Q9FUR2 (IP5P2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2
Short name=At5PTase2
EC=3.1.3.56

Gene names

Name:	IP5P2
Synonyms:	5P2
Ordered Locus Names:	At4g18010
ORF Names:	T6K21.190

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	646 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Seems to be involved in the abscisic acid (ABA) signaling pathway. Has phosphatase activity toward Ins(1,4,5)P3 and Ins(1,3,4,5)P4, but not toward PtdIns(4,5)P2. Ref.1
Catalytic activity	D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate. Ref.1 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate. Ref.1
Sequence similarities	Belongs to the inositol-1,4,5-trisphosphate 5-phosphatase type I family.
Sequence caution	The sequence CAA17144.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB78803.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Abscisic acid signaling pathway
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	abscisic acid mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW inositol phosphate dephosphorylation Inferred from direct assay Ref.1. Source: TAIR inositol trisphosphate metabolic process Inferred from mutant phenotype Ref.1. Source: TAIR seed germination Inferred from mutant phenotype. Source: TAIR
Molecular function	inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity Inferred from electronic annotation. Source: EC inositol-1,4,5-trisphosphate 5-phosphatase activity Inferred from electronic annotation. Source: EC inositol-polyphosphate 5-phosphatase activity Inferred from direct assay Ref.1. Source: TAIR
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9FUR2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9FUR2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     327-359: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 646	646	Type I inositol-1,4,5-trisphosphate 5-phosphatase 2		PRO_0000209723
Regions
	Region	495 – 510	16	Catalytic 1 Potential
	Region	575 – 590	16	Catalytic 2 Potential
	Compositional bias	333 – 337	5	Poly-Ser
Natural variations
	Alternative sequence	327 – 359	33	Missing in isoform 2.		VSP_013849
Experimental info
	Sequence conflict	72	1	A → R in CAB59428. Ref.2
	Sequence conflict	483	1	L → F in AAD10829. Ref.3
	Sequence conflict	573	1	P → G Ref.1
	Sequence conflict	573	1	P → G Ref.2
	Sequence conflict	573	1	P → G Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 7, 2005. Version 2. Checksum: FD7D59676B9862BE	FASTA	646	73,579
	10 20 30 40 50 60 MKTRRGKRPE RFWPSIVMNK WLNRKPKVYD FSEDEIDTEP ESEDDVCSVK DVPNVHCVTD 70 80 90 100 110 120 EDSHNGRRGS EADHGNNISD GGVSVRGGYQ RKHRRGKSET LRAQYINTKD IKVTVATWNV 130 140 150 160 170 180 AGKRPSDDLE IEDWLSTDNP SDIYIIGFQE VVPLNAGNVF GAEDRGPIPK WESIIRRTLN 190 200 210 220 230 240 KSNKESVYDQ SPSCNNNALH RSHSAPSSPI LAQEANSIIS HVMVENLVAD HSLDLATNEF 250 260 270 280 290 300 IDAATALPSL EPQRNPNMDW PELALDSNPQ IVGSEGKLRR VFSSNATLGF KLPENPSGAS 310 320 330 340 350 360 RFASEARQLK RSRSFETLNL SWNDIKEEID NRSSSSSEAE EAAKIMHDDS SDGDSSSQDE 370 380 390 400 410 420 EDGDKIRNSY GLPEDLVEEC RKVKDSQKYV RIVSKQMVGI YVSVWIRRRL RRHVNNLKVS 430 440 450 460 470 480 PVGVGLMGYM GNKGSVSISM TLYQSRMCFV CSHLTSGHKD GAEQRRNADV YEIIRRTRFA 490 500 510 520 530 540 SVLDTDQPRT IPCHDQVFWF GDLNYRLNMS DGEVRKLVSQ KRWDELKNSD QLIRELRRGH 550 560 570 580 590 600 VFDGWREGPI KFPPTYKYEF DSDRYAGENL REPEKKRAPA WCDRILWLGK GIRQECYKRS 610 620 630 640 EIRMSDHRPV TSIFNVGVEV FDHRKLQRAL HVNNAAASAV HPEPSF
	Isoform 2 [UniParc]. Checksum: EEE96FFEA4E61F1A	FASTA	613	70,081
