IP5P7_ARATH
ID IP5P7_ARATH Reviewed; 594 AA.
AC Q0WQ41; Q712G2; Q9SKZ8;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Type IV inositol polyphosphate 5-phosphatase 7 {ECO:0000303|PubMed:21677096};
DE Short=At5PTase7 {ECO:0000303|PubMed:21677096};
DE EC=3.1.3.36 {ECO:0000269|PubMed:19473324, ECO:0000269|PubMed:21677096, ECO:0000269|PubMed:23658066};
DE EC=3.1.3.86 {ECO:0000269|PubMed:19473324, ECO:0000269|PubMed:21677096, ECO:0000269|PubMed:23658066};
DE AltName: Full=Protein CVP2 LIKE 1 {ECO:0000303|PubMed:19473324};
DE Short=Protein CVL1 {ECO:0000303|PubMed:19473324};
GN Name=IP5P7 {ECO:0000305};
GN Synonyms=CVL1 {ECO:0000303|PubMed:19473324},
GN IPP4 {ECO:0000312|EMBL:CAC81920.1};
GN OrderedLocusNames=At2g32010 {ECO:0000312|Araport:AT2G32010};
GN ORFNames=F22D22.24 {ECO:0000312|EMBL:AAD15403.1};
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;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-594.
RC STRAIN=cv. Columbia; TISSUE=Hypocotyl {ECO:0000312|EMBL:CAC81920.1};
RA Lin W.H., Xu Z.H., Mueller-Roeber B., Xue H.W.;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=19363154; DOI=10.1242/dev.030098;
RA Naramoto S., Sawa S., Koizumi K., Uemura T., Ueda T., Friml J., Nakano A.,
RA Fukuda H.;
RT "Phosphoinositide-dependent regulation of VAN3 ARF-GAP localization and
RT activity essential for vascular tissue continuity in plants.";
RL Development 136:1529-1538(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND CATALYTIC ACTIVITY.
RX PubMed=19473324; DOI=10.1111/j.1365-313x.2009.03920.x;
RA Carland F., Nelson T.;
RT "CVP2- and CVL1-mediated phosphoinositide signaling as a regulator of the
RT ARF GAP SFC/VAN3 in establishment of foliar vein patterns.";
RL Plant J. 59:895-907(2009).
RN [8]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=21677096; DOI=10.1104/pp.111.176883;
RA Kaye Y., Golani Y., Singer Y., Leshem Y., Cohen G., Ercetin M.,
RA Gillaspy G., Levine A.;
RT "Inositol polyphosphate 5-phosphatase7 regulates the production of reactive
RT oxygen species and salt tolerance in Arabidopsis.";
RL Plant Physiol. 157:229-241(2011).
RN [9]
RP 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).
RN [10]
RP FUNCTION.
RX PubMed=25813544; DOI=10.1242/dev.118364;
RA Rodriguez-Villalon A., Gujas B., van Wijk R., Munnik T., Hardtke C.S.;
RT "Primary root protophloem differentiation requires balanced
RT phosphatidylinositol-4,5-biphosphate levels and systemically affects root
RT branching.";
RL Development 142:1437-1446(2015).
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
CC (PubMed:19473324, PubMed:21677096, PubMed:23658066). Acts redundantly
CC with CVP2 for maintaining vascular continuity (PubMed:19363154,
CC PubMed:25813544). Regulates phosphoinositide-dependent VAN3
CC localization (PubMed:19473324). Functions in salt stress response by
CC regulating reactive oxygen species (ROS) production and stress-
CC responsive genes expression (PubMed:21677096).
CC {ECO:0000269|PubMed:19363154, ECO:0000269|PubMed:19473324,
CC ECO:0000269|PubMed:21677096, ECO:0000269|PubMed:23658066,
CC ECO:0000269|PubMed:25813544}.
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:19473324, ECO:0000269|PubMed:21677096,
CC 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:19473324, ECO:0000269|PubMed:21677096,
CC ECO:0000269|PubMed:23658066};
CC -!- SUBCELLULAR LOCATION: Nucleus. Cell membrane; Peripheral membrane
CC protein {ECO:0000269|PubMed:21677096}.
CC -!- TISSUE SPECIFICITY: Broadly expressed in emerging organs. Mostly
CC localized in procambium of growing organs. Restricted to vascular
CC differentiating cells of young organs. {ECO:0000269|PubMed:19473324}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing veins of late torpedo,
CC walking stick and bent cotyledon stage embryos.
CC {ECO:0000269|PubMed:19473324}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:19473324). Increased
CC salt sensitivity with reduced production of reactive oxygen species
CC (ROS) (PubMed:21677096). {ECO:0000269|PubMed:19473324,
CC ECO:0000269|PubMed:21677096}.
