IP5PF_ARATH
ID IP5PF_ARATH Reviewed; 1101 AA.
AC Q84W55; O04475; Q5MK18; Q9XFT1;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Type II inositol polyphosphate 5-phosphatase 15 {ECO:0000305};
DE Short=At5PTase15 {ECO:0000305};
DE EC=3.1.3.36 {ECO:0000269|PubMed:15539468};
DE EC=3.1.3.86 {ECO:0000269|PubMed:15539468};
DE AltName: Full=Protein FRAGILE FIBER 3 {ECO:0000303|PubMed:15539468};
GN Name=IP5P15 {ECO:0000305}; Synonyms=FRA3 {ECO:0000303|PubMed:15539468};
GN OrderedLocusNames=At1g65580 {ECO:0000312|Araport:AT1G65580};
GN ORFNames=F5I14.11 {ECO:0000312|EMBL:AAB60921.1};
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, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, COFACTOR, AND
RP MUTAGENESIS OF ALA-833.
RC STRAIN=cv. Columbia;
RX PubMed=15539468; DOI=10.1105/tpc.104.027466;
RA Zhong R., Burk D.H., Morrison W.H. III, Ye Z.-H.;
RT "FRAGILE FIBER3, an Arabidopsis gene encoding a type II inositol
RT polyphosphate 5-phosphatase, is required for secondary wall synthesis and
RT actin organization in fiber cells.";
RL Plant Cell 16:3242-3259(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Xue H., Mueller-Roeber B.;
RL Submitted (APR-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].
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 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. Has a higher substrate affinity
CC toward PtdIns(4,5)P2. Required for secondary wall synthesis and actin
CC organization in fiber cells. {ECO:0000269|PubMed:15539468}.
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:15539468};
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:15539468};
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:15539468};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15539468};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=63 uM for PtdIns(4,5)P2 (at pH 7.0 and 22 degrees Celsius);
CC KM=299 uM for PtdIns(3,4,5)P3 (at pH 7.0 and 22 degrees Celsius);
CC KM=1040 uM for PtdIns(1,4,5)P3 (at pH 6.5 and 22 degrees Celsius);
CC Vmax=240 pmol/min/ug enzyme with PtdIns(4,5)P2 as substrate (at pH
CC 7.0 and 22 degrees Celsius);
CC Vmax=365 pmol/min/ug enzyme with PtdIns(3,4,5)P3 as substrate (at pH
CC 7.0 and 22 degrees Celsius);
CC Vmax=504 pmol/min/ug enzyme with Ins(1,4,5)P3 as substrate (at pH 6.5
CC and 22 degrees Celsius);
CC pH dependence:
CC Optimum pH is 6.5 with Ins(1,4,5)P3 as substrate, 7.5 with
CC PtdIns(3,4,5)P3 as substrate, and 6.5-8.5 with PtdIns(4,5)P2 as
CC substrate.;
CC Temperature dependence:
CC Optimum temperature is 22 degrees Celsius with Ins(1,4,5)P3 as
CC substrate, and 22-37 degrees Celsius with PtdIns(4,5)P2 and
CC PtdIns(3,4,5)P3 as substrates.;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in interfascicular fibers
CC and vascular bundles. Expressed in seedlings, stems, roots and flowers.
CC Expressed at lower level in mature leaves.
CC {ECO:0000269|PubMed:15539468}.
CC -!- SIMILARITY: Belongs to the inositol polyphosphate 5-phosphatase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB60921.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY761186; AAV87313.1; -; mRNA.
DR EMBL; AY761190; AAV87317.1; -; Genomic_DNA.
DR EMBL; AJ005682; CAB41466.1; -; mRNA.
DR EMBL; AC001229; AAB60921.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34398.1; -; Genomic_DNA.
DR EMBL; BT004211; AAO42229.1; -; mRNA.
DR PIR; G96680; G96680.
DR RefSeq; NP_176736.2; NM_105232.3.
DR AlphaFoldDB; Q84W55; -.
DR SMR; Q84W55; -.
DR BioGRID; 28090; 1.
DR STRING; 3702.AT1G65580.1; -.
DR iPTMnet; Q84W55; -.
DR PaxDb; Q84W55; -.
DR PRIDE; Q84W55; -.
DR ProteomicsDB; 228821; -.
DR EnsemblPlants; AT1G65580.1; AT1G65580.1; AT1G65580.
DR GeneID; 842869; -.
DR Gramene; AT1G65580.1; AT1G65580.1; AT1G65580.
DR KEGG; ath:AT1G65580; -.
DR Araport; AT1G65580; -.
DR TAIR; locus:2034141; AT1G65580.
DR eggNOG; KOG0565; Eukaryota.
