DPNP2_ARATH
ID DPNP2_ARATH Reviewed; 347 AA.
AC O49623;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=SAL2 phosphatase {ECO:0000303|PubMed:10205895};
DE AltName: Full=3'(2'),5'-bisphosphate nucleotidase 2 {ECO:0000305};
DE EC=3.1.3.7 {ECO:0000269|PubMed:10205895};
DE AltName: Full=3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase 2 {ECO:0000305};
DE AltName: Full=DPNPase 2 {ECO:0000305};
DE AltName: Full=Inositol polyphosphate 1-phosphatase 2 {ECO:0000305};
DE Short=IPPase 2 {ECO:0000305};
DE AltName: Full=Inositol-1,4-bisphosphate 1-phosphatase 2 {ECO:0000305};
DE EC=3.1.3.57 {ECO:0000269|PubMed:10205895};
GN Name=SAL2 {ECO:0000303|PubMed:10205895};
GN OrderedLocusNames=At5g64000 {ECO:0000312|Araport:AT5G64000};
GN ORFNames=MBM17.10 {ECO:0000312|EMBL:BAA96903.1};
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], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND COFACTOR.
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 [2]
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 [3]
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 [4]
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).
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 (PubMed:10205895)
CC (By similarity). Prevents both the toxicity of PAP on RNA processing
CC enzymes as well as the product inhibition by PAP of sulfate
CC conjugation. Is also able to hydrolyze inositol 1,4-bisphosphate
CC (PubMed:10205895). {ECO:0000250|UniProtKB:Q42546,
CC ECO:0000269|PubMed:10205895}.
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 Evidence={ECO:0000269|PubMed:10205895};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10041;
CC Evidence={ECO:0000269|PubMed:10205895};
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 Evidence={ECO:0000269|PubMed:10205895};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15554;
CC Evidence={ECO:0000269|PubMed:10205895};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:10205895};
CC -!- ACTIVITY REGULATION: Inhibited by Li(+) (IC(50)=10 millimolar), Na(+)
CC (IC(50)=200 millimolar) and Ca(2+) (IC(50)=0.03 millimolar).
CC {ECO:0000269|PubMed:10205895}.
CC -!- PATHWAY: Signal transduction; phosphatidylinositol signaling pathway.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Very low expression in roots, leaves, stems,
CC flowers and siliques. {ECO:0000269|PubMed:10205895}.
CC -!- MISCELLANEOUS: Substrate preference is 3'-phosphoadenosine 5'-phosphate
CC (PAP) > adenosine 3'-phosphate 5'-phosphosulfate (PAPS)>> inositol 1,4-
CC bisphosphate. No activity observed against 3' or 5'-AMP, inositol
CC monophosphate and fructose-1,6-bisphosphate.
CC {ECO:0000269|PubMed:10205895}.
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; Z83312; CAB05889.1; -; mRNA.
DR EMBL; AB019227; BAA96903.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97828.1; -; Genomic_DNA.
DR EMBL; AY070383; AAL49879.1; -; mRNA.
DR EMBL; AY096575; AAM20225.1; -; mRNA.
DR RefSeq; NP_201205.1; NM_125796.5.
DR AlphaFoldDB; O49623; -.
DR SMR; O49623; -.
DR STRING; 3702.AT5G64000.1; -.
DR PaxDb; O49623; -.
DR PRIDE; O49623; -.
DR ProteomicsDB; 220402; -.
DR EnsemblPlants; AT5G64000.1; AT5G64000.1; AT5G64000.
DR GeneID; 836521; -.
DR Gramene; AT5G64000.1; AT5G64000.1; AT5G64000.
DR KEGG; ath:AT5G64000; -.
DR Araport; AT5G64000; -.
DR TAIR; locus:2160836; AT5G64000.
DR eggNOG; KOG1528; Eukaryota.
DR HOGENOM; CLU_033446_2_1_1; -.
DR InParanoid; O49623; -.
DR OMA; ETHNRNC; -.
DR OrthoDB; 1096950at2759; -.
DR PhylomeDB; O49623; -.
DR BioCyc; ARA:AT5G64000-MON; -.
DR UniPathway; UPA00944; -.
DR PRO; PR:O49623; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O49623; baseline and differential.
DR Genevisible; O49623; AT.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IDA:TAIR.
DR GO; GO:0016312; F:inositol bisphosphate phosphatase activity; IDA:TAIR.
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: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 TIGRFAMs; TIGR01330; bisphos_HAL2; 1.
DR PROSITE; PS00629; IMP_1; 1.
PE 1: Evidence at protein level;
KW Calcium; Hydrolase; Lithium; Magnesium; Metal-binding;
KW Multifunctional enzyme; Reference proteome.
FT CHAIN 1..347
FT /note="SAL2 phosphatase"
FT /id="PRO_0000142531"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 136..139
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21327"
SQ SEQUENCE 347 AA; 37509 MW; 7F82E8EB4FAAF8FE CRC64;
MSYEKELAAA KKAVTLAARL SQEVQKTLLQ SQVWKKSDRS PVTAADYGSQ AVVSLVLERE
LQPDKLSLVA EEETGDLRKN GSEAFLEDIA KLVKDTLASE ESYTSSPLST DDVLNAIDCG
KSEGGCKGSH WVLDPIDGTR GFVRGEQYAV GLALLVEGKV VLGVMACPNL PLASAVCATD
NSSQEDVGCL FFATTGSGTY VQSLKGNSLP QKVQVSSNEN LDEAKFLESY HKPIPIHGTI
AKKLGIKALP VRIDSQAKYA ALSRGDAEIY LRFTLNGYRE CIWDHAPGSI ITTEAGGVVC
DATGKSLDFS KGKYLAHKTG IIVTTKKLKP WILKAVRESI EEENLYF
