IP5PE_ARATH
ID IP5PE_ARATH Reviewed; 1144 AA.
AC Q9SKB7;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Type II inositol polyphosphate 5-phosphatase 14 {ECO:0000303|PubMed:15574849};
DE Short=At5PTase14 {ECO:0000303|PubMed:15574849};
DE EC=3.1.3.36 {ECO:0000269|PubMed:15574849};
DE EC=3.1.3.86 {ECO:0000269|PubMed:15574849};
GN Name=IP5P14 {ECO:0000305}; Synonyms=5PTASE14;
GN OrderedLocusNames=At2g31830 {ECO:0000312|Araport:AT2G31830};
GN ORFNames=F20M17.13 {ECO:0000312|EMBL:AAD32289.1};
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 [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY,
RP INDUCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=15574849; DOI=10.1093/pcp/pch187;
RA Zhong R., Ye Z.-H.;
RT "Molecular and biochemical characterization of three WD-repeat-domain-
RT containing inositol polyphosphate 5-phosphatases in Arabidopsis thaliana.";
RL Plant Cell Physiol. 45:1720-1728(2004).
RN [2]
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 [3]
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 [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).
CC -!- FUNCTION: Has phosphatase activity toward PtdIns(4,5)P2,
CC PtdIns(3,4,5)P3 and Ins(1,4,5)P3. {ECO:0000269|PubMed:15574849}.
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:15574849};
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:15574849};
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; Evidence={ECO:0000269|PubMed:15574849};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15574849};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=101 uM for PtdIns(4,5) {ECO:0000269|PubMed:15574849};
CC KM=211 uM for PtdIns(3,4,5)P3 {ECO:0000269|PubMed:15574849};
CC KM=395 uM for Ins(1,4,5)P3 {ECO:0000269|PubMed:15574849};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SKB7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in young seedlings and flowers.
CC {ECO:0000269|PubMed:15574849}.
CC -!- INDUCTION: Slightly reduced by dark treatment.
CC {ECO:0000269|PubMed:15574849}.
CC -!- SIMILARITY: Belongs to the inositol polyphosphate 5-phosphatase family.
CC {ECO:0000305}.
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DR EMBL; AY761189; AAV87316.1; -; mRNA.
DR EMBL; AY761193; AAV87320.1; -; Genomic_DNA.
DR EMBL; AC006533; AAD32289.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08590.1; -; Genomic_DNA.
DR PIR; F84725; F84725.
DR RefSeq; NP_180742.1; NM_128741.3. [Q9SKB7-1]
DR AlphaFoldDB; Q9SKB7; -.
DR SMR; Q9SKB7; -.
DR STRING; 3702.AT2G31830.2; -.
DR iPTMnet; Q9SKB7; -.
DR PaxDb; Q9SKB7; -.
DR PRIDE; Q9SKB7; -.
DR ProteomicsDB; 238946; -. [Q9SKB7-1]
DR EnsemblPlants; AT2G31830.1; AT2G31830.1; AT2G31830. [Q9SKB7-1]
DR GeneID; 817740; -.
DR Gramene; AT2G31830.1; AT2G31830.1; AT2G31830. [Q9SKB7-1]
DR KEGG; ath:AT2G31830; -.
DR Araport; AT2G31830; -.
DR eggNOG; KOG0565; Eukaryota.
DR HOGENOM; CLU_004721_0_1_1; -.
DR InParanoid; Q9SKB7; -.
DR PhylomeDB; Q9SKB7; -.
DR BRENDA; 3.1.3.36; 399.
DR SABIO-RK; Q9SKB7; -.
DR PRO; PR:Q9SKB7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKB7; baseline and differential.
DR Genevisible; Q9SKB7; AT.
DR GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IEA:RHEA.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SMART; SM00128; IPPc; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Isopeptide bond; Magnesium; Metal-binding;
KW Reference proteome; Repeat; Ubl conjugation; WD repeat.
FT CHAIN 1..1144
FT /note="Type II inositol polyphosphate 5-phosphatase 14"
FT /id="PRO_0000359744"
FT REPEAT 158..196
FT /note="WD 1"
FT REPEAT 216..255
FT /note="WD 2"
FT REPEAT 269..307
FT /note="WD 3"
FT REPEAT 445..483
FT /note="WD 4"
FT REPEAT 524..561
FT /note="WD 5"
FT REGION 15..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..807
FT /note="Catalytic 1"
FT /evidence="ECO:0000250|UniProtKB:Q84MA2"
FT REGION 870..885
FT /note="Catalytic 2"
FT /evidence="ECO:0000250|UniProtKB:Q84MA2"
FT REGION 1111..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 949
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O80560"
SQ SEQUENCE 1144 AA; 125708 MW; 414BBDDD0DAB7249 CRC64;
MDSVIIEPDE REALASLVPA HPLPPRKTHS YVEQCEQKPH HPIRKYSLDE GSRSVTSDSE
AVYFDSSDGE FSTEGVAIVD GRTSGERGNG EECGFVTPPS KPASQGGGND GGREDDIESL
PEFIGAGGGL DVFKVPVRAA VNPGRPPCLE LRPHPLRETQ TGKFLRNIAC TESQLWAGQE
NGVRFWNLEE AYEVGCGLGG QVRRGDEDTA PFHESVPTSP ALCLLVDHGN RLVWTGHKDG
KIRAWKMNQP NTTTADDSKP FKERLSWQAH RGPVNYIVIS SYGDMWSCSD GGVIKIWTLD
SLEKSLVLKL EEKHMAALLV ERSGIDLRSQ VTVNGTCSIS SSDVKFLLVD TVKAKVWAVQ
HLSFSLWDAQ NKELLKVFNI DGQVENRVDM PPTQGQQVED TKAKFFSAPK KEKSQGFLQR
SRHAIMGAAG AVRRAATRSA GAFAEDTRKV EAIAIAADGS IWTGSMNGVI AQWDGNGSRL
REVNHHQQAV LCFCTFGDRI YVGYSSGYIQ VLDLGGKLIA SWVSHNEPVI KLAAGGGFIF
SLATHGGVRG WYVTSPGPLD SLIRTELSQK EMAYARQDSV KILIGTWNVG EGRASRGALV
SWLGSAVSDV GIVAIGLQEV DMGAGFLAMS TAKETVGVEG SAVGQWWLDA IGNALDERNT
FERMGSRQLA GLLISLWVRK SIRTHVGDLD VAAVPCGFGR AIGNKGGVGL RIRVYDRIMC
FVNCHLAAHL EAVTRRNADF NHIYRSMVFS KGQSVYTAAA AGASTSAQAL KNNPNTNNST
EEEKSHLASA DLVAFFGDFN YRLFGITYDE ARDFISHRSF DWLREKDQLR QEMNEGKVFQ
GMREALITFP PTYKFEKNKP GLGGYDSGEK KRIPAWCDRV IYRDNQSISY TECSLKCPVV
SSTIMYEACM DVTESDHKPV RCKLHANIAH TDKSVRRQEL GKIVKSNEKL RAMFEELKSV
PETSVSTNNI LLHSQDTFIF TIRNTSNSSR AIFNIVCKGQ TLVREDGEEP DNHSRGTFGL
PRWLEVSPGA GIIKPDASLQ VKVHHEDSHN SEEFIDGIQQ NSLSEESSDK EVTLIIIVQG
SCSTRTISHS IKVRHCSSAA KSLSLVHSKT TTMTKNLEGS TRYQTDANRG GSTRHRTDDS
TRRG
