Q84MA2 (IP5P1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	590 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 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.

Ontologies

Keywords
Biological process	Abscisic acid signaling pathway
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase
PTM	Phosphoprotein
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.7. Source: TAIR inositol trisphosphate metabolic process Inferred from direct assay Ref.7. Source: TAIR phosphatidylinositol phosphorylation Inferred from electronic annotation. Source: InterPro
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.7. Source: TAIR
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 590	590	Type I inositol 1,4,5-trisphosphate 5-phosphatase 1		PRO_0000209722
Regions
	Region	445 – 460	16	Catalytic 1 Potential
	Region	523 – 538	16	Catalytic 2 Potential
Amino acid modifications
	Modified residue	60	1	Phosphoserine Ref.9
Natural variations
	Alternative sequence	79 – 83	5	GNVIY → D in isoform 2.		VSP_013848
Experimental info
	Sequence conflict	21	1	S → L in AAG17824. Ref.1
	Sequence conflict	80	1	N → D in AAD10828. Ref.2
	Sequence conflict	239	1	S → G in AAD10828. Ref.2
	Sequence conflict	478	1	E → K in AAD10828. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 7, 2005. Version 2. Checksum: 53C31A05D4C04428	FASTA	590	67,783
	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
	Isoform 2 [UniParc]. Checksum: 3C116AA1EE16F359	FASTA	586	67,352
	10 20 30 40 50 60 MAEVRSRSRR TESNWATICC SAFSCLQLYW ARIVLRKWFN VSASESDYSA DSDDDYEDRS 70 80 90 100 110 120 QEFDPISSGV TNPRVDTDDR PKLRRRNSET FRMQYIDTKA IRICAGTWNV GGRVPSSDLD 130 140 150 160 170 180 IDGWLDTLEP ADIYVLGLQE IVPLNAGNIF GMEDDQPALE WENLIRDALN RVQPRKLKIK 190 200 210 220 230 240 SHSDPPSPSK FKQPEEVPYS VEDMFVETSH DACDGISSMD NKLNSVESTD VPIVSEDSLT 250 260 270 280 290 300 NIDVLGSTND NASCLPIQEY LQRQFSTPNT PDRSLSMQIN SDSKREERFS YTERVGLSWP 310 320 330 340 350 360 EPPLRLLNQY VSERRGSFKS VNLTITNLRK PSYVRIVSKQ MVGVFLTIWV RRNLRKHISN 370 380 390 400 410 420 LCVSTVGVGI MGYIGNKGSV SVSMSIYQTP FCFLCTHLSS GEKDTDQEKR NDDVREIHRR 430 440 450 460 470 480 TQFLPHSLNA NELPRSICNH ERIIWLGDLN YRINLSYEKT HELIARKEWQ RLVEYDQLSR 490 500 510 520 530 540 EMTKGNLFEG WSEGTLDFAP TYKYEIDSEN YIGDDPESGK RRPAWCDRII WNGKGMKLFN 550 560 570 580 YRRNEIKLSD HRPVTATFLA EVEVLSPRKL QHALTLTYAE IQGLDA

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] [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]	"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, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	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.
IPI	IPI00532161. IPI00532180.
PIR	C86465.
RefSeq	NP_564437.1. NM_103135.3. NP_849745.1. NM_179414.1.
UniGene	At.10999. At.73182.
3D structure databases
ProteinModelPortal	Q84MA2.
SMR	Q84MA2. Positions 337-570.
ModBase	Search...
Proteomic databases
PaxDb	Q84MA2.
PRIDE	Q84MA2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G34120.2; AT1G34120.2; AT1G34120.
GeneID	840311.
KEGG	ath:AT1G34120.
Organism-specific databases
GeneFarm	4925.
TAIR	At1g34120.
Phylogenomic databases
eggNOG	COG5411.
HOGENOM	HOG000241161.
InParanoid	Q84MA2.
OMA	SYEKTHE.
PhylomeDB	Q84MA2.
ProtClustDB	CLSN2688257.
Enzyme and pathway databases
BioCyc	MetaCyc:AT1G34120-MONOMER.
BRENDA	3.1.3.56. 399.
Gene expression databases
ArrayExpress	Q84MA2.
Genevestigator	Q84MA2.
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

IP5P1_ARATH

Accession

Primary (citable) accession number: Q84MA2
Secondary accession number(s): Q0WU22 , Q9FUR3, Q9FX20, Q9ZSC4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	May 1, 2013
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program