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Type I inositol polyphosphate 5-phosphatase 1 (At5PTase1) (EC 3.1.3.56)

 IP5P1_ARATH             Reviewed;         590 AA.
Q84MA2; Q0WU22; Q9FUR3; Q9FX20; Q9ZSC4;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 2.
10-OCT-2018, entry version 113.
RecName: Full=Type I inositol polyphosphate 5-phosphatase 1 {ECO:0000303|PubMed:11402208};
Short=At5PTase1 {ECO:0000303|PubMed:11402208};
EC=3.1.3.56 {ECO:0000269|PubMed:11402208};
Name=IP5P1 {ECO:0000303|PubMed:11340187};
Synonyms=5P1 {ECO:0000303|Ref.2};
OrderedLocusNames=At1g34120 {ECO:0000312|Araport:AT1G34120};
ORFNames=F12G12.6 {ECO:0000312|EMBL:AAG12525.1};
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 2).
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 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.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[4]
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[7]
GENE FAMILY, FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
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).
[8]
FUNCTION, AND INDUCTION.
PubMed=12805629; DOI=10.1104/pp.019000;
Burnette R.N., Gunesekera B.M., Gillaspy G.E.;
"An Arabidopsis inositol 5-phosphatase gain-of-function alters
abscisic acid signaling.";
Plant Physiol. 132:1011-1019(2003).
[9]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND 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).
[12]
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, but not toward Ins(1,4)P2, Ins(1)P
(PubMed:11402208). Seems to be involved in the abscisic acid (ABA)
signaling pathway (PubMed:12805629). Could also be able to
hydrolyze PtdIns(4,5)P2 and PtdIns(3,4,5)P3 (PubMed:23658066).
{ECO:0000269|PubMed:11402208, ECO:0000269|PubMed:12805629,
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:11402208}.
-!- CATALYTIC ACTIVITY: 1D-myo-inositol 1,3,4,5-tetrakisphosphate +
H(2)O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate.
{ECO:0000269|PubMed:11402208}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q84MA2-1; Sequence=Displayed;
Name=2;
IsoId=Q84MA2-2; Sequence=VSP_013848;
Note=May be due to a donor acceptor splice site.;
-!- TISSUE SPECIFICITY: Expressed ubiquitously.
{ECO:0000269|PubMed:11402208, ECO:0000269|PubMed:17237190}.
-!- INDUCTION: Induced by ABA at both transcript and protein levels in
a specific, transient manner. {ECO:0000269|PubMed:12805629}.
-!- DISRUPTION PHENOTYPE: No visible phenotype. Slightly reduced
production of reactive oxygen species (ROS) (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}.
-----------------------------------------------------------------------
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EMBL; AF289633; AAG17824.1; -; mRNA.
EMBL; AF117062; AAD10828.1; -; mRNA.
EMBL; AC015446; AAG12525.1; -; Genomic_DNA.
EMBL; CP002684; AEE31672.1; -; Genomic_DNA.
EMBL; CP002684; AEE31674.1; -; Genomic_DNA.
EMBL; BT006448; AAP21256.1; -; mRNA.
EMBL; AK227368; BAE99376.1; -; mRNA.
PIR; C86465; C86465.
RefSeq; NP_564437.1; NM_103135.4. [Q84MA2-2]
RefSeq; NP_849745.1; NM_179414.1. [Q84MA2-1]
UniGene; At.10999; -.
UniGene; At.73182; -.
ProteinModelPortal; Q84MA2; -.
STRING; 3702.AT1G34120.2; -.
iPTMnet; Q84MA2; -.
PaxDb; Q84MA2; -.
PRIDE; Q84MA2; -.
EnsemblPlants; AT1G34120.1; AT1G34120.1; AT1G34120. [Q84MA2-2]
EnsemblPlants; AT1G34120.2; AT1G34120.2; AT1G34120. [Q84MA2-1]
GeneID; 840311; -.
Gramene; AT1G34120.1; AT1G34120.1; AT1G34120. [Q84MA2-2]
Gramene; AT1G34120.2; AT1G34120.2; AT1G34120. [Q84MA2-1]
KEGG; ath:AT1G34120; -.
Araport; AT1G34120; -.
TAIR; locus:2009061; AT1G34120.
eggNOG; KOG0565; Eukaryota.
eggNOG; COG5411; LUCA.
HOGENOM; HOG000241161; -.
InParanoid; Q84MA2; -.
OMA; RDERFSY; -.
OrthoDB; EOG093605LL; -.
PhylomeDB; Q84MA2; -.
BioCyc; ARA:AT1G34120-MONOMER; -.
BioCyc; MetaCyc:AT1G34120-MONOMER; -.
BRENDA; 3.1.3.56; 399.
PRO; PR:Q84MA2; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q84MA2; baseline and differential.
Genevisible; Q84MA2; AT.
GO; GO:0046030; F:inositol trisphosphate phosphatase activity; IDA:TAIR.
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; IDA:TAIR.
GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB.
GO; GO:0009845; P:seed germination; IMP:UniProtKB.
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; 2.
1: Evidence at protein level;
Abscisic acid signaling pathway; Alternative splicing;
Complete proteome; Hydrolase; Phosphoprotein; Reference proteome.
CHAIN 1 590 Type I inositol polyphosphate 5-
phosphatase 1.
/FTId=PRO_0000209722.
REGION 445 460 Catalytic 1.
{ECO:0000303|PubMed:11402208}.
REGION 523 538 Catalytic 2.
{ECO:0000303|PubMed:11402208}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000244|PubMed:19245862,
ECO:0000244|PubMed:19376835}.
VAR_SEQ 79 83 GNVIY -> D (in isoform 2).
{ECO:0000303|PubMed:11340187,
ECO:0000303|PubMed:14593172,
ECO:0000303|Ref.6}.
/FTId=VSP_013848.
CONFLICT 21 21 S -> L (in Ref. 1; AAG17824).
{ECO:0000305}.
CONFLICT 80 80 N -> D (in Ref. 2; AAD10828).
{ECO:0000305}.
CONFLICT 239 239 S -> G (in Ref. 2; AAD10828).
{ECO:0000305}.
CONFLICT 478 478 E -> K (in Ref. 2; AAD10828).
{ECO:0000305}.
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


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