NSH3_ARATH
ID NSH3_ARATH Reviewed; 890 AA.
AC Q8RY23;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Nucleoside hydrolase 3 {ECO:0000303|PubMed:21235647};
DE AltName: Full=Adenosine nucleosidase {ECO:0000303|PubMed:21235647};
DE EC=3.2.2.7 {ECO:0000269|PubMed:21235647};
DE AltName: Full=Inosine nucleosidase {ECO:0000303|PubMed:21235647};
DE EC=3.2.2.2 {ECO:0000269|PubMed:21235647};
DE AltName: Full=Purine nucleosidase {ECO:0000303|PubMed:21235647};
DE EC=3.2.2.1 {ECO:0000269|PubMed:21235647};
DE Flags: Precursor;
GN Name=NSH3 {ECO:0000303|PubMed:21235647};
GN OrderedLocusNames=At5g18860 {ECO:0000312|Araport:AT5G18860};
GN ORFNames=F17K4.110 {ECO:0000312|EMBL:AC068655};
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).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY WOUNDING AND JASMONIC ACID,
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=21235647; DOI=10.1111/j.1365-313x.2010.04455.x;
RA Jung B., Hoffmann C., Moehlmann T.;
RT "Arabidopsis nucleoside hydrolases involved in intracellular and
RT extracellular degradation of purines.";
RL Plant J. 65:703-711(2011).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=26779190; DOI=10.3389/fpls.2015.01158;
RA Daumann M., Fischer M., Niopek-Witz S., Girke C., Moehlmann T.;
RT "Apoplastic nucleoside accumulation in Arabidopsis leads to reduced
RT photosynthetic performance and increased susceptibility against Botrytis
RT cinerea.";
RL Front. Plant Sci. 6:1158-1158(2015).
CC -!- FUNCTION: Extracellular purine-specific hydrolase present in the
CC apoplastic fluid involved in the degradation of extracellular
CC nucleosides, including inosine and adenosine, and which may participate
CC in wound and pathogen responses (e.g. Botrytis cinerea).
CC {ECO:0000269|PubMed:21235647, ECO:0000269|PubMed:26779190}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a purine D-ribonucleoside + H2O = a purine nucleobase + D-
CC ribose; Xref=Rhea:RHEA:23344, ChEBI:CHEBI:15377, ChEBI:CHEBI:26386,
CC ChEBI:CHEBI:47013, ChEBI:CHEBI:142355; EC=3.2.2.1;
CC Evidence={ECO:0000269|PubMed:21235647};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + inosine = D-ribose + hypoxanthine; Xref=Rhea:RHEA:16657,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17368, ChEBI:CHEBI:17596,
CC ChEBI:CHEBI:47013; EC=3.2.2.2;
CC Evidence={ECO:0000269|PubMed:21235647};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + H2O = adenine + D-ribose; Xref=Rhea:RHEA:18669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:16708,
CC ChEBI:CHEBI:47013; EC=3.2.2.7;
CC Evidence={ECO:0000269|PubMed:21235647};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=97.2 uM for inosine {ECO:0000269|PubMed:21235647};
CC KM=43.1 uM for adenosine {ECO:0000269|PubMed:21235647};
CC pH dependence:
CC Optimum pH is 4.8.;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:21235647}. Note=Present in the apoplastic fluid.
CC {ECO:0000269|PubMed:21235647}.
CC -!- INDUCTION: By jasmonic acid (JA) and wounding.
CC {ECO:0000269|PubMed:21235647}.
CC -!- DISRUPTION PHENOTYPE: Impaired hydrolysis of inosine and adenosine by
CC apoplastic fluid leading to an increased sensitivity to 2-
CC chloroadenosine (PubMed:21235647). The isolated apoplastic sap
CC extracted from the double mutant missing both NSH3 and ENT3 lacks the
CC ability to catalyze the conversion of inosine in hypoxanthine; this
CC double mutant is unable to grow on medium containing inosine as sole
CC nitrogen source, in addition plants are more sensitive to the
CC necrotrophic fungus Botrytis cinerea BMM but are resistant to the
CC cytotoxic adenosine analog 2-chloro-adenosine (CADO) and to 5-fluoro-
CC uridine (PubMed:26779190). {ECO:0000269|PubMed:21235647,
CC ECO:0000269|PubMed:26779190}.
CC -!- SIMILARITY: Belongs to the IUNH family. {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; AC068655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92622.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68442.1; -; Genomic_DNA.
DR EMBL; AY078950; AAL84950.1; -; mRNA.
