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Q42546 (DPNP1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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 polyphosphate 1-phosphatase 1
Short name=IPPase 1
Inositol-1,4-bisphosphate 1-phosphatase 1
EC=3.1.3.57
Protein FIERY 1
Gene names
Name:SAL1
Synonyms:FRY1
Ordered Locus Names:At5g63980
ORF Names:MBM17.8
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processAbscisic acid signaling pathway
   LigandCalcium
Lithium
Magnesium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological processabscisic acid mediated signaling pathway

Inferred from mutant phenotype Ref.2. Source: TAIR

miRNA catabolic process

Inferred from mutant phenotype Ref.6. Source: TAIR

negative regulation of signal transduction

Inferred from mutant phenotype. Source: TAIR

negative regulation of transcription, DNA-dependent

Inferred from expression pattern. Source: TAIR

phosphatidylinositol-mediated signaling

Traceable author statement Ref.1. Source: TAIR

photoperiodism, flowering

Inferred from mutant phenotype. Source: TAIR

positive regulation of unidimensional cell growth

Inferred from mutant phenotype. Source: TAIR

regulation of jasmonic acid biosynthetic process

Inferred from mutant phenotype. Source: TAIR

response to cation stress

Inferred from genetic interaction Ref.1. Source: TAIR

response to cold

Inferred from mutant phenotype. Source: TAIR

response to water deprivation

Inferred from mutant phenotype. Source: TAIR

sulfur compound metabolic process

Inferred from genetic interaction Ref.1. Source: TAIR

   Cellular componentchloroplast stroma

Inferred from direct assay. Source: TAIR

cytosol

Inferred from direct assay. Source: TAIR

nucleus

Inferred from direct assay. Source: TAIR

   Molecular function3'(2'),5'-bisphosphate nucleotidase activity

Inferred from direct assay Ref.1. Source: TAIR

inositol-1,4-bisphosphate 1-phosphatase activity

Inferred from direct assay Ref.1. Source: TAIR

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide phosphatase activity

Inferred from direct assay. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 353353SAL1 phosphatase
PRO_0000142530

Regions

Region136 – 1394Substrate binding By similarity

Sites

Metal binding711Magnesium 1 By similarity
Metal binding1341Magnesium 1 By similarity
Metal binding1341Magnesium 2 By similarity
Metal binding1361Magnesium 1; via carbonyl oxygen By similarity
Metal binding1371Magnesium 2 By similarity
Metal binding2881Magnesium 2 By similarity
Binding site711Substrate By similarity
Binding site2881Substrate By similarity

Experimental info

Mutagenesis287 – 35367Missing in fry1-1; abolishes activity.

Sequences

Sequence LengthMass (Da)Tools
Q42546 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 351EBB6826B93A4A

FASTA35337,564
        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 

« Hide

References

« Hide '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. 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: 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U40433 mRNA. Translation: AAC49263.1.
AY034894 mRNA. Translation: AAK58887.1.
AB019227 Genomic DNA. Translation: BAA96901.1.
BT005993 mRNA. Translation: AAO64928.1.
IPIIPI00542330.

3D structure databases

ProteinModelPortalQ42546.
SMRQ42546. Positions 2-347.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ42546.

Proteomic databases

PRIDEQ42546.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GenomeReviewsGene locus AT5G63980 in contig BA000015_GR.
NMPDRfig|3702.1.peg.28453.

Organism-specific databases

GeneFarm2320.
TAIRAt5g63980.

Phylogenomic databases

GeneTreeEPGT00070000029602.
HOGENOMHBG599916.
InParanoidQ42546.
OMAHAAGCIV.
PhylomeDBQ42546.

Gene expression databases

ArrayExpressQ42546.
GenevestigatorQ42546.
GermOnlineAT5G63980. Arabidopsis thaliana.

Family and domain databases

InterProIPR006239. Bisphos_HAL2.
IPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
[Graphical view]
PANTHERPTHR20854. Inositol_P. 1 hit.
PfamPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSPR00377. IMPHPHTASES.
TIGRFAMsTIGR01330. Bisphos_HAL2. 1 hit.
PROSITEPS00629. IMP_1. 1 hit.
PS00630. IMP_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDPNP1_ARATH
AccessionPrimary (citable) accession number: Q42546
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: November 16, 2011
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families