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Protein

SAL1 phosphatase

Gene

SAL1

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

Functioni

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.3 Publications

Catalytic activityi

Adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.
1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate.

Cofactori

Enzyme regulationi

Inhibited by Li+ (IC50=0.20 millimolar) and Na+ (IC50=200 millimolar).

Pathwayi: phosphatidylinositol signaling pathway

This protein is involved in the pathway phosphatidylinositol signaling pathway, which is part of Signal transduction.
View all proteins of this organism that are known to be involved in the pathway phosphatidylinositol signaling pathway and in Signal transduction.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi71Magnesium 1By similarity1
Binding sitei71SubstrateBy similarity1
Metal bindingi134Magnesium 1By similarity1
Metal bindingi134Magnesium 2By similarity1
Metal bindingi136Magnesium 1; via carbonyl oxygenBy similarity1
Metal bindingi137Magnesium 2By similarity1
Metal bindingi288Magnesium 2By similarity1
Binding sitei288SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Abscisic acid signaling pathway

Keywords - Ligandi

Calcium, Lithium, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT5G63980-MONOMER.
BRENDAi3.1.3.31. 399.
3.1.3.57. 399.
3.1.3.7. 399.
UniPathwayiUPA00944.

Names & Taxonomyi

Protein namesi
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 polyphosphate 1-phosphatase 1
Short name:
IPPase 1
Inositol-1,4-bisphosphate 1-phosphatase 1 (EC:3.1.3.57)
Protein FIERY 1
Gene namesi
Name:SAL1
Synonyms:FRY1
Ordered Locus Names:At5g63980
ORF Names:MBM17.8
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G63980.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi287 – 353Missing in fry1-1; abolishes activity. Add BLAST67

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001425301 – 353SAL1 phosphataseAdd BLAST353

Proteomic databases

PaxDbiQ42546.
PRIDEiQ42546.

Expressioni

Tissue specificityi

Expressed in roots, leaves, stems, flowers and siliques.2 Publications

Gene expression databases

GenevisibleiQ42546. AT.

Interactioni

Protein-protein interaction databases

BioGridi21761. 6 interactors.
MINTiMINT-8067043.
STRINGi3702.AT5G63980.1.

Structurei

Secondary structure

1353
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 22Combined sources19
Helixi44 – 60Combined sources17
Helixi83 – 89Combined sources7
Helixi110 – 118Combined sources9
Beta strandi128 – 135Combined sources8
Turni139 – 144Combined sources6
Beta strandi150 – 156Combined sources7
Beta strandi159 – 169Combined sources11
Beta strandi190 – 195Combined sources6
Turni196 – 198Combined sources3
Beta strandi199 – 203Combined sources5
Turni205 – 207Combined sources3
Beta strandi227 – 229Combined sources3
Beta strandi233 – 235Combined sources3
Beta strandi241 – 243Combined sources3
Helixi244 – 247Combined sources4
Helixi262 – 268Combined sources7
Beta strandi272 – 276Combined sources5
Turni287 – 289Combined sources3
Helixi290 – 297Combined sources8
Turni298 – 300Combined sources3
Beta strandi302 – 308Combined sources7
Beta strandi325 – 328Combined sources4
Beta strandi330 – 334Combined sources5
Helixi335 – 339Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5ESYX-ray3.05A/B1-346[»]
ProteinModelPortaliQ42546.
SMRiQ42546.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni136 – 139Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the inositol monophosphatase family.Curated

Phylogenomic databases

eggNOGiKOG1528. Eukaryota.
COG1218. LUCA.
HOGENOMiHOG000170673.
InParanoidiQ42546.
KOiK15422.
OrthoDBiEOG09360EFU.
PhylomeDBiQ42546.