DR EMBL; AY133631; AAM91461.1; -; mRNA.
DR RefSeq; NP_001330199.1; NM_001343573.1.
DR RefSeq; NP_197387.1; NM_121891.4.
DR AlphaFoldDB; Q8RY23; -.
DR SMR; Q8RY23; -.
DR STRING; 3702.AT5G18860.1; -.
DR PaxDb; Q8RY23; -.
DR PRIDE; Q8RY23; -.
DR ProteomicsDB; 181332; -.
DR EnsemblPlants; AT5G18860.1; AT5G18860.1; AT5G18860.
DR EnsemblPlants; AT5G18860.2; AT5G18860.2; AT5G18860.
DR GeneID; 832004; -.
DR Gramene; AT5G18860.1; AT5G18860.1; AT5G18860.
DR Gramene; AT5G18860.2; AT5G18860.2; AT5G18860.
DR KEGG; ath:AT5G18860; -.
DR Araport; AT5G18860; -.
DR TAIR; locus:2144910; AT5G18860.
DR eggNOG; KOG2938; Eukaryota.
DR HOGENOM; CLU_018945_1_0_1; -.
DR InParanoid; Q8RY23; -.
DR OMA; KHRRYTH; -.
DR OrthoDB; 824591at2759; -.
DR PhylomeDB; Q8RY23; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8RY23; baseline and differential.
DR GO; GO:0048046; C:apoplast; IDA:TAIR.
DR GO; GO:0047622; F:adenosine nucleosidase activity; IMP:TAIR.
DR GO; GO:0047724; F:inosine nucleosidase activity; IMP:TAIR.
DR GO; GO:0006154; P:adenosine catabolic process; IMP:TAIR.
DR GO; GO:0006148; P:inosine catabolic process; IMP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR Gene3D; 3.90.245.10; -; 2.
DR InterPro; IPR001910; Inosine/uridine_hydrolase_dom.
DR InterPro; IPR036452; Ribo_hydro-like.
DR Pfam; PF01156; IU_nuc_hydro; 2.
DR SUPFAM; SSF53590; SSF53590; 2.
PE 1: Evidence at protein level;
KW Apoplast; Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..890
FT /note="Nucleoside hydrolase 3"
FT /id="PRO_5015099346"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 740
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 890 AA; 99072 MW; 1CFEA20F101A1A76 CRC64;
MLTSPTLKSL WFLFTILGLL GQNLPCVLSS SHRILVDTDV DTDDLFAILY LLKLNKSEFD
LVGITLSANA WTNAGHAVNQ VYDLLHMMDR DDIPVGVGGE GGISDDGTIH SDVGGYFPII
EQGMTTTGEC RYRQAIPKGL GGLLDIDSNY GFRKQFLPQG NRRYTPLQQP TAQKVIVDKI
SEGPTTVILL GSHTNFALFL MSNPHLKHNI QHIYIMGGGV RSQNPTGCCP ANSTVAECQP
RQCGNRGNLF TDYTSNPYSE FNIFADPFAA YQVFHSGVPV TLVPLDATNT IPINQKFFET
FENNYQRTYE AQYVFLSLKI ARDTWFDDEF YKSYFMWDSF TAGVAVSIMR NSANKNNKNG
ENDFAEMEYM NITVVTSNKP YGRSDGSNPF FDNRRTPKFN LALGGVHSGH VQTGLRDPTC
LPKSGIGRGK CKDGYTQEIS GSDSVRVLVA TRAKPNINIK SKLDREFYVD FLEVLNRPEE
TGRFNFSSQF PYYKEELFRP DLSKTRPGKP VVFDMDMSAG DFLSLFYLLK VPVDKIDLKA
IIVSPTGWAN AATIDVVYDL LHMMGRDDIP VGLGDMLALN QSDPIFPPVG GCKYVKAIPR
GCGGFLDSDT LYGLARDLPR SPRRYTAENS VTHGAPRDTD RPELRQPLAI EVWQNLTKSG
NGVSKITVLT NGPLTNLAKI ISSDKKSSSL IKEVYIVGGH INREKSDKGN IFTIPSNAYA
EFNMFLDPLA AKTVLESALN ITLVPLATQH KLSSFQTMLD RLYSSTKTPE ARFVKRLLVR
LQALHQKHRR YTHIDMFLGE VLGAVLLGGD DASLKPKMRA EHIKVIAEGD ESRDGKILID
KLRGKQIKIL ERVDLISISE SFASRLDDKK QSAVIGSFEE QKKIWSTPPS
