSLCKDEL RQGMGLSAAA EVFDAHMISK EEYINSATSI LESENLVVRI
RETYMPWTKA ARIVLGKAVF DLDLDIQPDD VISVEENESP KPKDDETTIT PSSSGTRWRL
WPIPFRRVKT VEHTGSNSSS EEDLFVDSEP GLQNSPETQS TTESRHESPR RQLVRTNVPT
NEQIASLNLK DGQNMITFSF STRVLGTQQV DAHIYRWRWD TKIVISDVDG TITKSDVLGQ
FMPFIGKDWT QSGVAKLFSA IKENGYQLLF LSARAIVQAY LTRNFLNNLK QDGKALPTGP
VVISPDGLFP ALYREVIRRA PHEFKIACLE DIRKLFPTDY NPFYAGFGNR DTDELSYRKL
GIPKGKIFII NPKGEVATGH RIDVKKSYTS LHTLVNDMFP PTSLVEQEDY NPWNFWKLPI
EEVE
