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Q84MA2 (IP5P1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Type I inositol 1,4,5-trisphosphate 5-phosphatase 1

Short name=At5PTase1
EC=3.1.3.56
Gene names
Name:IP5P1
Synonyms:5P1
Ordered Locus Names:At1g34120
ORF Names:F12G12.6
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length590 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 Ins(1,4)P2 and Ins1P. Ref.7 Ref.8

Catalytic activity

D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate. Ref.7

1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate. Ref.7

Tissue specificity

Expressed ubiquitously. Ref.7

Induction

Induced by ABA at both transcript and protein levels in a specific, transient manner. Ref.8

Sequence similarities

Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase type I family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q84MA2-1)

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: Q84MA2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     79-83: GNVIY → D
Note: May be due to a donor acceptor splice site.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 590590Type I inositol 1,4,5-trisphosphate 5-phosphatase 1
PRO_0000209722

Regions

Region445 – 46016Catalytic 1 Potential
Region523 – 53816Catalytic 2 Potential

Amino acid modifications

Modified residue601Phosphoserine Ref.9 Ref.10

Natural variations

Alternative sequence79 – 835GNVIY → D in isoform 2.
VSP_013848

Experimental info

Sequence conflict211S → L in AAG17824. Ref.1
Sequence conflict801N → D in AAD10828. Ref.2
Sequence conflict2391S → G in AAD10828. Ref.2
Sequence conflict4781E → K in AAD10828. Ref.2

Sequences

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

Last modified June 7, 2005. Version 2.
Checksum: 53C31A05D4C04428

FASTA59067,783
        10         20         30         40         50         60 
MAEVRSRSRR TESNWATICC SAFSCLQLYW ARIVLRKWFN VSASESDYSA DSDDDYEDRS 

        70         80         90        100        110        120 
QEFDPISSGV TNPRVDTDGN VIYRPKLRRR NSETFRMQYI DTKAIRICAG TWNVGGRVPS 

       130        140        150        160        170        180 
SDLDIDGWLD TLEPADIYVL GLQEIVPLNA GNIFGMEDDQ PALEWENLIR DALNRVQPRK 

       190        200        210        220        230        240 
LKIKSHSDPP SPSKFKQPEE VPYSVEDMFV ETSHDACDGI SSMDNKLNSV ESTDVPIVSE 

       250        260        270        280        290        300 
DSLTNIDVLG STNDNASCLP IQEYLQRQFS TPNTPDRSLS MQINSDSKRE ERFSYTERVG 

       310        320        330        340        350        360 
LSWPEPPLRL LNQYVSERRG SFKSVNLTIT NLRKPSYVRI VSKQMVGVFL TIWVRRNLRK 

       370        380        390        400        410        420 
HISNLCVSTV GVGIMGYIGN KGSVSVSMSI YQTPFCFLCT HLSSGEKDTD QEKRNDDVRE 

       430        440        450        460        470        480 
IHRRTQFLPH SLNANELPRS ICNHERIIWL GDLNYRINLS YEKTHELIAR KEWQRLVEYD 

       490        500        510        520        530        540 
QLSREMTKGN LFEGWSEGTL DFAPTYKYEI DSENYIGDDP ESGKRRPAWC DRIIWNGKGM 

       550        560        570        580        590 
KLFNYRRNEI KLSDHRPVTA TFLAEVEVLS PRKLQHALTL TYAEIQGLDA 

« Hide

Isoform 2 [UniParc].

Checksum: 3C116AA1EE16F359
Show »

FASTA58667,352

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: cv. Landsberg erecta.
[2]"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.
[3]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: cv. Columbia.
[6]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: cv. Columbia.
[7]"Molecular characterization of At5PTase1, an inositol phosphatase capable of terminating inositol trisphosphate signaling."
Berdy S.E., Kudla J., Gruissem W., Gillaspy G.E.
Plant Physiol. 126:801-810(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
[8]"An Arabidopsis inositol 5-phosphatase gain-of-function alters abscisic acid signaling."
Burnette R.N., Gunesekera B.M., Gillaspy G.E.
Plant Physiol. 132:1011-1019(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[9]"Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: cv. Columbia.
[10]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF289633 mRNA. Translation: AAG17824.1.
AF117062 mRNA. Translation: AAD10828.1.
AC015446 Genomic DNA. Translation: AAG12525.1.
CP002684 Genomic DNA. Translation: AEE31672.1.
CP002684 Genomic DNA. Translation: AEE31674.1.
BT006448 mRNA. Translation: AAP21256.1.
AK227368 mRNA. Translation: BAE99376.1.
PIRC86465.
RefSeqNP_564437.1. NM_103135.3.
NP_849745.1. NM_179414.1.
UniGeneAt.10999.
At.73182.

3D structure databases

ProteinModelPortalQ84MA2.
SMRQ84MA2. Positions 99-572.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ84MA2.
PRIDEQ84MA2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G34120.2; AT1G34120.2; AT1G34120. [Q84MA2-1]
GeneID840311.
KEGGath:AT1G34120.

Organism-specific databases

GeneFarm4925.
TAIRAT1G34120.

Phylogenomic databases

eggNOGCOG5411.
HOGENOMHOG000241161.
InParanoidQ84MA2.
OMAIRICAGT.
PhylomeDBQ84MA2.
ProtClustDBCLSN2688257.

Enzyme and pathway databases

BioCycARA:AT1G34120-MONOMER.
ARA:GQT-260-MONOMER.
ARA:GQT-261-MONOMER.
MetaCyc:AT1G34120-MONOMER.
BRENDA3.1.3.56. 399.

Gene expression databases

GenevestigatorQ84MA2.

Family and domain databases

Gene3D3.60.10.10. 2 hits.
InterProIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
[Graphical view]
PfamPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SMARTSM00128. IPPc. 1 hit.
[Graphical view]
SUPFAMSSF56219. SSF56219. 2 hits.
ProtoNetSearch...

Entry information

Entry nameIP5P1_ARATH
AccessionPrimary (citable) accession number: Q84MA2
Secondary accession number(s): Q0WU22 expand/collapse secondary AC list , Q9FUR3, Q9FX20, Q9ZSC4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: April 16, 2014
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names