DPNP3_ARATH
ID DPNP3_ARATH Reviewed; 357 AA.
AC Q8GY63; Q8L8N7; Q9LVN5;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Probable SAL3 phosphatase;
DE AltName: Full=3'(2'),5'-bisphosphate nucleotidase 3;
DE EC=3.1.3.7;
DE AltName: Full=3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase 3;
DE AltName: Full=DPNPase 3;
DE AltName: Full=Inositol polyphosphate 1-phosphatase 3;
DE Short=IPPase 3;
DE AltName: Full=Inositol-1,4-bisphosphate 1-phosphatase 3;
DE EC=3.1.3.57;
GN Name=SAL3; OrderedLocusNames=At5g63990; ORFNames=MBM17.9;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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. Is also able to hydrolyze inositol 1,4-
CC bisphosphate. {ECO:0000250}.
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; Evidence={ECO:0000250};
CC -!- PATHWAY: Signal transduction; phosphatidylinositol signaling pathway.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8GY63-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA96902.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB019227; BAA96902.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97827.1; -; Genomic_DNA.
DR EMBL; AK117842; BAC42483.1; -; mRNA.
DR EMBL; BT006247; AAP12896.1; -; mRNA.
DR EMBL; AY088896; AAM67202.1; -; mRNA.
DR RefSeq; NP_568983.1; NM_125795.5. [Q8GY63-1]
DR AlphaFoldDB; Q8GY63; -.
DR SMR; Q8GY63; -.
DR STRING; 3702.AT5G63990.1; -.
DR PaxDb; Q8GY63; -.
DR PRIDE; Q8GY63; -.
DR ProteomicsDB; 220403; -. [Q8GY63-1]
DR EnsemblPlants; AT5G63990.1; AT5G63990.1; AT5G63990. [Q8GY63-1]
DR GeneID; 836520; -.
DR Gramene; AT5G63990.1; AT5G63990.1; AT5G63990. [Q8GY63-1]
DR KEGG; ath:AT5G63990; -.
DR Araport; AT5G63990; -.
DR TAIR; locus:2160831; AT5G63990.
DR eggNOG; KOG1528; Eukaryota.
DR HOGENOM; CLU_033446_2_1_1; -.
DR InParanoid; Q8GY63; -.
DR OMA; MGRHWIL; -.
DR OrthoDB; 1096950at2759; -.
DR PhylomeDB; Q8GY63; -.
DR BioCyc; ARA:AT5G63990-MON; -.
DR UniPathway; UPA00944; -.
DR PRO; PR:Q8GY63; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GY63; baseline and differential.
DR Genevisible; Q8GY63; 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:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
DR InterPro; IPR006239; Bisphos_HAL2.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR Pfam; PF00459; Inositol_P; 1.
DR TIGRFAMs; TIGR01330; bisphos_HAL2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Reference proteome.
FT CHAIN 1..357
FT /note="Probable SAL3 phosphatase"
FT /id="PRO_0000142532"
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 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 137..140
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CONFLICT 212
FT /note="A -> V (in Ref. 5; AAM67202)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="D -> Y (in Ref. 5; AAM67202)"
FT /evidence="ECO:0000305"
SQ 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
