DPNP1_ARATH
ID DPNP1_ARATH Reviewed; 353 AA.
AC Q42546; F4KC73; Q0WTT5;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=SAL1 phosphatase;
DE AltName: Full=3'(2'),5'-bisphosphate nucleotidase 1;
DE EC=3.1.3.7;
DE AltName: Full=3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase 1;
DE AltName: Full=DPNPase 1;
DE AltName: Full=Inositol polyphosphate 1-phosphatase 1;
DE Short=IPPase 1;
DE AltName: Full=Inositol-1,4-bisphosphate 1-phosphatase 1;
DE EC=3.1.3.57;
DE AltName: Full=Protein FIERY 1;
GN Name=SAL1; Synonyms=FRY1; OrderedLocusNames=At5g63980; ORFNames=MBM17.8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Root;
RX PubMed=8721754; DOI=10.2307/3870330;
RA Quintero F.J., Garciadeblas B., Rodriguez-Navarro A.;
RT "The SAL1 gene of Arabidopsis, encoding an enzyme with 3'(2'),5'-
RT bisphosphate nucleotidase and inositol polyphosphate 1-phosphatase
RT activities, increases salt tolerance in yeast.";
RL Plant Cell 8:529-537(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, FUNCTION, AND MUTANT
RP FRY1-1.
RC STRAIN=cv. C24;
RX PubMed=11485991; DOI=10.1101/gad.891901;
RA Xiong L., Lee B.-H., Ishitani M., Lee H., Zhang C., Zhu J.-K.;
RT "FIERY1 encoding an inositol polyphosphate 1-phosphatase is a negative
RT regulator of abscisic acid and stress signaling in Arabidopsis.";
RL Genes Dev. 15:1971-1984(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP TISSUE SPECIFICITY, AND CHARACTERIZATION.
RC STRAIN=cv. Columbia;
RX PubMed=10205895; DOI=10.1046/j.1365-313x.1999.00385.x;
RA Gil-Mascarell R., Lopez-Coronado J.M., Belles J.M., Serrano R.,
RA Rodriguez P.L.;
RT "The Arabidopsis HAL2-like gene family includes a novel sodium-sensitive
RT phosphatase.";
RL Plant J. 17:373-383(1999).
RN [8]
RP FUNCTION.
RX PubMed=17993620; DOI=10.1105/tpc.107.055319;
RA Gy I., Gasciolli V., Lauressergues D., Morel J.-B., Gombert J., Proux F.,
RA Proux C., Vaucheret H., Mallory A.C.;
RT "Arabidopsis FIERY1, XRN2, and XRN3 are endogenous RNA silencing
RT suppressors.";
RL Plant Cell 19:3451-3461(2007).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 1-346.
RX PubMed=27432987; DOI=10.1073/pnas.1604936113;
RA Chan K.X., Mabbitt P.D., Phua S.Y., Mueller J.W., Nisar N.,
RA Gigolashvili T., Stroeher E., Grassl J., Arlt W., Estavillo G.M.,
RA Jackson C.J., Pogson B.J.;
RT "Sensing and signaling of oxidative stress in chloroplasts by inactivation
RT of the SAL1 phosphoadenosine phosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E4567-E4576(2016).
CC -!- FUNCTION: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to
CC adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine
CC 5'- phosphate (PAP) to AMP. May regulate the flux of sulfur in the
CC sulfur-activation pathway by converting PAPS to APS. May play a role in
CC the biosynthesis of sulfate conjugates and RNA processing. Is also able
CC to hydrolyze inositol 1,4-bisphosphate and inositol 1,3,4-
CC trisphosphate. Could be considered as a negative regulator of abscisic
CC acid (ABA)- and stress-responsive genes, through modulating the
CC inositol 1,4,5-trisphosphate (IP3) turnover. Is also involved in salt
CC tolerance. Acts as a suppressor of virus- and transgene-induced
CC silencing. {ECO:0000269|PubMed:11485991, ECO:0000269|PubMed:17993620,
CC ECO:0000269|PubMed:8721754}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate;
CC Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-
CC phosphate + phosphate; Xref=Rhea:RHEA:15553, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58282, ChEBI:CHEBI:58469; EC=3.1.3.57;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Inhibited by Li(+) (IC(50)=0.20 millimolar) and
CC Na(+) (IC(50)=200 millimolar).
CC -!- PATHWAY: Signal transduction; phosphatidylinositol signaling pathway.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. {ECO:0000269|PubMed:10205895, ECO:0000269|PubMed:11485991}.
CC -!- MISCELLANEOUS: Mutation in the FRY1 gene results in super-induction of
CC abscisic acid (ABA)- and stress-responsive genes, due to inositol
CC 1,4,5-trisphosphate (IP3) accumulation.