CC -!- MISCELLANEOUS: Cvp1 and cvp2 double mutant displays high PtdIns(4,5)P2
CC levels. {ECO:0000269|PubMed:25813544}.
CC -!- SIMILARITY: Belongs to the inositol polyphosphate 5-phosphatase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD15403.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAC81920.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC006223; AAD15403.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08621.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08622.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62725.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62726.1; -; Genomic_DNA.
DR EMBL; AK228865; BAF00758.1; -; mRNA.
DR EMBL; AJ277885; CAC81920.1; ALT_FRAME; mRNA.
DR PIR; H84727; H84727.
DR RefSeq; NP_001189654.1; NM_001202725.1.
DR RefSeq; NP_001324864.1; NM_001336367.1.
DR RefSeq; NP_001324865.1; NM_001336366.1.
DR RefSeq; NP_180761.2; NM_128761.4.
DR AlphaFoldDB; Q0WQ41; -.
DR SMR; Q0WQ41; -.
DR STRING; 3702.AT2G32010.1; -.
DR PaxDb; Q0WQ41; -.
DR PRIDE; Q0WQ41; -.
DR EnsemblPlants; AT2G32010.1; AT2G32010.1; AT2G32010.
DR EnsemblPlants; AT2G32010.2; AT2G32010.2; AT2G32010.
DR EnsemblPlants; AT2G32010.3; AT2G32010.3; AT2G32010.
DR EnsemblPlants; AT2G32010.4; AT2G32010.4; AT2G32010.
DR GeneID; 817761; -.
DR Gramene; AT2G32010.1; AT2G32010.1; AT2G32010.
DR Gramene; AT2G32010.2; AT2G32010.2; AT2G32010.
DR Gramene; AT2G32010.3; AT2G32010.3; AT2G32010.
DR Gramene; AT2G32010.4; AT2G32010.4; AT2G32010.
DR KEGG; ath:AT2G32010; -.
DR Araport; AT2G32010; -.
DR TAIR; locus:2045502; AT2G32010.
DR eggNOG; KOG0565; Eukaryota.
DR HOGENOM; CLU_011711_4_0_1; -.
DR InParanoid; Q0WQ41; -.
DR OMA; MPRNSRY; -.
DR OrthoDB; 1399831at2759; -.
DR PhylomeDB; Q0WQ41; -.
DR PRO; PR:Q0WQ41; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q0WQ41; baseline and differential.
DR Genevisible; Q0WQ41; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IEA:InterPro.
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:UniProtKB.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR GO; GO:0010305; P:leaf vascular tissue pattern formation; IGI:TAIR.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; 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; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Hydrolase; Membrane; Nucleus; Reference proteome.
FT CHAIN 1..594
FT /note="Type IV inositol polyphosphate 5-phosphatase 7"
FT /id="PRO_0000433257"
FT REGION 246..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..450
FT /note="Catalytic 1"
FT /evidence="ECO:0000250|UniProtKB:Q84MA2"
FT REGION 515..530
FT /note="Catalytic 2"
FT /evidence="ECO:0000250|UniProtKB:Q84MA2"
FT COMPBIAS 246..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 568
FT /note="T -> I (in Ref. 4; CAC81920)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 594 AA; 68245 MW; B9BBC2A961CCECAF CRC64;
MRDDKTKKSK LSWSKKMVRK WFNIKSKTEK FQADVSLPQG VEVEHRNSFS EREPCTIKKS
KTEKLNKNWE QQARQRKMNY ENPRIIDVQN HSIFVATWNV AGRSPPEDLN LDEWLHSSAP
ADIYVLGFQE IVPLNAGNVL GAEDNGPAKK WHSLIRKTLN NLPGASSACH TPSPIPVPIA
EIDADFSGSS RQKNETFFNR RSFQTPSVWS MEENDPSISQ PRLDRRFSVC DRVFFSHRPS
DFDPSFRCGH RPSDYSRRPS DYSRPSDYYS RPSNYSRPSD VSRWGSSDDD NGPGDSPSTF
LNSPGSFLGS AANENGYRTP WNSSQYCLVA SKQMVGIFLT IWVKSELREH VKNMKVSCVG
RGLMGYLGNK GSISISMLLH QTSFCFVCTH LTSGQKEGDE LRRNSDVMEI LKKTRFPRVQ
SSADEKSPEN ILQHDRVIWL GDLNYRIALS YRSAKALVEM QNWRALLEND QLRIEQKRGH
VFKGWNEGKI YFPPTYKYSN NSDRYAGGDL HPKEKRRTPA WCDRILWHGE GLHQLSYVRG
ESRFSDHRPV YGIFSAEVES NHKRSKRTNS HSTARVEAEE LLPYARGYTE LTFF
