ID IP5P1_ARATH Reviewed; 590 AA. AC Q84MA2; Q0WU22; Q9FUR3; Q9FX20; Q9ZSC4; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 2. DT 24-JAN-2024, entry version 137. DE RecName: Full=Type I inositol polyphosphate 5-phosphatase 1 {ECO:0000303|PubMed:11402208}; DE Short=At5PTase1 {ECO:0000303|PubMed:11402208}; DE EC=3.1.3.56 {ECO:0000269|PubMed:11402208}; GN Name=IP5P1 {ECO:0000303|PubMed:11340187}; GN Synonyms=5P1 {ECO:0000303|Ref.2}; GN OrderedLocusNames=At1g34120 {ECO:0000312|Araport:AT1G34120}; GN ORFNames=F12G12.6 {ECO:0000312|EMBL:AAG12525.1}; 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] (ISOFORM 2). RC STRAIN=cv. Landsberg erecta; RX PubMed=11340187; DOI=10.1105/tpc.13.5.1143; RA Sanchez J.-P., Chua N.-H.; RT "Arabidopsis PLC1 is required for secondary responses to abscisic acid RT signals."; RL Plant Cell 13:1143-1154(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=cv. Columbia; RA Parzer M.S.A., de Vos S., van Lookeren Campagne M.M.; RT "Characterization of putative inositol (1,4,5)- RT trisphosphate/phosphatidylinositol (4,5)-bisphosphate 5-phosphatase cDNAs RT from Arabidopsis thaliana."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., RA Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."; RL Nature 408:816-820(2000). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [7] RP GENE FAMILY, FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY. RX PubMed=11402208; DOI=10.1104/pp.126.2.801; RA Berdy S.E., Kudla J., Gruissem W., Gillaspy G.E.; RT "Molecular characterization of At5PTase1, an inositol phosphatase capable RT of terminating inositol trisphosphate signaling."; RL Plant Physiol. 126:801-810(2001). RN [8] RP FUNCTION, AND INDUCTION. RX PubMed=12805629; DOI=10.1104/pp.102.019000; RA Burnette R.N., Gunesekera B.M., Gillaspy G.E.; RT "An Arabidopsis inositol 5-phosphatase gain-of-function alters abscisic RT acid signaling."; RL Plant Physiol. 132:1011-1019(2003). RN [9] RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY. RX PubMed=17237190; DOI=10.1104/pp.106.089474; RA Gunesekera B., Torabinejad J., Robinson J., Gillaspy G.E.; RT "Inositol polyphosphate 5-phosphatases 1 and 2 are required for regulating RT seedling growth."; RL Plant Physiol. 143:1408-1417(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY RP 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, 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 [12] RP DISRUPTION PHENOTYPE, AND FUNCTION. RX PubMed=23658066; DOI=10.1093/mp/sst072; RA Golani Y., Kaye Y., Gilhar O., Ercetin M., Gillaspy G., Levine A.; RT "Inositol polyphosphate phosphatidylinositol 5-phosphatase9 (At5ptase9) RT controls plant salt tolerance by regulating endocytosis."; RL Mol. Plant 6:1781-1794(2013). CC -!- FUNCTION: Has phosphatase activity toward Ins(1,4,5)P3 and CC Ins(1,3,4,5)P4, but not toward Ins(1,4)P2, Ins(1)P (PubMed:11402208). CC Seems to be involved in the abscisic acid (ABA) signaling pathway CC (PubMed:12805629). Could also be able to hydrolyze PtdIns(4,5)P2 and CC PtdIns(3,4,5)P3 (PubMed:23658066). {ECO:0000269|PubMed:11402208, CC ECO:0000269|PubMed:12805629, ECO:0000269|PubMed:23658066}. CC -!- CATALYTIC ACTIVITY: CC Reaction=1D-myo-inositol 1,4,5-trisphosphate + H2O = 1D-myo-inositol CC 1,4-bisphosphate + phosphate; Xref=Rhea:RHEA:19797, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58282, CC ChEBI:CHEBI:203600; EC=3.1.3.56; CC Evidence={ECO:0000269|PubMed:11402208}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo- CC inositol 1,3,4-trisphosphate + phosphate; Xref=Rhea:RHEA:11392, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57895, CC ChEBI:CHEBI:58414; EC=3.1.3.56; CC Evidence={ECO:0000269|PubMed:11402208}; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=Q84MA2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q84MA2-2; Sequence=VSP_013848; CC -!- TISSUE SPECIFICITY: Expressed ubiquitously. CC {ECO:0000269|PubMed:11402208, ECO:0000269|PubMed:17237190}. CC -!- INDUCTION: Induced by ABA at both transcript and protein levels in a CC specific, transient manner. {ECO:0000269|PubMed:12805629}. CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Slightly reduced production CC of reactive oxygen species (ROS) (PubMed:23658066). Alterations in CC germination and in early seedling growth. Enhanced sensibility to CC abscisic acid (ABA) with elevated levels of Ins(1,4,5)P3 CC (PubMed:17237190). {ECO:0000269|PubMed:17237190, CC ECO:0000269|PubMed:23658066}. CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a donor acceptor splice site. