IP5P3_ARATH
ID IP5P3_ARATH Reviewed; 664 AA.
AC Q8H0Z6; Q94AB6; Q9C9J4; Q9M9H5;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Type IV inositol polyphosphate 5-phosphatase 3 {ECO:0000305};
DE Short=At5PTase3 {ECO:0000305};
DE EC=3.1.3.36 {ECO:0000269|PubMed:21677096};
DE EC=3.1.3.86 {ECO:0000269|PubMed:21677096};
GN Name=IP5P3 {ECO:0000305};
GN OrderedLocusNames=At1g71710 {ECO:0000312|Araport:AT1G71710};
GN ORFNames=F14O23_9 {ECO:0000312|EMBL:AAF43224.1},
GN F26A9.1 {ECO:0000312|EMBL:AAG51823.1};
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=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 [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=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 [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 IDENTIFICATION BY 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 [6]
RP CATALYTIC ACTIVITY, AND FUNCTION.
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).
CC -!- FUNCTION: Has phosphatase activity toward PtdIns(4,5)P2 and
CC PtdIns(3,4,5)P3. {ECO:0000269|PubMed:21677096}.
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:21677096};
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:21677096};
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=Q8H0Z6-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the inositol polyphosphate 5-phosphatase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF43224.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC012654; AAF43224.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC016163; AAG51823.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35221.1; -; Genomic_DNA.
DR EMBL; AY048296; AAK82558.1; -; mRNA.
DR EMBL; BT001070; AAN46835.1; -; mRNA.
DR PIR; D96739; D96739.
DR RefSeq; NP_565023.1; NM_105829.4. [Q8H0Z6-1]
DR AlphaFoldDB; Q8H0Z6; -.
DR SMR; Q8H0Z6; -.
DR STRING; 3702.AT1G71710.1; -.
DR iPTMnet; Q8H0Z6; -.
DR PaxDb; Q8H0Z6; -.
DR PRIDE; Q8H0Z6; -.
DR ProteomicsDB; 228822; -. [Q8H0Z6-1]
DR EnsemblPlants; AT1G71710.1; AT1G71710.1; AT1G71710. [Q8H0Z6-1]
DR GeneID; 843501; -.
DR Gramene; AT1G71710.1; AT1G71710.1; AT1G71710. [Q8H0Z6-1]
DR KEGG; ath:AT1G71710; -.
DR Araport; AT1G71710; -.
DR TAIR; locus:2013031; AT1G71710.
DR eggNOG; KOG0565; Eukaryota.
DR InParanoid; Q8H0Z6; -.
DR PhylomeDB; Q8H0Z6; -.
DR BioCyc; ARA:AT1G71710-MON; -.
DR PRO; PR:Q8H0Z6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8H0Z6; baseline and differential.
DR Genevisible; Q8H0Z6; AT.
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:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA: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; 2.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF56219; SSF56219; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Reference proteome.
FT CHAIN 1..664
FT /note="Type IV inositol polyphosphate 5-phosphatase 3"
FT /id="PRO_0000433254"
FT REGION 35..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..529
FT /note="Catalytic 1"
FT /evidence="ECO:0000250|UniProtKB:Q84MA2"
FT REGION 592..607
FT /note="Catalytic 2"
FT /evidence="ECO:0000250|UniProtKB:Q84MA2"
FT COMPBIAS 44..63
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 165
FT /note="L -> S (in Ref. 3; AAK82558)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 664 AA; 74780 MW; 46B578594A21A8D4 CRC64;
MSPVEPAGIM KKSHRQKSQR LWAKLVMRKW LNISGRDPEY GADTDNESEN EDAREDNDDS
SSDEEGGSGS RGRESKVYEN AEDAIAAASA VVDAAAAAAE FISNDAPMKL RRRNSETLRA
QYINNKEIRV CVGTWNVGGI SPPSDLDIDD WIEINQPADI YVLGLQEIVP LNAGNILGAE
DDRPVAKWEE VIREALNRVR PKLSGVKSYS DPPSPGRFKP FEETHDIIEE EVAFESDSDA
GVEIHPIDEE EEEETDRLWA LKHDGGVIGE VKTLVDPNTG LPVVEIKRQF SIPKKLDRQL
CLRADSFKGI SDDDSTQTGM KTINRMLSGK ERIGLSWPEP PLNMLGPCVL DRQPSIKTVK
SLKTAKSFKA YSSFKSVAGN NNGIPPEVLA LAEMDLKLLM ERKRRPAYVR LVSKQMVGIL
LTIWVKRSLR KHIQNVRVST VGVGVMGYIG NKGAVSVSMS INQTFFCFIN THLTAGEREV
DQIKRNADVH EIHKRTVFHS VSALGLPKLI YDHERIIWLG DLNYRLSSSY EKTRDLISKR
EWSKLLEYDQ LVKEYRKGRA FDGWSEGTLH FPPTYKYQAN SDEYTANDGK APKRTPAWCD
RVLSYGKGMR LVHYRRTEQK FSDHRPVTAI YMAEVEVFSA RKLQRALTFT DAEIEDEGLV
AVLV
