IP5P6_ARATH
ID IP5P6_ARATH Reviewed; 617 AA.
AC Q9LR47;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Type IV inositol polyphosphate 5-phosphatase 6 {ECO:0000305};
DE Short=At5PTase6 {ECO:0000305};
DE EC=3.1.3.36 {ECO:0000269|PubMed:19473324};
DE EC=3.1.3.86 {ECO:0000269|PubMed:19473324};
DE AltName: Full=Protein COTYLEDON VASCULAR PATTERN 2 {ECO:0000303|PubMed:10559439};
GN Name=IP5P6 {ECO:0000305}; Synonyms=CVP2 {ECO:0000303|PubMed:10559439};
GN OrderedLocusNames=At1g05470 {ECO:0000312|Araport:AT1G05470};
GN ORFNames=T25N20.12 {ECO:0000312|EMBL:AAF79735.1};
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] (ISOFORM 2).
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 FUNCTION, AND MUTANT CVP2-1.
RX PubMed=10559439; DOI=10.2307/3871014;
RA Carland F.M., Berg B.L., FitzGerald J.N., Jinamornphongs S., Nelson T.,
RA Keith B.;
RT "Genetic regulation of vascular tissue patterning in Arabidopsis.";
RL Plant Cell 11:2123-2137(1999).
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, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP ALA-543 AND GLY-575.
RX PubMed=15100402; DOI=10.1105/tpc.021030;
RA Carland F.M., Nelson T.;
RT "COTYLEDON VASCULAR PATTERN2-mediated inositol (1,4,5) triphosphate signal
RT transduction is essential for closed venation patterns of Arabidopsis
RT foliar organs.";
RL Plant Cell 16:1263-1275(2004).
RN [7]
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 [8]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, 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 [9]
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
CC PtdIns(3,4,5)P3 (PubMed:19473324). Required for the patterning of
CC procambium and during the differentiation of vascular tissues. Acts
CC before the acquisition of preprocambial identity. Seems to be also
CC involved in the abscisic acid (ABA) signaling pathway (PubMed:10559439,
CC PubMed:15100402). Acts redundantly with CVL1 for maintaining vascular
CC continuity (PubMed:19363154, PubMed:25813544). Regulates
CC phosphoinositide-dependent VAN3 localization (PubMed:19473324).
CC {ECO:0000269|PubMed:10559439, ECO:0000269|PubMed:15100402,
CC ECO:0000269|PubMed:19363154, ECO:0000269|PubMed:19473324,
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};
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};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LR47-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LR47-2; Sequence=VSP_037992, VSP_037993;
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:15100402,
CC ECO:0000269|PubMed:19473324}.
CC -!- DEVELOPMENTAL STAGE: During early stages of embryogenesis, broadly
CC expressed throughout globular and torpedo stages. At late torpedo
CC stage, strongly expressed in developing vascular cells and weakly
CC expressed in surrounding cells. By the walking-stick stage, restricted
CC to incipient vascular cells of the apical loop, the midvein of the
CC cotyledon and the root vasculature. In emerging leaves, strongly
CC expressed in procambium and weakly expressed in areole cells. Limited
CC to developing vascular cells in later stage of leaf development. In
CC roots, expressed in procambium of the elongating zone and in immature
CC vascular cells of the root differentiation zone. During inflorescence
CC development, broadly expressed in young floral buds, and gradually
CC restricted to procambium of cauline leaves, sepals, petals, gynoecia
CC and anthers. {ECO:0000269|PubMed:15100402,
CC ECO:0000269|PubMed:19473324}.
CC -!- MISCELLANEOUS: CVP2 overexpression impairs protophloeme sieve element
CC differentiation and overall root growth. Cvp1 and cvp2 double mutant
CC displays high PtdIns(4,5)P2 levels. {ECO:0000269|PubMed:25813544}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the inositol polyphosphate 5-phosphatase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79735.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BX816898; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AC005106; AAF79735.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27844.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59756.1; -; Genomic_DNA.
DR EMBL; BX816898; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001322092.1; NM_001331550.1. [Q9LR47-1]
DR RefSeq; NP_172038.4; NM_100426.5. [Q9LR47-1]
DR AlphaFoldDB; Q9LR47; -.
DR SMR; Q9LR47; -.
DR BioGRID; 22290; 1.
DR STRING; 3702.AT1G05470.1; -.
DR PaxDb; Q9LR47; -.
DR PRIDE; Q9LR47; -.