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the inositol polyphosphate 5-phosphatase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF289633; AAG17824.1; -; mRNA. DR EMBL; AF117062; AAD10828.1; -; mRNA. DR EMBL; AC015446; AAG12525.1; -; Genomic_DNA. DR EMBL; CP002684; AEE31672.1; -; Genomic_DNA. DR EMBL; CP002684; AEE31674.1; -; Genomic_DNA. DR EMBL; BT006448; AAP21256.1; -; mRNA. DR EMBL; AK227368; BAE99376.1; -; mRNA. DR PIR; C86465; C86465. DR RefSeq; NP_564437.1; NM_103135.4. [Q84MA2-2] DR RefSeq; NP_849745.1; NM_179414.1. [Q84MA2-1] DR AlphaFoldDB; Q84MA2; -. DR SMR; Q84MA2; -. DR STRING; 3702.Q84MA2; -. DR iPTMnet; Q84MA2; -. DR PaxDb; 3702-AT1G34120-2; -. DR EnsemblPlants; AT1G34120.1; AT1G34120.1; AT1G34120. [Q84MA2-2] DR EnsemblPlants; AT1G34120.2; AT1G34120.2; AT1G34120. [Q84MA2-1] DR GeneID; 840311; -. DR Gramene; AT1G34120.1; AT1G34120.1; AT1G34120. [Q84MA2-2] DR Gramene; AT1G34120.2; AT1G34120.2; AT1G34120. [Q84MA2-1] DR KEGG; ath:AT1G34120; -. DR Araport; AT1G34120; -. DR TAIR; AT1G34120; IP5PI. DR eggNOG; KOG0565; Eukaryota. DR InParanoid; Q84MA2; -. DR OMA; KQLWPKT; -. DR OrthoDB; 21647at2759; -. DR PhylomeDB; Q84MA2; -. DR BioCyc; ARA:AT1G34120-MONOMER; -. DR BioCyc; MetaCyc:AT1G34120-MONOMER; -. DR BRENDA; 3.1.3.56; 399. DR PRO; PR:Q84MA2; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q84MA2; baseline and differential. DR GO; GO:0046030; F:inositol trisphosphate phosphatase activity; IDA:TAIR. DR GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IDA:TAIR. DR GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IDA:UniProtKB. DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IDA:UniProtKB. DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0032957; P:inositol trisphosphate metabolic process; IDA:TAIR. DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB. DR GO; GO:0009845; P:seed germination; IMP:UniProtKB. DR GO; GO:0090351; P:seedling development; IMP:UniProtKB. DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 2. DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf. DR InterPro; IPR045849; IP5P_plant. DR InterPro; IPR000300; IPPc. DR PANTHER; PTHR45666:SF30; TYPE I INOSITOL POLYPHOSPHATE 5-PHOSPHATASE 1; 1. DR PANTHER; PTHR45666; TYPE IV INOSITOL POLYPHOSPHATE 5-PHOSPHATASE 9; 1. DR SMART; SM00128; IPPc; 1. DR SUPFAM; SSF56219; DNase I-like; 1. DR Genevisible; Q84MA2; AT. PE 1: Evidence at protein level; KW Abscisic acid signaling pathway; Alternative splicing; Hydrolase; KW Phosphoprotein; Reference proteome. FT CHAIN 1..590 FT /note="Type I inositol polyphosphate 5-phosphatase 1" FT /id="PRO_0000209722" FT REGION 47..73 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 445..460 FT /note="Catalytic 1" FT /evidence="ECO:0000303|PubMed:11402208" FT REGION 523..538 FT /note="Catalytic 2" FT /evidence="ECO:0000303|PubMed:11402208" FT MOD_RES 60 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19245862, FT ECO:0007744|PubMed:19376835" FT VAR_SEQ 79..83 FT /note="GNVIY -> D (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11340187, FT ECO:0000303|PubMed:14593172, ECO:0000303|Ref.6" FT /id="VSP_013848" FT CONFLICT 21 FT /note="S -> L (in Ref. 1; AAG17824)" FT /evidence="ECO:0000305" FT CONFLICT 80 FT /note="N -> D (in Ref. 2; AAD10828)" FT /evidence="ECO:0000305" FT CONFLICT 239 FT /note="S -> G (in Ref. 2; AAD10828)" FT /evidence="ECO:0000305" FT CONFLICT 478 FT /note="E -> K (in Ref. 2; AAD10828)" FT /evidence="ECO:0000305" SQ SEQUENCE 590 AA; 67783 MW; 53C31A05D4C04428 CRC64; MAEVRSRSRR TESNWATICC SAFSCLQLYW ARIVLRKWFN VSASESDYSA DSDDDYEDRS QEFDPISSGV TNPRVDTDGN VIYRPKLRRR NSETFRMQYI DTKAIRICAG TWNVGGRVPS SDLDIDGWLD TLEPADIYVL GLQEIVPLNA GNIFGMEDDQ PALEWENLIR DALNRVQPRK LKIKSHSDPP SPSKFKQPEE VPYSVEDMFV ETSHDACDGI SSMDNKLNSV ESTDVPIVSE DSLTNIDVLG STNDNASCLP IQEYLQRQFS TPNTPDRSLS MQINSDSKRE ERFSYTERVG LSWPEPPLRL LNQYVSERRG SFKSVNLTIT NLRKPSYVRI VSKQMVGVFL TIWVRRNLRK HISNLCVSTV GVGIMGYIGN KGSVSVSMSI YQTPFCFLCT HLSSGEKDTD QEKRNDDVRE IHRRTQFLPH SLNANELPRS ICNHERIIWL GDLNYRINLS YEKTHELIAR KEWQRLVEYD QLSREMTKGN LFEGWSEGTL DFAPTYKYEI DSENYIGDDP ESGKRRPAWC DRIIWNGKGM KLFNYRRNEI KLSDHRPVTA TFLAEVEVLS PRKLQHALTL TYAEIQGLDA //