IP5P2_ARATH
ID IP5P2_ARATH Reviewed; 646 AA.
AC Q9FUR2; O49700; Q9SNF1; Q9ZSC3;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Type I inositol polyphosphate 5-phosphatase 2 {ECO:0000303|PubMed:11402208};
DE Short=At5PTase2 {ECO:0000303|PubMed:11402208};
DE EC=3.1.3.56 {ECO:0000269|PubMed:11340187};
GN Name=IP5P2 {ECO:0000303|PubMed:11340187}; Synonyms=5P2 {ECO:0000303|Ref.3};
GN OrderedLocusNames=At4g18010 {ECO:0000312|Araport:AT4G18010};
GN ORFNames=T6K21.190 {ECO:0000312|EMBL:CAA17144.1};
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 1), FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=11340187; DOI=10.2307/3871369;
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 2).
RC TISSUE=Hypocotyl;
RA Xue H., Mueller-Roeber B.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [5]
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 [6]
RP GENE FAMILY.
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 [7]
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 [8]
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 [9]
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. Seems to be involved in the abscisic acid (ABA)
CC signaling pathway (PubMed:11340187). Could also be able to hydrolyze
CC PtdIns(4,5)P2 and PtdIns(3,4,5)P3 (PubMed:23658066).
CC {ECO:0000269|PubMed:11340187, 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:11340187};
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:11340187};
CC -!- INTERACTION:
CC Q9FUR2; Q9ZVY7: OBAP1A; NbExp=4; IntAct=EBI-25510894, EBI-4425342;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FUR2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FUR2-2; Sequence=VSP_013849;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC {ECO:0000269|PubMed:17237190}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:23658066).
CC Alterations in germination and in early seedling growth. Enhanced
CC sensibility to 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 -!- SIMILARITY: Belongs to the inositol polyphosphate 5-phosphatase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA17144.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78803.1; Type=Erroneous gene model prediction; Evidence={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; AF289634; AAG17825.1; -; mRNA.
DR EMBL; AJ002295; CAB59428.1; -; mRNA.
DR EMBL; AF117063; AAD10829.1; -; mRNA.
DR EMBL; AL021889; CAA17144.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161547; CAB78803.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83979.1; -; Genomic_DNA.
DR PIR; T05087; T05087.
DR PIR; T51937; T51937.
DR PIR; T51938; T51938.
DR RefSeq; NP_567547.1; NM_117911.4. [Q9FUR2-1]
DR AlphaFoldDB; Q9FUR2; -.
DR SMR; Q9FUR2; -.
DR BioGRID; 12819; 2.
DR IntAct; Q9FUR2; 1.
DR STRING; 3702.AT4G18010.1; -.
DR iPTMnet; Q9FUR2; -.
DR PaxDb; Q9FUR2; -.
DR PRIDE; Q9FUR2; -.
DR ProteomicsDB; 232225; -. [Q9FUR2-1]
DR EnsemblPlants; AT4G18010.1; AT4G18010.1; AT4G18010. [Q9FUR2-1]
DR GeneID; 827526; -.
DR Gramene; AT4G18010.1; AT4G18010.1; AT4G18010. [Q9FUR2-1]
DR KEGG; ath:AT4G18010; -.
DR Araport; AT4G18010; -.
DR TAIR; locus:2141095; AT4G18010.
DR eggNOG; KOG0565; Eukaryota.
DR InParanoid; Q9FUR2; -.
DR OrthoDB; 1399831at2759; -.
DR PhylomeDB; Q9FUR2; -.
DR BioCyc; ARA:AT4G18010-MON; -.
DR BRENDA; 3.1.3.56; 399.
DR PRO; PR:Q9FUR2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9FUR2; baseline and differential.
DR Genevisible; Q9FUR2; AT.
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:0046855; P:inositol phosphate dephosphorylation; IDA:TAIR.
DR GO; GO:0032957; P:inositol trisphosphate metabolic process; IMP:UniProtKB.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR GO; GO:0090351; P:seedling development; IMP:UniProtKB.
DR Gene3D; 3.60.10.10; -; 2.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR045849; IP5P_plant.
DR InterPro; IPR000300; IPPc.
DR PANTHER; PTHR45666; PTHR45666; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing; Hydrolase;
KW Reference proteome.
FT CHAIN 1..646
FT /note="Type I inositol polyphosphate 5-phosphatase 2"
FT /id="PRO_0000209723"
FT REGION 59..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..510
FT /note="Catalytic 1"
FT /evidence="ECO:0000250|UniProtKB:Q84MA2"
FT REGION 575..590
FT /note="Catalytic 2"
FT /evidence="ECO:0000250|UniProtKB:Q84MA2"
FT COMPBIAS 59..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 327..359
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_013849"
FT CONFLICT 72
FT /note="A -> R (in Ref. 2; CAB59428)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="L -> F (in Ref. 3; AAD10829)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="P -> G (in Ref. 1; AAG17825, 2; CAB59428 and 3;
FT AAD10829)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 646 AA; 73579 MW; FD7D59676B9862BE CRC64;
MKTRRGKRPE RFWPSIVMNK WLNRKPKVYD FSEDEIDTEP ESEDDVCSVK DVPNVHCVTD
EDSHNGRRGS EADHGNNISD GGVSVRGGYQ RKHRRGKSET LRAQYINTKD IKVTVATWNV
AGKRPSDDLE IEDWLSTDNP SDIYIIGFQE VVPLNAGNVF GAEDRGPIPK WESIIRRTLN
KSNKESVYDQ SPSCNNNALH RSHSAPSSPI LAQEANSIIS HVMVENLVAD HSLDLATNEF
IDAATALPSL EPQRNPNMDW PELALDSNPQ IVGSEGKLRR VFSSNATLGF KLPENPSGAS
RFASEARQLK RSRSFETLNL SWNDIKEEID NRSSSSSEAE EAAKIMHDDS SDGDSSSQDE
EDGDKIRNSY GLPEDLVEEC RKVKDSQKYV RIVSKQMVGI YVSVWIRRRL RRHVNNLKVS
PVGVGLMGYM GNKGSVSISM TLYQSRMCFV CSHLTSGHKD GAEQRRNADV YEIIRRTRFA
SVLDTDQPRT IPCHDQVFWF GDLNYRLNMS DGEVRKLVSQ KRWDELKNSD QLIRELRRGH
VFDGWREGPI KFPPTYKYEF DSDRYAGENL REPEKKRAPA WCDRILWLGK GIRQECYKRS
EIRMSDHRPV TSIFNVGVEV FDHRKLQRAL HVNNAAASAV HPEPSF