DR ProteomicsDB; 228816; -. [Q9LR47-1]
DR EnsemblPlants; AT1G05470.1; AT1G05470.1; AT1G05470. [Q9LR47-1]
DR EnsemblPlants; AT1G05470.2; AT1G05470.2; AT1G05470. [Q9LR47-1]
DR GeneID; 837048; -.
DR Gramene; AT1G05470.1; AT1G05470.1; AT1G05470. [Q9LR47-1]
DR Gramene; AT1G05470.2; AT1G05470.2; AT1G05470. [Q9LR47-1]
DR KEGG; ath:AT1G05470; -.
DR Araport; AT1G05470; -.
DR TAIR; locus:2201016; AT1G05470.
DR eggNOG; KOG0565; Eukaryota.
DR HOGENOM; CLU_011711_4_0_1; -.
DR InParanoid; Q9LR47; -.
DR OMA; IPVPMAE; -.
DR PhylomeDB; Q9LR47; -.
DR BioCyc; ARA:AT1G05470-MON; -.
DR PRO; PR:Q9LR47; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LR47; baseline and differential.
DR Genevisible; Q9LR47; AT.
DR GO; GO:0046030; F:inositol trisphosphate phosphatase activity; IMP:TAIR.
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:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0010588; P:cotyledon vascular tissue pattern formation; IMP:TAIR.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IMP:TAIR.
DR GO; GO:0048016; P:inositol phosphate-mediated signaling; IC:TAIR.
DR GO; GO:0032957; P:inositol trisphosphate metabolic process; IMP:TAIR.
DR GO; GO:0010305; P:leaf vascular tissue pattern formation; IMP:TAIR.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB.
DR GO; GO:0010067; P:procambium histogenesis; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0010051; P:xylem and phloem pattern formation; IMP:TAIR.
DR Gene3D; 3.60.10.10; -; 2.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR045849; IP5P_plant.
DR InterPro; IPR000300; IPPc.
DR PANTHER; PTHR45666; PTHR45666; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF56219; SSF56219; 2.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing; Differentiation;
KW Hydrolase; Reference proteome.
FT CHAIN 1..617
FT /note="Type IV inositol polyphosphate 5-phosphatase 6"
FT /id="PRO_0000209724"
FT REGION 30..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..473
FT /note="Catalytic 1"
FT /evidence="ECO:0000250|UniProtKB:Q84MA2"
FT REGION 538..553
FT /note="Catalytic 2"
FT /evidence="ECO:0000250|UniProtKB:Q84MA2"
FT COMPBIAS 257..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..111
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037992"
FT VAR_SEQ 112..128
FT /note="LDEWLHSSAPADIYVLG -> MSGFIHQLLLISMYSGI (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037993"
FT MUTAGEN 543
FT /note="A->V: In cvp2-2; induces an open vein network."
FT /evidence="ECO:0000269|PubMed:15100402"
FT MUTAGEN 575
FT /note="G->D: In cvp2-1; induces an open vein network."
FT /evidence="ECO:0000269|PubMed:15100402"
SQ SEQUENCE 617 AA; 70853 MW; B4325EA5F3FE915C CRC64;
MREEKSKTNK LAWSKKMVRK WFNIKSKTEE FQADDPSSAG IEVEHRSSFS AEKAPSTIKN
TKTEKLSKNW EQQARQRRMN YENPRIIDVQ NYSIFVATWN VAGRSPPSDL NLDEWLHSSA
PADIYVLGFQ EIVPLNAGNV LGAEDNGPAQ KWLSLIRKTL NNRPGTSGTS GYHTPSPIPV
PMAELDADFS GSTRQKNSTF FHRRSFQTPS STWNDPSIPQ PGLDRRFSVC DRVFFSHRPS
DFDPSFRGSS SSHRPSDYSR RPSDYSRRPS DYSRRPSDYS RRPSDSRPSD YSRPSDYYSR
PSDYSRPSDF SRSSDDDNGL GDSPSTVLYS PGSAANENGY RIPWNSSQYC LVASKQMVGV
FLTIWVKSEL REHVKNMKVS CVGRGLMGYL GNKGSISISM LLHQTSFCFV CTHLTSGQKE
GDELKRNSDV MEILKKTRFP RVKSSEEEKS PENILQHDRV IWLGDLNYRI ALSYRSAKAL
VEMQNWRALL ENDQLRIEQK RGHVFKGWNE GKIYFPPTYK YSRNSDRYSG DDLHPKEKRR
TPAWCDRILW FGEGLHQLSY VRGESRFSDH RPVYGIFCAE VESAHNRIKR TTSYSASRVQ
AEELLPYSRG YTELSFF
