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Protein

Type I inositol 1,4,5-trisphosphate 5-phosphatase 1

Gene

IP5P1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

GO - Molecular functioni

  1. inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity Source: UniProtKB-EC
  2. inositol-1,4,5-trisphosphate 5-phosphatase activity Source: UniProtKB-EC
  3. inositol-polyphosphate 5-phosphatase activity Source: TAIR
  4. inositol trisphosphate phosphatase activity Source: TAIR

GO - Biological processi

  1. abscisic acid-activated signaling pathway Source: UniProtKB-KW
  2. inositol phosphate dephosphorylation Source: TAIR
  3. inositol trisphosphate metabolic process Source: TAIR
  4. phosphatidylinositol dephosphorylation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Abscisic acid signaling pathway

Enzyme and pathway databases

BioCyciARA:AT1G34120-MONOMER.
ARA:GQT-260-MONOMER.
ARA:GQT-261-MONOMER.
MetaCyc:AT1G34120-MONOMER.
BRENDAi3.1.3.56. 399.
ReactomeiREACT_187614. Synthesis of IP3 and IP4 in the cytosol.
REACT_187626. Synthesis of IP2, IP, and Ins in the cytosol.
REACT_187642. Synthesis of PIPs at the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Type I inositol 1,4,5-trisphosphate 5-phosphatase 1 (EC:3.1.3.56)
Short name:
At5PTase1
Gene namesi
Name:IP5P1
Synonyms:5P1
Ordered Locus Names:At1g34120
ORF Names:F12G12.6
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G34120.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 590590Type I inositol 1,4,5-trisphosphate 5-phosphatase 1PRO_0000209722Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ84MA2.
PRIDEiQ84MA2.

Expressioni

Tissue specificityi

Expressed ubiquitously.1 Publication

Inductioni

Induced by ABA at both transcript and protein levels in a specific, transient manner.1 Publication

Gene expression databases

ExpressionAtlasiQ84MA2. baseline.
GenevestigatoriQ84MA2.

Structurei

3D structure databases

ProteinModelPortaliQ84MA2.
SMRiQ84MA2. Positions 337-570.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni445 – 46016Catalytic 1Sequence AnalysisAdd
BLAST
Regioni523 – 53816Catalytic 2Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5411.
HOGENOMiHOG000241161.
InParanoidiQ84MA2.
OMAiIRICAGT.
PhylomeDBiQ84MA2.

Family and domain databases

Gene3Di3.60.10.10. 2 hits.
InterProiIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SMARTiSM00128. IPPc. 1 hit.
[Graphical view]
SUPFAMiSSF56219. SSF56219. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q84MA2-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAEVRSRSRR TESNWATICC SAFSCLQLYW ARIVLRKWFN VSASESDYSA
60 70 80 90 100
DSDDDYEDRS QEFDPISSGV TNPRVDTDGN VIYRPKLRRR NSETFRMQYI
110 120 130 140 150
DTKAIRICAG TWNVGGRVPS SDLDIDGWLD TLEPADIYVL GLQEIVPLNA
160 170 180 190 200
GNIFGMEDDQ PALEWENLIR DALNRVQPRK LKIKSHSDPP SPSKFKQPEE
210 220 230 240 250
VPYSVEDMFV ETSHDACDGI SSMDNKLNSV ESTDVPIVSE DSLTNIDVLG
260 270 280 290 300
STNDNASCLP IQEYLQRQFS TPNTPDRSLS MQINSDSKRE ERFSYTERVG
310 320 330 340 350
LSWPEPPLRL LNQYVSERRG SFKSVNLTIT NLRKPSYVRI VSKQMVGVFL
360 370 380 390 400
TIWVRRNLRK HISNLCVSTV GVGIMGYIGN KGSVSVSMSI YQTPFCFLCT
410 420 430 440 450
HLSSGEKDTD QEKRNDDVRE IHRRTQFLPH SLNANELPRS ICNHERIIWL
460 470 480 490 500
GDLNYRINLS YEKTHELIAR KEWQRLVEYD QLSREMTKGN LFEGWSEGTL
510 520 530 540 550
DFAPTYKYEI DSENYIGDDP ESGKRRPAWC DRIIWNGKGM KLFNYRRNEI
560 570 580 590
KLSDHRPVTA TFLAEVEVLS PRKLQHALTL TYAEIQGLDA
Length:590
Mass (Da):67,783
Last modified:June 7, 2005 - v2
Checksum:i53C31A05D4C04428
GO
Isoform 2 (identifier: Q84MA2-2) [UniParc]FASTAAdd to basket

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.

Show »
Length:586
Mass (Da):67,352
Checksum:i3C116AA1EE16F359
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211S → L in AAG17824 (PubMed:11340187).Curated
Sequence conflicti80 – 801N → D in AAD10828 (Ref. 2) Curated
Sequence conflicti239 – 2391S → G in AAD10828 (Ref. 2) Curated
Sequence conflicti478 – 4781E → K in AAD10828 (Ref. 2) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei79 – 835GNVIY → D in isoform 2. 3 PublicationsVSP_013848

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiC86465.
RefSeqiNP_564437.1. NM_103135.3. [Q84MA2-2]
NP_849745.1. NM_179414.1. [Q84MA2-1]
UniGeneiAt.10999.
At.73182.

Genome annotation databases

EnsemblPlantsiAT1G34120.2; AT1G34120.2; AT1G34120. [Q84MA2-1]
GeneIDi840311.
KEGGiath:AT1G34120.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiC86465.
RefSeqiNP_564437.1. NM_103135.3. [Q84MA2-2]
NP_849745.1. NM_179414.1. [Q84MA2-1]
UniGeneiAt.10999.
At.73182.

3D structure databases

ProteinModelPortaliQ84MA2.
SMRiQ84MA2. Positions 337-570.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiQ84MA2.
PRIDEiQ84MA2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G34120.2; AT1G34120.2; AT1G34120. [Q84MA2-1]
GeneIDi840311.
KEGGiath:AT1G34120.

Organism-specific databases

GeneFarmi4925.
TAIRiAT1G34120.

Phylogenomic databases

eggNOGiCOG5411.
HOGENOMiHOG000241161.
InParanoidiQ84MA2.
OMAiIRICAGT.
PhylomeDBiQ84MA2.

Enzyme and pathway databases

BioCyciARA:AT1G34120-MONOMER.
ARA:GQT-260-MONOMER.
ARA:GQT-261-MONOMER.
MetaCyc:AT1G34120-MONOMER.
BRENDAi3.1.3.56. 399.
ReactomeiREACT_187614. Synthesis of IP3 and IP4 in the cytosol.
REACT_187626. Synthesis of IP2, IP, and Ins in the cytosol.
REACT_187642. Synthesis of PIPs at the plasma membrane.

Gene expression databases

ExpressionAtlasiQ84MA2. baseline.
GenevestigatoriQ84MA2.

Family and domain databases

Gene3Di3.60.10.10. 2 hits.
InterProiIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SMARTiSM00128. IPPc. 1 hit.
[Graphical view]
SUPFAMiSSF56219. SSF56219. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.
    , 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].

Entry informationi

Entry nameiIP5P1_ARATH
AccessioniPrimary (citable) accession number: Q84MA2
Secondary accession number(s): Q0WU22
, Q9FUR3, Q9FX20, Q9ZSC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: January 7, 2015
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.