DR HOGENOM; CLU_004721_0_1_1; -.
DR InParanoid; Q84W55; -.
DR OMA; NSWCEDA; -.
DR OrthoDB; 106112at2759; -.
DR PhylomeDB; Q84W55; -.
DR BioCyc; ARA:AT1G65580-MON; -.
DR BRENDA; 3.1.3.36; 399.
DR PRO; PR:Q84W55; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84W55; baseline and differential.
DR Genevisible; Q84W55; 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; 5.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Isopeptide bond; Magnesium; Metal-binding; Reference proteome;
KW Repeat; Ubl conjugation; WD repeat.
FT CHAIN 1..1101
FT /note="Type II inositol polyphosphate 5-phosphatase 15"
FT /id="PRO_0000209726"
FT REPEAT 121..162
FT /note="WD 1"
FT REPEAT 180..219
FT /note="WD 2"
FT REPEAT 225..263
FT /note="WD 3"
FT REPEAT 403..432
FT /note="WD 4"
FT REPEAT 433..481
FT /note="WD 5"
FT REPEAT 483..519
FT /note="WD 6"
FT REGION 31..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..765
FT /note="Catalytic 1"
FT /evidence="ECO:0000250|UniProtKB:Q84MA2"
FT REGION 828..843
FT /note="Catalytic 2"
FT /evidence="ECO:0000250|UniProtKB:Q84MA2"
FT COMPBIAS 31..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 907
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O80560"
FT MUTAGEN 833
FT /note="A->V: In fra3; induces a dramatic reduction in
FT secondary wall thickness and a concomitant decrease in stem
FT strength. Causes elevated levels of PtdIns(4,5)P2 and
FT Ins(1,4,5)P3."
FT /evidence="ECO:0000269|PubMed:15539468"
FT CONFLICT 583
FT /note="G -> R (in Ref. 5; AAO42229)"
FT /evidence="ECO:0000305"
FT CONFLICT 847
FT /note="L -> F (in Ref. 2; CAB41466)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1101 AA; 121711 MW; 256882EB27511965 CRC64;
MEDRQNDQND DVFSFFSPSF SAATPSTLFN RSAYSSSSSS GDDESQPSVD DSNKRIDYMI
QFLDRRLSED GNHDGIGDGN GSDSLPEFVG KCGESGIFKV PIRSAVHPNR PPSLDVRPHP
LRETQIGRFL RTMTSTERQL WTGGEDGALR VWEFSELYGS GRGLEVEDTA PYKESLGNEF
GSAAVVCMIG DEGSRVVWSG HRDGRIRCWR LRGDHGIEEA LSWQAHRGPV LSIAISAYGD
IWSGSEGGAL KVWPWDGALG KSLSLKMEER HMAALAVERS YIDPRNMVSA NGFANTLTSD
VTFLVSDHTR ARVWSASPLT FAIWDARTRD LIKVFNIDGQ LENRPENSVY PDFGSEEEGK
MKVTASKKEK AQSSLGFFQR SRNAIMGAAD AVRRAATKGG FCDDSRKTEA IVISVDGMIW
TGSSNGILMR WDGNGNCLQE FAYESSGILC MFTFCSRLWV GYSNGTVQVW DLEGKLLGGW
VAHSGPVIKM AIGAGYLFTL ANHGGIRGWN VTSPGPLDNV LRAELAGKEF LYSRIENLKI
LAGTWNVGEG RASTDSLVSW LGCAATGVEI VVVGLQEVEM GAGVLAMSAA KETVGLEGSP
LGQWWLDMIG KTLDEGSSFV RVGSRQLAGL LICVWVRHDL KPHVGDVDAA AVPCGFGRAI
GNKGAVGVRL RMYDRVLCFV NCHFAAHLEA VNRRNADFDH VYRTMTFSRQ SSSLNAGVAG
ASFGVTMPRG GNALGVNTIE ARPELSEADM VIFLGDFNYR LDDITYDETR DFISQRCFDW
LREKDQLHTE MEAGNVFQGM REAIIRFPPT YKFERHQAGL AGYDSGEKKR IPAWCDRILY
RDNKKHLGAE CSLDCPVVSS ISQYDACMEV TDSDHKPVRC VFSVKIARVD ESVRRQEYGN
IINSNKKIKV LLGELSKVPE TIVSTNNIIL QNQDSTILRI TNKSEKNIAF FKIICEGQSK
IEEDGQAHDH RARGSFGFPQ WLEVSPGTGT IKPNQIAEVS VHLEDFPTVE EFVDGVAQNS
WCEDTRDKEV ILVLVVHGRF STETRKHRIR VRHCPRGGPA KNHFNDGTKT SGQINALHRS
DYHQLSNTLD VVEQLKNLHS P
