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Probable SAL3 phosphatase (3'(2'),5'-bisphosphate nucleotidase 3) (EC 3.1.3.7) (3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase 3) (DPNPase 3) (Inositol polyphosphate 1-phosphatase 3) (IPPase 3) (Inositol-1,4-bisphosphate 1-phosphatase 3) (EC 3.1.3.57)

 DPNP3_ARATH             Reviewed;         357 AA.
Q8GY63; Q8L8N7; Q9LVN5;
29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
23-MAY-2018, entry version 115.
RecName: Full=Probable SAL3 phosphatase;
AltName: Full=3'(2'),5'-bisphosphate nucleotidase 3;
EC=3.1.3.7;
AltName: Full=3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase 3;
AltName: Full=DPNPase 3;
AltName: Full=Inositol polyphosphate 1-phosphatase 3;
Short=IPPase 3;
AltName: Full=Inositol-1,4-bisphosphate 1-phosphatase 3;
EC=3.1.3.57;
Name=SAL3; OrderedLocusNames=At5g63990; ORFNames=MBM17.9;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10718197; DOI=10.1093/dnares/7.1.31;
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
Tabata S.;
"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.";
DNA Res. 7:31-63(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=11910074; DOI=10.1126/science.1071006;
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.,
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS)
to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine
5'- phosphate (PAP) to AMP. Is also able to hydrolyze inositol
1,4-bisphosphate. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Adenosine 3',5'-bisphosphate + H(2)O =
adenosine 5'-phosphate + phosphate.
-!- CATALYTIC ACTIVITY: 1D-myo-inositol 1,4-bisphosphate + H(2)O = 1D-
myo-inositol 4-phosphate + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- PATHWAY: Signal transduction; phosphatidylinositol signaling
pathway.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=Q8GY63-1; Sequence=Displayed;
-!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA96902.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB019227; BAA96902.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002688; AED97827.1; -; Genomic_DNA.
EMBL; AK117842; BAC42483.1; -; mRNA.
EMBL; BT006247; AAP12896.1; -; mRNA.
EMBL; AY088896; AAM67202.1; -; mRNA.
RefSeq; NP_568983.1; NM_125795.5. [Q8GY63-1]
UniGene; At.28970; -.
ProteinModelPortal; Q8GY63; -.
STRING; 3702.AT5G63990.1; -.
PaxDb; Q8GY63; -.
PRIDE; Q8GY63; -.
EnsemblPlants; AT5G63990.1; AT5G63990.1; AT5G63990. [Q8GY63-1]
GeneID; 836520; -.
Gramene; AT5G63990.1; AT5G63990.1; AT5G63990. [Q8GY63-1]
KEGG; ath:AT5G63990; -.
Araport; AT5G63990; -.
TAIR; locus:2160831; AT5G63990.
eggNOG; KOG1528; Eukaryota.
eggNOG; COG1218; LUCA.
HOGENOM; HOG000170673; -.
InParanoid; Q8GY63; -.
KO; K15422; -.
OMA; VTDVWNK; -.
OrthoDB; EOG09360EFU; -.
PhylomeDB; Q8GY63; -.
BioCyc; ARA:AT5G63990-MONOMER; -.
UniPathway; UPA00944; -.
PRO; PR:Q8GY63; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q8GY63; baseline and differential.
Genevisible; Q8GY63; AT.
GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:UniProtKB-EC.
GO; GO:0004441; F:inositol-1,4-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
GO; GO:0006790; P:sulfur compound metabolic process; IEA:InterPro.
InterPro; IPR006239; Bisphos_HAL2.
InterPro; IPR000760; Inositol_monophosphatase-like.
Pfam; PF00459; Inositol_P; 1.
TIGRFAMs; TIGR01330; bisphos_HAL2; 1.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Hydrolase; Magnesium;
Metal-binding; Multifunctional enzyme; Reference proteome.
CHAIN 1 357 Probable SAL3 phosphatase.
/FTId=PRO_0000142532.
REGION 137 140 Substrate binding. {ECO:0000250}.
METAL 71 71 Magnesium 1. {ECO:0000250}.
METAL 135 135 Magnesium 1. {ECO:0000250}.
METAL 135 135 Magnesium 2. {ECO:0000250}.
METAL 137 137 Magnesium 1; via carbonyl oxygen.
{ECO:0000250}.
BINDING 71 71 Substrate. {ECO:0000250}.
CONFLICT 212 212 A -> V (in Ref. 5; AAM67202).
{ECO:0000305}.
CONFLICT 220 220 D -> Y (in Ref. 5; AAM67202).
{ECO:0000305}.
SEQUENCE 357 AA; 38385 MW; B2570242F2B5EFA6 CRC64;
MSYDEMLSAA KKAVSLAARL SNEVRKSLLV TDVWNKSDDS PVTVADYGSQ AVVSLVLERE
LQNEPVSLVA EEDSGELRKI AAETVLARIT ELVKDTLASD ESYAIASPLT SDDVLNAIDR
GKSEGGPKGR HWILDPIGGT RGFIRGEQYA IGLALLVEGK VVLGVMACPK LPLASTAGNA
LKSLPEKVGC LFYGSVGNGT YVQSLSVDSL PAKVEVSSID DPAKASFFES YHTPVPIHNT
IATKLGIKES PIKINSQTKY AALSRGDGEV YLRFTRKARP ESIWNHAAGS IIVSEAGGKV
TDAAGNPLDF SKGKYLDYKR GIVVTTQKLL PRLLTAVRES IKEEEEEEEK AASLKLH


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