IP5P9_ARATH
ID IP5P9_ARATH Reviewed; 417 AA.
AC Q9SIS4;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Type IV inositol polyphosphate 5-phosphatase 9 {ECO:0000303|PubMed:23658066};
DE Short=At5PTase9 {ECO:0000303|PubMed:23658066};
DE EC=3.1.3.36 {ECO:0000269|PubMed:23658066};
DE EC=3.1.3.86 {ECO:0000269|PubMed:23658066};
GN Name=IP5P9 {ECO:0000305};
GN OrderedLocusNames=At2g01900 {ECO:0000312|Araport:AT2G01900};
GN ORFNames=T23K3.9 {ECO:0000312|EMBL:AAD21781.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
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 [5]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, 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 PtdIns(4,5)P2 and at a lower
CC extent toward PtdIns(3,4,5)P3 but not toward Ins(1,4,5)P3. Functions in
CC salt stress response by regulating reactive oxygen species (ROS)
CC production, endocytosis, Ca(2+) influx and stress-responsive genes
CC expression. {ECO:0000269|PubMed:23658066}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456; EC=3.1.3.36;
CC Evidence={ECO:0000269|PubMed:23658066};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-
CC trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:25528,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:57836; EC=3.1.3.86;
CC Evidence={ECO:0000269|PubMed:23658066};
CC -!- TISSUE SPECIFICITY: Specifically expressed in roots.
CC {ECO:0000269|PubMed:23658066}.
CC -!- DISRUPTION PHENOTYPE: Increased salt sensitivity with reduced
CC production of reactive oxygen species (ROS), reduced Ca(2+) influx, as
CC well as decreased fluid-phase endocytosis.
CC {ECO:0000269|PubMed:23658066}.
CC -!- SIMILARITY: Belongs to the inositol polyphosphate 5-phosphatase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX818920; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AC007069; AAD21781.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05514.1; -; Genomic_DNA.
DR EMBL; BX818920; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; E84430; E84430.
DR RefSeq; NP_178299.1; NM_126251.3.
DR AlphaFoldDB; Q9SIS4; -.
DR SMR; Q9SIS4; -.
DR STRING; 3702.AT2G01900.1; -.
DR PaxDb; Q9SIS4; -.
DR PRIDE; Q9SIS4; -.
DR EnsemblPlants; AT2G01900.1; AT2G01900.1; AT2G01900.
DR GeneID; 814721; -.
DR Gramene; AT2G01900.1; AT2G01900.1; AT2G01900.
DR KEGG; ath:AT2G01900; -.
DR Araport; AT2G01900; -.
DR TAIR; locus:2059708; AT2G01900.
DR eggNOG; KOG0565; Eukaryota.
DR HOGENOM; CLU_011711_1_0_1; -.
DR InParanoid; Q9SIS4; -.
DR OMA; VACCHLA; -.
DR PhylomeDB; Q9SIS4; -.
DR PRO; PR:Q9SIS4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIS4; baseline and differential.
DR Genevisible; Q9SIS4; AT.
DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IEA:InterPro.
DR GO; GO:0034595; F:phosphatidylinositol phosphate 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:0071472; P:cellular response to salt stress; IMP:TAIR.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; IMP:TAIR.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:UniProtKB.
DR Gene3D; 3.60.10.10; -; 1.
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 Hydrolase; Reference proteome.
FT CHAIN 1..417
FT /note="Type IV inositol polyphosphate 5-phosphatase 9"
FT /id="PRO_0000433259"
FT REGION 258..273
FT /note="Catalytic 1"
FT /evidence="ECO:0000250|UniProtKB:Q84MA2"
FT REGION 339..354
FT /note="Catalytic 2"
FT /evidence="ECO:0000250|UniProtKB:Q84MA2"
SQ SEQUENCE 417 AA; 47924 MW; 13A4527DEC6A6B7B CRC64;
MWPRLVANKI LRKSLGSNNF VADFPPNTDQ KLIEASGLAD ERSKSILHNQ HKTTLLNYKV
FVSTWNVGGI VPDDGLDMED LLETHKTPCD IYVLGFQEVV PLRASNVLGS DNNKVSTKWN
SLIRDALNKR ARPHRDEDLS ESKGINGISQ DFRCIISKQM VGILITVWVR GDLWPYIRYP
SVSCVGCGIM GCLGNKGSVS VRFQLHETTF CFVCSHLASG GRDRDERQRN SDVNEILARS
SFPRGSSLDL PKKILDHDRV IFLGDLNYRI SLPEEKTRLL VESKKWNILL ENDQLRMEIM
NGQIFRGWQE GIVKFAPTYK YVPNSDLYYG CITYKKDEKK RAPAWCDRII WYGNGLKQHE
YTRGETKISD HRPVKAIFTT EITVTRRGKK IRNFFFSDRF EERIGDIDSK DYSWIST
