Q5EAF2 (IP5PB_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Type I inositol 1,4,5-trisphosphate 5-phosphatase 11
Short name=At5PTase11
EC=3.1.3.56

Gene names

Ordered Locus Names:	At1g47510
ORF Names:	F16N3.22

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	334 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Has phosphatase activity toward PtdIns(4,5)P2, and in vitro toward PtdIns(3,5)P2 and PtdIns(3,4,5)P3. Can not dephosphorylate PtdIns5P, Ins(1,4,5)P3 and Ins(1,3,4,5)P4. Ref.4
Catalytic activity	D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate. 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate.
Tissue specificity	Expressed ubiquitously. Ref.4
Induction	Induced by abscisic acid (ABA), jasmonic acid (JA) and auxin. Ref.4
Sequence similarities	Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase type I family.
Caution	It is uncertain whether Met-1 or Met-4 is the initiator.
Sequence caution	The sequence AAD46036.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	phosphatidylinositol dephosphorylation Inferred from direct assay Ref.4. Source: TAIR phosphatidylinositol phosphorylation Inferred from electronic annotation. Source: InterPro response to abscisic acid stimulus Inferred from expression pattern Ref.4. Source: TAIR response to auxin stimulus Inferred from expression pattern Ref.4. Source: TAIR response to jasmonic acid stimulus Inferred from expression pattern Ref.4. 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 electronic annotation. Source: EC phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity Inferred from direct assay Ref.4. Source: TAIR phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity Inferred from direct assay Ref.4. Source: TAIR phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Inferred from direct assay Ref.4. Source: TAIR
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q5EAF2-1)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 334	334	Type I inositol 1,4,5-trisphosphate 5-phosphatase 11		PRO_0000209725
Regions
	Region	206 – 222	17	Catalytic 1 Potential
	Region	282 – 297	16	Catalytic 2 Potential

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 73F28B12173C772A	FASTA	334	37,580
	10 20 30 40 50 60 MPTMGNKNSM CGLKRFPNYK KSPIGSFAKN SSSHDGIKTI EAVNSCSFSR KADLCIRIIT 70 80 90 100 110 120 WNMNGNVSYE DLVELVGKER KFDLLVVGLQ EAPKANVDQL LQTASSPTHE LLGKAKLQSV 130 140 150 160 170 180 QLYLFGPKNS HTLVKELKAE RYSVGGCGGL IGRKKGAVAI RINYDDIKMV FISCHLSAHA 190 200 210 220 230 240 KKVDQRNTEL RHIANSLLPR DKRKRDLTVW LGDLNYRIQD VSNHPVRSLI QNHLQSVLVS 250 260 270 280 290 300 KDQLLQEAER GEIFKGYSEG TLGFKPTYKY NVGSSDYDTS HKIRVPAWTD RILFKIQDTD 310 320 330 NIQATLHSYD SIDQVYGSDH KPVKADLCLK WVNS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Arabidopsis ORF clones." Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Molecular characterization of an Arabidopsis gene encoding a phospholipid-specific inositol polyphosphate 5-phosphatase." Ercetin M.E., Gillaspy G.E. Plant Physiol. 135:938-946(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-334, FUNCTION, INDUCTION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC007519 Genomic DNA. Translation: AAD46036.1. Different initiation. CP002684 Genomic DNA. Translation: AEE32179.1. BT020617 mRNA. Translation: AAW81725.1. BT021928 mRNA. Translation: AAX49377.1. AY627297 mRNA. Translation: AAT45895.1.
IPI	IPI00530331.
PIR	D96515.
RefSeq	NP_175182.2. NM_103644.2.
UniGene	At.49311.
3D structure databases
ProteinModelPortal	Q5EAF2.
SMR	Q5EAF2. Positions 48-325.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q5EAF2. 1 interaction.
STRING	3702.AT1G47510.1-P.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G47510.1; AT1G47510.1; AT1G47510.
GeneID	841160.
KEGG	ath:AT1G47510.
Organism-specific databases
TAIR	At1g47510.
Phylogenomic databases
eggNOG	COG5411.
HOGENOM	HOG000005663.
InParanoid	Q5EAF2.
OMA	CHLSAHA.
PhylomeDB	Q5EAF2.
ProtClustDB	CLSN2680743.
Gene expression databases
Genevestigator	Q5EAF2.
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

IP5PB_ARATH

Accession

Primary (citable) accession number: Q5EAF2
Secondary accession number(s): Q9SX81

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	March 15, 2005
Last modified:	May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program