PAH2_ARATH
ID PAH2_ARATH Reviewed; 930 AA.
AC Q9FMN2; D8L211;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Phosphatidate phosphatase PAH2;
DE EC=3.1.3.4;
DE AltName: Full=Phosphatidic acid phosphohydrolase 2;
DE Short=AtPAH2;
GN Name=PAH2; OrderedLocusNames=At5g42870; ORFNames=MBD2.6;
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, AND IDENTIFICATION BY
RP 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 [6]
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 [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 PAH1 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FMN2-1; Sequence=Displayed;
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. {ECO:0000250}.
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}.
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DR EMBL; FJ591134; ACT37432.1; -; mRNA.
DR EMBL; AB008264; BAB09188.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94877.1; -; Genomic_DNA.
DR RefSeq; NP_199101.1; NM_123652.3. [Q9FMN2-1]
DR AlphaFoldDB; Q9FMN2; -.
DR SMR; Q9FMN2; -.
DR STRING; 3702.AT5G42870.1; -.
DR iPTMnet; Q9FMN2; -.
DR PaxDb; Q9FMN2; -.
DR PRIDE; Q9FMN2; -.
DR ProteomicsDB; 226050; -. [Q9FMN2-1]
DR EnsemblPlants; AT5G42870.1; AT5G42870.1; AT5G42870. [Q9FMN2-1]
DR GeneID; 834298; -.
DR Gramene; AT5G42870.1; AT5G42870.1; AT5G42870. [Q9FMN2-1]
DR KEGG; ath:AT5G42870; -.
DR Araport; AT5G42870; -.
DR TAIR; locus:2160036; AT5G42870.
DR eggNOG; KOG2116; Eukaryota.
DR HOGENOM; CLU_002546_1_0_1; -.
DR InParanoid; Q9FMN2; -.
DR OrthoDB; 866929at2759; -.
DR PhylomeDB; Q9FMN2; -.
DR BRENDA; 3.1.3.4; 399.
DR PRO; PR:Q9FMN2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMN2; baseline and differential.
DR Genevisible; Q9FMN2; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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: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 Alternative splicing; Cytoplasm; Hydrolase; Lipid biosynthesis;
KW Lipid metabolism; Phosphoprotein; Reference proteome.
FT CHAIN 1..930
FT /note="Phosphatidate phosphatase PAH2"
FT /id="PRO_0000425529"
FT REGION 1..97
FT /note="N-LIP"
FT REGION 192..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..885
FT /note="C-LIP"
FT MOTIF 734..738
FT /note="DXDXT motif"
FT COMPBIAS 205..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 227
FT /note="L -> I (in Ref. 1; ACT37432)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="S -> N (in Ref. 1; ACT37432)"
FT /evidence="ECO:0000305"
FT CONFLICT 439..442
FT /note="KGVE -> NGVD (in Ref. 1; ACT37432)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="N -> I (in Ref. 1; ACT37432)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 930 AA; 101218 MW; F1B5BD4404218E19 CRC64;
MNAVGRIGSY IYRGVGTVSG PFHPFGGAID IIVVEQPDGT FKSSPWYVRF GKFQGVLKNG
RNLIRIDVNG VDSGFNMYLA HTGQAYFLRE VEDVVGESES GEVYTLSSGD EAETTSRDDV
VDKVKIPLKS RSCNYDSPSP RTGNGKIVGK PGILGYVFGG RSVRESQDCG VERAEIAADL
LEVKWSTNID TRKRGKGMSS ESLDGKDYGE STSTSGKSCV EGSSEMLVDS DSILETPLVA
SPTLRFLDEK EQDFRESTNV EDYCEEDGSS GVVVENGLCE ASSMVFSVTS EGSGNVEIFV
EPRTEALAED AVSGSDLDSK QELLRAPESV EIATLGSADQ ADMGSIGTSQ EGSSTGSPVQ
DENKITIKDM HISAGDFEKS QSASGESILQ PEIEEEQFSF SDLDECKPGG NSSVGSSSSD
TVKVDGKESY DETKTSPEKG VENTMALSEP INIERKKDIF TDEMERLVGS LPIMRLQNND
DMDASPSQPL SQSFDPCFNT SKLDLREDES SSGGLDAESV AESSPKLKAF KHVIANPEVV
ELSLCKHLLS EGMGAEAASQ AFNSEKLDME KFASLGPSIL ENDKLVVKIG GCYFPWDAAA
PIILGVVSFG TAQVFEPKGM IAVDRNEKPG DVLAQGSGSW KLWPFSLRRS TKEAEASPSG
DTAEPEEKQE KSSPRPMKKT VRALTPTSEQ LASLDLKDGM NSVTFTFSTN IVGTQQVDAR
IYLWKWNSRI VVSDVDGTIT RSDVLGQFMP LVGIDWSQTG VTHLFSAVKE NGYQLIFLSA
RAISQASVTR QFLVNLKQDG KALPDGPVVI SPDGLFPSLF REVIRRAPHE FKIACLEEIR
GLFPPEHNPF YAGFGNRDTD EISYLKVGIP RGKIFIINPK GEVAVNRRID TRSYTNLHTL
VNRMFPATSS SEPEDFNTWN FWKLPPPSLM