CC -!- MISCELLANEOUS: Substrate preference is 3'-phosphoadenosine 5'-phosphate
CC (PAP) = adenosine 3'-phosphate 5'-phosphosulfate (PAPS)> inositol 1,4-
CC bisphosphate >> inositol 1,4,5-trisphosphate. No activity observed
CC against 3' or 5'-AMP, inositol monophosphate and fructose-1,6-
CC bisphosphate.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U40433; AAC49263.1; -; mRNA.
DR EMBL; AY034894; AAK58887.1; -; mRNA.
DR EMBL; AB019227; BAA96901.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97825.2; -; Genomic_DNA.
DR EMBL; BT005993; AAO64928.1; -; mRNA.
DR EMBL; AK227460; BAE99463.1; -; mRNA.
DR RefSeq; NP_201203.3; NM_125794.5.
DR PDB; 5ESY; X-ray; 3.05 A; A/B=1-346.
DR PDBsum; 5ESY; -.
DR AlphaFoldDB; Q42546; -.
DR SMR; Q42546; -.
DR BioGRID; 21761; 6.
DR STRING; 3702.AT5G63980.1; -.
DR PaxDb; Q42546; -.
DR PRIDE; Q42546; -.
DR ProteomicsDB; 220401; -.
DR EnsemblPlants; AT5G63980.1; AT5G63980.1; AT5G63980.
DR GeneID; 836519; -.
DR Gramene; AT5G63980.1; AT5G63980.1; AT5G63980.
DR KEGG; ath:AT5G63980; -.
DR Araport; AT5G63980; -.
DR eggNOG; KOG1528; Eukaryota.
DR HOGENOM; CLU_033446_2_1_1; -.
DR InParanoid; Q42546; -.
DR OMA; MSYQQER; -.
DR OrthoDB; 1096950at2759; -.
DR PhylomeDB; Q42546; -.
DR BioCyc; ARA:AT5G63980-MON; -.
DR BRENDA; 3.1.3.57; 399.
DR BRENDA; 3.1.3.7; 399.
DR UniPathway; UPA00944; -.
DR PRO; PR:Q42546; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q42546; baseline and differential.
DR Genevisible; Q42546; AT.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IBA:GO_Central.
DR GO; GO:0004441; F:inositol-1,4-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042578; F:phosphoric ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
DR InterPro; IPR006239; Bisphos_HAL2.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR TIGRFAMs; TIGR01330; bisphos_HAL2; 1.
DR PROSITE; PS00629; IMP_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Abscisic acid signaling pathway; Calcium; Hydrolase; Lithium;
KW Magnesium; Metal-binding; Multifunctional enzyme; Reference proteome.
FT CHAIN 1..353
FT /note="SAL1 phosphatase"
FT /id="PRO_0000142530"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 136..139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 287..353
FT /note="Missing: In fry1-1; abolishes activity."
FT HELIX 4..22
FT /evidence="ECO:0007829|PDB:5ESY"
FT HELIX 44..60
FT /evidence="ECO:0007829|PDB:5ESY"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:5ESY"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:5ESY"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:5ESY"
FT TURN 139..144
FT /evidence="ECO:0007829|PDB:5ESY"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:5ESY"
FT STRAND 159..169
FT /evidence="ECO:0007829|PDB:5ESY"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:5ESY"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:5ESY"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:5ESY"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:5ESY"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:5ESY"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:5ESY"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:5ESY"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:5ESY"
FT HELIX 262..268
FT /evidence="ECO:0007829|PDB:5ESY"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:5ESY"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:5ESY"
FT HELIX 290..297
FT /evidence="ECO:0007829|PDB:5ESY"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:5ESY"
FT STRAND 302..308
FT /evidence="ECO:0007829|PDB:5ESY"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:5ESY"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:5ESY"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:5ESY"
SQ SEQUENCE 353 AA; 37564 MW; 351EBB6826B93A4A CRC64;
MAYEKELDAA KKAASLAARL CQKVQKALLQ SDVQSKSDKS PVTVADYGSQ AVVSLVLEKE
LSSEPFSLVA EEDSGDLRKD GSQDTLERIT KLVNDTLATE ESFNGSTLST DDLLRAIDCG
TSEGGPNGRH WVLDPIDGTK GFLRGDQYAV ALGLLEEGKV VLGVLACPNL PLASIAGNNK
NKSSSDEIGC LFFATIGSGT YMQLLDSKSS PVKVQVSSVE NPEEASFFES FEGAHSLHDL
SSSIANKLGV KAPPVRIDSQ AKYGALSRGD GAIYLRFPHK GYREKIWDHV AGAIVVTEAG
GIVTDAAGKP LDFSKGKYLD LDTGIIVANE KLMPLLLKAV RDSIAEQEKA SAL
