ID   DPNP1_ARATH             Reviewed;         353 AA.
AC   Q42546;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 74.
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-1,4-bisphosphate 1-phosphatase 1;
DE            EC=3.1.3.57;
DE   AltName: Full=Inositol polyphosphate 1-phosphatase 1;
DE            Short=IPPase 1;
DE   AltName: Full=Protein FIERY 1;
GN   Name=SAL1; Synonyms=FRY1; OrderedLocusNames=At5g63980;
GN   ORFNames=MBM17.8;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Root;
RX   MEDLINE=96361882; PubMed=8721754; DOI=10.1105/tpc.8.3.529;
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
RP   MUTANT FRY1-1.
RC   STRAIN=cv. C24;
RX   MEDLINE=21378382; 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   MEDLINE=20181125; 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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   TISSUE SPECIFICITY, AND CHARACTERIZATION.
RC   STRAIN=cv. Columbia;
RX   MEDLINE=99222627; PubMed=10205895;
RX   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-
RT   sensitive phosphatase.";
RL   Plant J. 17:373-383(1999).
RN   [6]
RP   FUNCTION.
RX   PubMed=17993620; DOI=10.1105/tpc.107.055319;
RA   Gy I., Gasciolli V., Lauressergues D., Morel J.-B., Gombert J.,
RA   Proux F., 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).
CC   -!- FUNCTION: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS)
CC       to 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
CC       role in the biosynthesis of sulfate conjugates and RNA processing.
CC       Is also able to hydrolyze inositol 1,4-bisphosphate and inositol
CC       1,3,4-trisphosphate. Could be considered as a negative regulator
CC       of abscisic acid (ABA)- and stress-responsive genes, through
CC       modulating the inositol 1,4,5-trisphosphate (IP3) turnover. Is
CC       also involved in salt tolerance. Acts as a suppressor of virus-
CC       and transgene-induced silencing.
CC   -!- CATALYTIC ACTIVITY: Adenosine 3',5'-bisphosphate + H(2)O =
CC       adenosine 5'-phosphate + phosphate.
CC   -!- CATALYTIC ACTIVITY: 1D-myo-inositol 1,4-bisphosphate + H(2)O = 1D-
CC       myo-inositol 4-phosphate + phosphate.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Inhibited by Li(+) (IC(50)=0.20 millimolar) and
CC       Na(+) (IC(50)=200 millimolar).
CC   -!- PATHWAY: Signal transduction; phosphatidylinositol signaling
CC       pathway.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC       siliques.
CC   -!- MISCELLANEOUS: Mutation in the FRY1 gene results in super-
CC       induction of abscisic acid (ABA)- and stress-responsive genes, due
CC       to inositol 1,4,5-trisphosphate (IP3) accumulation.
CC   -!- MISCELLANEOUS: Substrate preference is 3'-phosphoadenosine 5'-
CC       phosphate (PAP) = adenosine 3'-phosphate 5'-phosphosulfate (PAPS)>
CC       inositol-1,4-bisphosphate >> inositol 1,4,5-trisphosphate. No
CC       activity observed against 3' or 5'-AMP, inositol monophosphate and
CC       fructose-1,6-bisphosphate.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase family.
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DR   EMBL; U40433; AAC49263.1; -; mRNA.
DR   EMBL; AY034894; AAK58887.1; -; mRNA.
DR   EMBL; AB019227; BAA96901.1; -; Genomic_DNA.
DR   EMBL; BT005993; AAO64928.1; -; mRNA.
DR   IPI; IPI00542330; -.
DR   HSSP; P32179; 1KA1.
DR   PRIDE; Q42546; -.
DR   GenomeReviews; BA000015_GR; AT5G63980.
DR   NMPDR; fig|3702.1.peg.28453; -.
DR   GeneFarm; 2320; -.
DR   TAIR; At5g63980; -.
DR   OMA; Q42546; DGAIYLR.
DR   BRENDA; 3.1.3.57; 302.
DR   BRENDA; 3.1.3.7; 302.
DR   ArrayExpress; Q42546; -.
DR   GermOnline; AT5G63980; Arabidopsis thaliana.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IDA:TAIR.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004441; F:inositol-1,4-bisphosphate 1-phosphatase act...; IEA:EC.
DR   GO; GO:0031403; F:lithium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009738; P:abscisic acid mediated signaling; IMP:TAIR.
DR   GO; GO:0010587; P:miRNA catabolic process; IMP:TAIR.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IMP:TAIR.
DR   GO; GO:0016481; P:negative regulation of transcription; IEP:TAIR.
DR   GO; GO:0048015; P:phosphoinositide-mediated signaling; TAS:TAIR.
DR   GO; GO:0048573; P:photoperiodism, flowering; IMP:TAIR.
DR   GO; GO:0051512; P:positive regulation of unidimensional cell ...; IMP:TAIR.
DR   GO; GO:0043157; P:response to cation stress; IGI:TAIR.
DR   GO; GO:0009409; P:response to cold; IMP:TAIR.
DR   GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR   GO; GO:0006790; P:sulfur metabolic process; IGI:TAIR.
DR   InterPro; IPR006239; Bisphos_HAL2.
DR   InterPro; IPR000760; Inositol_P.
DR   PANTHER; PTHR20854; Inositol_P; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00378; INOSPHPHTASE.
DR   ProDom; PD023420; Inositol_P; 1.
DR   TIGRFAMs; TIGR01330; bisphos_HAL2; 1.
DR   PROSITE; PS00629; IMP_1; 1.
DR   PROSITE; PS00630; IMP_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Abscisic acid signaling pathway; Calcium; Complete proteome;
KW   Hydrolase; Lithium; Magnesium; Metal-binding; Multifunctional enzyme.
FT   CHAIN         1    353       SAL1 phosphatase.
FT                                /FTId=PRO_0000142530.
FT   METAL        71     71       Magnesium 1 (By similarity).
FT   METAL       134    134       Magnesium 1 (By similarity).
FT   METAL       134    134       Magnesium 2 (By similarity).
FT   METAL       136    136       Magnesium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       137    137       Magnesium 2 (By similarity).
FT   METAL       288    288       Magnesium 2 (By similarity).
FT   MUTAGEN     287    353       Missing: In fry1-1; abolishes activity.
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
//