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Type I inositol polyphosphate 5-phosphatase 2 (At5PTase2) (EC 3.1.3.56)

 IP5P2_ARATH             Reviewed;         646 AA.
Q9FUR2; O49700; Q9SNF1; Q9ZSC3;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 2.
07-NOV-2018, entry version 116.
RecName: Full=Type I inositol polyphosphate 5-phosphatase 2 {ECO:0000303|PubMed:11402208};
Short=At5PTase2 {ECO:0000303|PubMed:11402208};
EC=3.1.3.56 {ECO:0000269|PubMed:11340187};
Name=IP5P2 {ECO:0000303|PubMed:11340187};
Synonyms=5P2 {ECO:0000303|Ref.3};
OrderedLocusNames=At4g18010 {ECO:0000312|Araport:AT4G18010};
ORFNames=T6K21.190 {ECO:0000312|EMBL:CAA17144.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CATALYTIC
ACTIVITY.
STRAIN=cv. Landsberg erecta;
PubMed=11340187; DOI=10.1105/tpc.13.5.1143;
Sanchez J.-P., Chua N.-H.;
"Arabidopsis PLC1 is required for secondary responses to abscisic acid
signals.";
Plant Cell 13:1143-1154(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Hypocotyl;
Xue H., Mueller-Roeber B.;
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
Parzer M.S.A., de Vos S., van Lookeren Campagne M.M.;
"Characterization of putative inositol (1,4,5)-
trisphosphate/phosphatidylinositol (4,5)-bisphosphate 5-phosphatase
cDNAs from Arabidopsis thaliana.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[6]
GENE FAMILY.
PubMed=11402208; DOI=10.1104/pp.126.2.801;
Berdy S.E., Kudla J., Gruissem W., Gillaspy G.E.;
"Molecular characterization of At5PTase1, an inositol phosphatase
capable of terminating inositol trisphosphate signaling.";
Plant Physiol. 126:801-810(2001).
[7]
DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=17237190; DOI=10.1104/pp.106.089474;
Gunesekera B., Torabinejad J., Robinson J., Gillaspy G.E.;
"Inositol polyphosphate 5-phosphatases 1 and 2 are required for
regulating seedling growth.";
Plant Physiol. 143:1408-1417(2007).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[9]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=23658066; DOI=10.1093/mp/sst072;
Golani Y., Kaye Y., Gilhar O., Ercetin M., Gillaspy G., Levine A.;
"Inositol polyphosphate phosphatidylinositol 5-phosphatase9
(At5ptase9) controls plant salt tolerance by regulating endocytosis.";
Mol. Plant 6:1781-1794(2013).
-!- FUNCTION: Has phosphatase activity toward Ins(1,4,5)P3 and
Ins(1,3,4,5)P4. Seems to be involved in the abscisic acid (ABA)
signaling pathway (PubMed:11340187). Could also be able to
hydrolyze PtdIns(4,5)P2 and PtdIns(3,4,5)P3 (PubMed:23658066).
{ECO:0000269|PubMed:11340187, ECO:0000269|PubMed:23658066}.
-!- CATALYTIC ACTIVITY: D-myo-inositol 1,4,5-trisphosphate + H(2)O =
myo-inositol 1,4-bisphosphate + phosphate.
{ECO:0000269|PubMed:11340187}.
-!- CATALYTIC ACTIVITY: 1D-myo-inositol 1,3,4,5-tetrakisphosphate +
H(2)O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate.
{ECO:0000269|PubMed:11340187}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9FUR2-1; Sequence=Displayed;
Name=2;
IsoId=Q9FUR2-2; Sequence=VSP_013849;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed ubiquitously.
{ECO:0000269|PubMed:17237190}.
-!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:23658066).
Alterations in germination and in early seedling growth. Enhanced
sensibility to abscisic acid (ABA) with elevated levels of
Ins(1,4,5)P3 (PubMed:17237190). {ECO:0000269|PubMed:17237190,
ECO:0000269|PubMed:23658066}.
-!- SIMILARITY: Belongs to the inositol polyphosphate 5-phosphatase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA17144.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB78803.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF289634; AAG17825.1; -; mRNA.
EMBL; AJ002295; CAB59428.1; -; mRNA.
EMBL; AF117063; AAD10829.1; -; mRNA.
EMBL; AL021889; CAA17144.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161547; CAB78803.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; AEE83979.1; -; Genomic_DNA.
PIR; T05087; T05087.
PIR; T51937; T51937.
PIR; T51938; T51938.
RefSeq; NP_567547.1; NM_117911.4. [Q9FUR2-1]
UniGene; At.2057; -.
ProteinModelPortal; Q9FUR2; -.
BioGrid; 12819; 1.
STRING; 3702.AT4G18010.1; -.
iPTMnet; Q9FUR2; -.
PaxDb; Q9FUR2; -.
PRIDE; Q9FUR2; -.
EnsemblPlants; AT4G18010.1; AT4G18010.1; AT4G18010. [Q9FUR2-1]
GeneID; 827526; -.
Gramene; AT4G18010.1; AT4G18010.1; AT4G18010. [Q9FUR2-1]
KEGG; ath:AT4G18010; -.
Araport; AT4G18010; -.
TAIR; locus:2141095; AT4G18010.
eggNOG; KOG0565; Eukaryota.
eggNOG; COG5411; LUCA.
HOGENOM; HOG000241161; -.
InParanoid; Q9FUR2; -.
OrthoDB; EOG093609I2; -.
PhylomeDB; Q9FUR2; -.
BioCyc; ARA:AT4G18010-MONOMER; -.
BRENDA; 3.1.3.56; 399.
PRO; PR:Q9FUR2; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q9FUR2; baseline and differential.
Genevisible; Q9FUR2; AT.
GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IDA:TAIR.
GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IDA:UniProtKB.
GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IDA:UniProtKB.
GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:TAIR.
GO; GO:0032957; P:inositol trisphosphate metabolic process; IMP:UniProtKB.
GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB.
GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
GO; GO:0009845; P:seed germination; IMP:TAIR.
GO; GO:0090351; P:seedling development; IMP:UniProtKB.
Gene3D; 3.60.10.10; -; 2.
InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
InterPro; IPR005135; Endo/exonuclease/phosphatase.
InterPro; IPR000300; IPPc.
Pfam; PF03372; Exo_endo_phos; 1.
SMART; SM00128; IPPc; 1.
SUPFAM; SSF56219; SSF56219; 1.
1: Evidence at protein level;
Abscisic acid signaling pathway; Alternative splicing;
Complete proteome; Hydrolase; Reference proteome.
CHAIN 1 646 Type I inositol polyphosphate 5-
phosphatase 2.
/FTId=PRO_0000209723.
REGION 495 510 Catalytic 1.
{ECO:0000250|UniProtKB:Q84MA2}.
REGION 575 590 Catalytic 2.
{ECO:0000250|UniProtKB:Q84MA2}.
COMPBIAS 333 337 Poly-Ser.
VAR_SEQ 327 359 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_013849.
CONFLICT 72 72 A -> R (in Ref. 2; CAB59428).
{ECO:0000305}.
CONFLICT 483 483 L -> F (in Ref. 3; AAD10829).
{ECO:0000305}.
CONFLICT 573 573 P -> G (in Ref. 1; AAG17825, 2; CAB59428
and 3; AAD10829). {ECO:0000305}.
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


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