DPNP4_ARATH
ID DPNP4_ARATH Reviewed; 345 AA.
AC Q84VY5; Q9FY86;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable SAL4 phosphatase;
DE AltName: Full=3'(2'),5'-bisphosphate nucleotidase 4;
DE EC=3.1.3.7;
DE AltName: Full=3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase 4;
DE AltName: Full=DPNPase 4;
DE AltName: Full=Inositol polyphosphate 1-phosphatase 4;
DE Short=IPPase 4;
DE AltName: Full=Inositol-1,4-bisphosphate 1-phosphatase 4;
DE EC=3.1.3.57;
GN Name=SAL4; OrderedLocusNames=At5g09290; ORFNames=T5E8_90;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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=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. 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 -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC05455.1; Type=Erroneous gene model prediction; Evidence={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; AL391712; CAC05455.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91370.1; -; Genomic_DNA.
DR EMBL; BT004622; AAO42868.1; -; mRNA.
DR RefSeq; NP_196491.2; NM_120965.6.
DR AlphaFoldDB; Q84VY5; -.
DR SMR; Q84VY5; -.
DR STRING; 3702.AT5G09290.1; -.
DR PaxDb; Q84VY5; -.
DR PRIDE; Q84VY5; -.
DR ProteomicsDB; 220404; -.
DR EnsemblPlants; AT5G09290.1; AT5G09290.1; AT5G09290.
DR GeneID; 830788; -.
DR Gramene; AT5G09290.1; AT5G09290.1; AT5G09290.
DR KEGG; ath:AT5G09290; -.
DR Araport; AT5G09290; -.
DR TAIR; locus:2184812; AT5G09290.
DR eggNOG; KOG1528; Eukaryota.
DR HOGENOM; CLU_033446_2_1_1; -.
DR InParanoid; Q84VY5; -.
DR OMA; CPKLENH; -.
DR OrthoDB; 1096950at2759; -.
DR PhylomeDB; Q84VY5; -.
DR BioCyc; ARA:AT5G09290-MON; -.
DR UniPathway; UPA00944; -.
DR PRO; PR:Q84VY5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84VY5; baseline and differential.
DR Genevisible; Q84VY5; 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; 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 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Metal-binding; Multifunctional enzyme;
KW Reference proteome.
FT CHAIN 1..345
FT /note="Probable SAL4 phosphatase"
FT /id="PRO_0000142533"
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"
SQ SEQUENCE 345 AA; 37489 MW; CD6CBD373A286706 CRC64;
MPYEKELAAA KKAVSLAARL SQEVQKSLLQ SDVRSKSDKS PVTAADYGSQ AVISHVLERE
LHPEPLYLVA EENAEDLHKN GAEEFLESIT KLVNNALASD DSYANSSLSM DDVRKAIDHG
RSQGGSSGRH WILDPVDGTR GFVKGEEYAV ALALLVEGKV VLGVMACPKL ENHKSSSSGC
LFFATVGEGA YVQSLEGDSH PPQKVQVSNI ENPEEATFVE SSHKPIPIHS SIANKLGIKA
PPLRIHSQVK YAALARGDAE IYLRFTLKGY REFIWNHAAG AIITTEAGGV VCDADGNPLD
FSRGNHLEHK TGIVVSTKNL MPRLLKAIRE SIEEEMLLSE TQLKL
