Reviewed, UniProtKB/Swiss-Prot Q42546 (DPNP1_ARATH)

Names and origin

Protein names

Recommended name:
    SAL1 phosphatase
Alternative name(s):
    3'(2'),5'-bisphosphate nucleotidase 1
    EC=3.1.3.7
    3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase 1
    DPNPase 1
    Inositol-1,4-bisphosphate 1-phosphatase 1
    EC=3.1.3.57
    Inositol polyphosphate 1-phosphatase 1
      Short name=IPPase 1
    Protein FIERY 1

Gene names

Name:	SAL1
Synonyms:	FRY1
Ordered Locus Names:	At5g63980
ORF Names:	MBM17.8

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	353 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. May regulate the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS. May play a role in the biosynthesis of sulfate conjugates and RNA processing. Is also able to hydrolyze inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate. Could be considered as a negative regulator of abscisic acid (ABA)- and stress-responsive genes, through modulating the inositol 1,4,5-trisphosphate (IP3) turnover. Is also involved in salt tolerance. Acts as a suppressor of virus- and transgene-induced silencing. Ref.1 Ref.2 Ref.6
Catalytic activity	Adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate. 1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate.
Cofactor	Magnesium.
Enzyme regulation	Inhibited by Li+ (IC50=0.20 millimolar) and Na+ (IC50=200 millimolar).
Pathway	Signal transduction; phosphatidylinositol signaling pathway.
Tissue specificity	Expressed in roots, leaves, stems, flowers and siliques. Ref.2 Ref.5
Miscellaneous	Mutation in the FRY1 gene results in super-induction of abscisic acid (ABA)- and stress-responsive genes, due to inositol 1,4,5-trisphosphate (IP3) accumulation. Substrate preference is 3'-phosphoadenosine 5'-phosphate (PAP) = adenosine 3'-phosphate 5'-phosphosulfate (PAPS)> inositol-1,4-bisphosphate >> inositol 1,4,5-trisphosphate. No activity observed against 3' or 5'-AMP, inositol monophosphate and fructose-1,6-bisphosphate.
Sequence similarities	Belongs to the inositol monophosphatase family.

Ontologies

Keywords
Biological process	Abscisic acid signaling pathway
Ligand	Calcium Lithium Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	abscisic acid mediated signaling Ref.2 Inferred from mutant phenotype. Source: TAIR miRNA catabolic process Ref.6 Inferred from mutant phenotype. Source: TAIR negative regulation of signal transduction Inferred from mutant phenotype. Source: TAIR negative regulation of transcription Inferred from expression pattern. Source: TAIR phosphoinositide-mediated signaling Ref.1 Traceable author statement. Source: TAIR photoperiodism, flowering Inferred from mutant phenotype. Source: TAIR positive regulation of unidimensional cell growth Inferred from mutant phenotype. Source: TAIR response to cation stress Ref.1 Inferred from genetic interaction. Source: TAIR response to cold Inferred from mutant phenotype. Source: TAIR response to water deprivation Inferred from mutant phenotype. Source: TAIR sulfur metabolic process Ref.1 Inferred from genetic interaction. Source: TAIR
Cellular component	chloroplast stroma Inferred from direct assay. Source: TAIR nucleus Inferred from direct assay. Source: TAIR
Molecular function	3'(2'),5'-bisphosphate nucleotidase activity Ref.1 Inferred from direct assay. Source: TAIR calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW inositol-1,4-bisphosphate 1-phosphatase activity Inferred from electronic annotation. Source: EC lithium ion binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 353	353	SAL1 phosphatase		PRO_0000142530
Sites
	Metal binding	71	1	Magnesium 1 By similarity
	Metal binding	134	1	Magnesium 1 By similarity
	Metal binding	134	1	Magnesium 2 By similarity
	Metal binding	136	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	137	1	Magnesium 2 By similarity
	Metal binding	288	1	Magnesium 2 By similarity
Experimental info
	Mutagenesis	287 – 353	67	Missing in fry1-1; abolishes activity.