Family and domain databases

InterProiIPR006239. Bisphos_HAL2.
IPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase-like.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 3 hits.
PfamiPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSiPR00377. IMPHPHTASES.
TIGRFAMsiTIGR01330. bisphos_HAL2. 1 hit.
PROSITEiPS00629. IMP_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q42546-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYEKELDAA KKAASLAARL CQKVQKALLQ SDVQSKSDKS PVTVADYGSQ
60 70 80 90 100
AVVSLVLEKE LSSEPFSLVA EEDSGDLRKD GSQDTLERIT KLVNDTLATE
110 120 130 140 150
ESFNGSTLST DDLLRAIDCG TSEGGPNGRH WVLDPIDGTK GFLRGDQYAV
160 170 180 190 200
ALGLLEEGKV VLGVLACPNL PLASIAGNNK NKSSSDEIGC LFFATIGSGT
210 220 230 240 250
YMQLLDSKSS PVKVQVSSVE NPEEASFFES FEGAHSLHDL SSSIANKLGV
260 270 280 290 300
KAPPVRIDSQ AKYGALSRGD GAIYLRFPHK GYREKIWDHV AGAIVVTEAG
310 320 330 340 350
GIVTDAAGKP LDFSKGKYLD LDTGIIVANE KLMPLLLKAV RDSIAEQEKA

SAL
Length:353
Mass (Da):37,564
Last modified:November 1, 1996 - v1
Checksum:i351EBB6826B93A4A
GO

Sequence cautioni

The sequence AED97825 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40433 mRNA. Translation: AAC49263.1.
AY034894 mRNA. Translation: AAK58887.1.
AB019227 Genomic DNA. Translation: BAA96901.1.
CP002688 Genomic DNA. Translation: AED97825.1. Different initiation.
BT005993 mRNA. Translation: AAO64928.1.
AK227460 mRNA. Translation: BAE99463.1.
RefSeqiNP_201203.3. NM_125794.5.
UniGeneiAt.9555.

Genome annotation databases

EnsemblPlantsiAT5G63980.1; AT5G63980.1; AT5G63980.
GeneIDi836519.
GrameneiAT5G63980.1; AT5G63980.1; AT5G63980.
KEGGiath:AT5G63980.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40433 mRNA. Translation: AAC49263.1.
AY034894 mRNA. Translation: AAK58887.1.
AB019227 Genomic DNA. Translation: BAA96901.1.
CP002688 Genomic DNA. Translation: AED97825.1. Different initiation.
BT005993 mRNA. Translation: AAO64928.1.
AK227460 mRNA. Translation: BAE99463.1.
RefSeqiNP_201203.3. NM_125794.5.
UniGeneiAt.9555.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5ESYX-ray3.05A/B1-346[»]
ProteinModelPortaliQ42546.
SMRiQ42546.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi21761. 6 interactors.
MINTiMINT-8067043.
STRINGi3702.AT5G63980.1.

Proteomic databases

PaxDbiQ42546.
PRIDEiQ42546.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G63980.1; AT5G63980.1; AT5G63980.
GeneIDi836519.
GrameneiAT5G63980.1; AT5G63980.1; AT5G63980.
KEGGiath:AT5G63980.

Organism-specific databases

TAIRiAT5G63980.

Phylogenomic databases

eggNOGiKOG1528. Eukaryota.
COG1218. LUCA.
HOGENOMiHOG000170673.
InParanoidiQ42546.
KOiK15422.
OrthoDBiEOG09360EFU.
PhylomeDBiQ42546.

Enzyme and pathway databases

UniPathwayiUPA00944.
BioCyciARA:AT5G63980-MONOMER.
BRENDAi3.1.3.31. 399.
3.1.3.57. 399.
3.1.3.7. 399.

Miscellaneous databases

PROiQ42546.

Gene expression databases

GenevisibleiQ42546. AT.

Family and domain databases

InterProiIPR006239. Bisphos_HAL2.
IPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase-like.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 3 hits.
PfamiPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSiPR00377. IMPHPHTASES.
TIGRFAMsiTIGR01330. bisphos_HAL2. 1 hit.
PROSITEiPS00629. IMP_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDPNP1_ARATH
AccessioniPrimary (citable) accession number: Q42546
Secondary accession number(s): F4KC73, Q0WTT5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.