	10 20 30 40 50 60 MKTRRGKRPE RFWPSIVMNK WLNRKPKVYD FSEDEIDTEP ESEDDVCSVK DVPNVHCVTD 70 80 90 100 110 120 EDSHNGRRGS EADHGNNISD GGVSVRGGYQ RKHRRGKSET LRAQYINTKD IKVTVATWNV 130 140 150 160 170 180 AGKRPSDDLE IEDWLSTDNP SDIYIIGFQE VVPLNAGNVF GAEDRGPIPK WESIIRRTLN 190 200 210 220 230 240 KSNKESVYDQ SPSCNNNALH RSHSAPSSPI LAQEANSIIS HVMVENLVAD HSLDLATNEF 250 260 270 280 290 300 IDAATALPSL EPQRNPNMDW PELALDSNPQ IVGSEGKLRR VFSSNATLGF KLPENPSGAS 310 320 330 340 350 360 RFASEARQLK RSRSFETLNL SWNDIKEEDG DKIRNSYGLP EDLVEECRKV KDSQKYVRIV 370 380 390 400 410 420 SKQMVGIYVS VWIRRRLRRH VNNLKVSPVG VGLMGYMGNK GSVSISMTLY QSRMCFVCSH 430 440 450 460 470 480 LTSGHKDGAE QRRNADVYEI IRRTRFASVL DTDQPRTIPC HDQVFWFGDL NYRLNMSDGE 490 500 510 520 530 540 VRKLVSQKRW DELKNSDQLI RELRRGHVFD GWREGPIKFP PTYKYEFDSD RYAGENLREP 550 560 570 580 590 600 EKKRAPAWCD RILWLGKGIR QECYKRSEIR MSDHRPVTSI FNVGVEVFDH RKLQRALHVN 610 NAAASAVHPE PSF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Arabidopsis PLC1 is required for secondary responses to abscisic acid signals." Sanchez J.-P., Chua N.-H. Plant Cell 13:1143-1154(2001) [PubMed: 11340187] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY. Strain: cv. Landsberg erecta.
[2]	Xue H., Mueller-Roeber B. Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Hypocotyl.
[3]	"Characterization of putative inositol (1,4,5)-trisphosphate/phosphatidylinositol (4,5)-bisphosphate 5-phosphatase cDNAs from Arabidopsis thaliana." Parzer M.S.A., de Vos S., van Lookeren Campagne M.M. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: cv. Columbia.
[4]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[5]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF289634 mRNA. Translation: AAG17825.1. AJ002295 mRNA. Translation: CAB59428.1. AF117063 mRNA. Translation: AAD10829.1. AL021889 Genomic DNA. Translation: CAA17144.1. Sequence problems. AL161547 Genomic DNA. Translation: CAB78803.1. Sequence problems. CP002687 Genomic DNA. Translation: AEE83978.1. CP002687 Genomic DNA. Translation: AEE83979.1.
IPI	IPI00523513. IPI00525232.
PIR	T05087. T51937. T51938.
RefSeq	NP_567547.1. NM_117911.3. NP_849402.1. NM_179071.1.
UniGene	At.2057.
3D structure databases
ProteinModelPortal	Q9FUR2.
SMR	Q9FUR2. Positions 105-623.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9FUR2.
Proteomic databases
PRIDE	Q9FUR2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G18010.1; AT4G18010.1; AT4G18010.
GeneID	827526.
GenomeReviews	Gene locus AT4G18010 in contig CT486007_GR.
KEGG	ath:AT4G18010.
NMPDR	fig|3702.1.peg.19594.
Organism-specific databases
GeneFarm	4926.
TAIR	At4g18010.
Phylogenomic databases
eggNOG	KOG0565.
GeneTree	EPGT00050000003839.
HOGENOM	HBG593315.
InParanoid	Q9FUR2.
OMA	VEVFDHR.
PhylomeDB	Q9FUR2.
ProtClustDB	PLN03191.
Enzyme and pathway databases
BRENDA	3.1.3.56. 399.
Gene expression databases
Genevestigator	Q9FUR2.
GermOnline	AT4G18010. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR005135. Endo/exonuclease/phosphatase. IPR000300. IPPc. [Graphical view]
Pfam	PF03372. Exo_endo_phos. 1 hit. [Graphical view]
SMART	SM00128. IPPc. 1 hit. [Graphical view]
SUPFAM	SSF56219. Exo_endo_phos. 1 hit.
ProtoNet	Search...

Entry information

Entry name

IP5P2_ARATH

Accession

Primary (citable) accession number: Q9FUR2
Secondary accession number(s): O49700, Q9SNF1, Q9ZSC3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	November 16, 2011
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program