IP5P1_ARATH
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 03-AUG-2022, entry version 130.
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}; 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=10.2307/3871369;
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 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}.
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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.AT1G34120.2; -.
DR iPTMnet; Q84MA2; -.
DR PaxDb; Q84MA2; -.
DR PRIDE; Q84MA2; -.
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; locus:2009061; AT1G34120.
DR eggNOG; KOG0565; Eukaryota.
DR InParanoid; Q84MA2; -.
DR OrthoDB; 1399831at2759; -.
DR PhylomeDB; Q84MA2; -.
DR BioCyc; ARA:AT1G34120-MON; -.
DR BioCyc; MetaCyc:AT1G34120-MON; -.
DR BRENDA; 3.1.3.56; 399.
DR PRO; PR:Q84MA2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84MA2; baseline and differential.
DR Genevisible; Q84MA2; AT.
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:0046855; P:inositol phosphate dephosphorylation; IDA:TAIR.
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; -; 2.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR045849; IP5P_plant.
DR InterPro; IPR000300; IPPc.
DR PANTHER; PTHR45666; PTHR45666; 1.
DR Pfam; PF03372; Exo_endo_phos; 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 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