Sequences

	Sequence		Length	Mass (Da)
	Q42546-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 351EBB6826B93A4A	FASTA	353	37,564
	10 20 30 40 50 60 MAYEKELDAA KKAASLAARL CQKVQKALLQ SDVQSKSDKS PVTVADYGSQ AVVSLVLEKE 70 80 90 100 110 120 LSSEPFSLVA EEDSGDLRKD GSQDTLERIT KLVNDTLATE ESFNGSTLST DDLLRAIDCG 130 140 150 160 170 180 TSEGGPNGRH WVLDPIDGTK GFLRGDQYAV ALGLLEEGKV VLGVLACPNL PLASIAGNNK 190 200 210 220 230 240 NKSSSDEIGC LFFATIGSGT YMQLLDSKSS PVKVQVSSVE NPEEASFFES FEGAHSLHDL 250 260 270 280 290 300 SSSIANKLGV KAPPVRIDSQ AKYGALSRGD GAIYLRFPHK GYREKIWDHV AGAIVVTEAG 310 320 330 340 350 GIVTDAAGKP LDFSKGKYLD LDTGIIVANE KLMPLLLKAV RDSIAEQEKA SAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The SAL1 gene of Arabidopsis, encoding an enzyme with 3'(2'),5'-bisphosphate nucleotidase and inositol polyphosphate 1-phosphatase activities, increases salt tolerance in yeast." Quintero F.J., Garciadeblas B., Rodriguez-Navarro A. Plant Cell 8:529-537(1996) [PubMed: 8721754] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Tissue: Root.
[2]	"FIERY1 encoding an inositol polyphosphate 1-phosphatase is a negative regulator of abscisic acid and stress signaling in Arabidopsis." Xiong L., Lee B.-H., Ishitani M., Lee H., Zhang C., Zhu J.-K. Genes Dev. 15:1971-1984(2001) [PubMed: 11485991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, FUNCTION, MUTANT FRY1-1. Strain: cv. C24.
[3]	"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones." Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S. DNA Res. 7:31-63(2000) [PubMed: 10718197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"The Arabidopsis HAL2-like gene family includes a novel sodium-sensitive phosphatase." Gil-Mascarell R., Lopez-Coronado J.M., Belles J.M., Serrano R., Rodriguez P.L. Plant J. 17:373-383(1999) [PubMed: 10205895] [Abstract] Cited for: TISSUE SPECIFICITY, CHARACTERIZATION. Strain: cv. Columbia.
[6]	"Arabidopsis FIERY1, XRN2, and XRN3 are endogenous RNA silencing suppressors." Gy I., Gasciolli V., Lauressergues D., Morel J.-B., Gombert J., Proux F., Proux C., Vaucheret H., Mallory A.C. Plant Cell 19:3451-3461(2007) [PubMed: 17993620] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U40433 mRNA. Translation: AAC49263.1. AY034894 mRNA. Translation: AAK58887.1. AB019227 Genomic DNA. Translation: BAA96901.1. BT005993 mRNA. Translation: AAO64928.1.
IPI	IPI00542330.
3D structure databases
HSSP	HSSP built from PDB template 1KA1 based on UniProtKB P32179.
ModBase	Search...
Proteomic databases
PRIDE	Q42546.
Genome annotation databases
GenomeReviews	Gene locus AT5G63980 in contig BA000015_GR.
NMPDR	fig|3702.1.peg.28453.
Organism-specific databases
GeneFarm	2320.
TAIR	At5g63980.
Phylogenomic databases
OMA	Q42546. DGAIYLR.
Enzyme and pathway databases
BRENDA	3.1.3.57. 302. 3.1.3.7. 302.
Gene expression databases
ArrayExpress	Q42546.
GermOnline	AT5G63980. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR006239. Bisphos_HAL2. IPR000760. Inositol_P. [Graphical view]
PANTHER	PTHR20854. Inositol_P. 1 hit.
Pfam	PF00459. Inositol_P. 1 hit. [Graphical view]
PRINTS	PR00378. INOSPHPHTASE.
ProDom	PD023420. Inositol_P. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01330. bisphos_HAL2. 1 hit.
PROSITE	PS00629. IMP_1. 1 hit. PS00630. IMP_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DPNP1_ARATH

Accession

Primary (citable) accession number: Q42546

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)