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Reviewed, UniProtKB/Swiss-Prot Q9FUR2 (IP5P2_ARATH)

Last modified February 9, 2010. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length646 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 646646Type I inositol-1,4,5-trisphosphate 5-phosphatase 2
PRO_0000209723

Regions

Region495 – 51016Catalytic 1 Potential
Region575 – 59016Catalytic 2 Potential
Compositional bias333 – 3375Poly-Ser

Natural variations

Alternative sequence327 – 35933Missing in isoform 2.
VSP_013849

Experimental info

Sequence conflict721A → R in CAB59428. Ref.2
Sequence conflict4831L → F in AAD10829. Ref.3
Sequence conflict5731P → G Ref.1
Sequence conflict5731P → G Ref.2
Sequence conflict5731P → G Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: FD7D59676B9862BE

FASTA64673,579
        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 

« Hide

Isoform 2.

Checksum: EEE96FFEA4E61F1A
Show »

FASTA61370,081

References

« Hide '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. expand/collapse author list , 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.
+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.
IPIIPI00523513.
IPI00525232.
PIRT05087.
T51937.
T51938.
RefSeqNP_567547.1.
NP_849402.1.
UniGeneAt.2057

3D structure databases

SMRQ9FUR2. Positions 103-629.
ModBaseSearch...

Proteomic databases

PRIDEQ9FUR2.

Genome annotation databases

GeneID827526.
GenomeReviewsGene locus AT4G18010 in contig CT486007_GR.
KEGGath:AT4G18010.
NMPDRfig|3702.1.peg.19594.

Organism-specific databases

GeneFarm4926.
TAIRAt4g18010.

Phylogenomic databases

eggNOGKOG0565.
HOGENOMHBG593315.
InParanoidQ9FUR2.
OMAVEVFDHR.
PhylomeDBQ9FUR2.

Enzyme and pathway databases

BRENDA3.1.3.56. 302.

Gene expression databases

GenevestigatorQ9FUR2.
GermOnlineAT4G18010. Arabidopsis thaliana.

Family and domain databases

InterProIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
[Graphical view]
PfamPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SMARTSM00128. IPPc. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIP5P2_ARATH
AccessionPrimary (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: February 9, 2010
This is version 55 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents