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NSH5_ARATH
ID   NSH5_ARATH              Reviewed;         258 AA.
AC   F4JZJ0;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Nucleoside hydrolase 5 {ECO:0000303|PubMed:21235647};
DE            EC=3.2.2.- {ECO:0000250|UniProtKB:Q8RY23};
DE   Flags: Precursor;
GN   Name=NSH5 {ECO:0000303|PubMed:21235647};
GN   OrderedLocusNames=At5g18870 {ECO:0000312|Araport:AT5G18870};
GN   ORFNames=F17K4.120 {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   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).
CC   -!- FUNCTION: May be involved in the degradation of extracellular
CC       nucleosides. {ECO:0000250|UniProtKB:Q8RY23}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000250|UniProtKB:Q8RY23}. Note=Present in the apoplastic fluid.
CC       {ECO:0000250|UniProtKB:Q8RY23}.
CC   -!- SIMILARITY: Belongs to the IUNH family. {ECO:0000305}.
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DR   EMBL; AC068655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED92623.1; -; Genomic_DNA.
DR   RefSeq; NP_197388.1; NM_121892.1.
DR   AlphaFoldDB; F4JZJ0; -.
DR   SMR; F4JZJ0; -.
DR   STRING; 3702.AT5G18870.1; -.
DR   PaxDb; F4JZJ0; -.
DR   PRIDE; F4JZJ0; -.
DR   ProteomicsDB; 199289; -.
DR   EnsemblPlants; AT5G18870.1; AT5G18870.1; AT5G18870.
DR   GeneID; 832005; -.
DR   Gramene; AT5G18870.1; AT5G18870.1; AT5G18870.
DR   KEGG; ath:AT5G18870; -.
DR   Araport; AT5G18870; -.
DR   TAIR; locus:2144925; AT5G18870.
DR   eggNOG; KOG2938; Eukaryota.
DR   HOGENOM; CLU_069014_0_0_1; -.
DR   InParanoid; F4JZJ0; -.
DR   OMA; QGPISIF; -.
DR   OrthoDB; 824591at2759; -.
DR   PhylomeDB; F4JZJ0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; F4JZJ0; differential.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IEA:InterPro.
DR   Gene3D; 3.90.245.10; -; 1.
DR   InterPro; IPR001910; Inosine/uridine_hydrolase_dom.
DR   InterPro; IPR036452; Ribo_hydro-like.
DR   Pfam; PF01156; IU_nuc_hydro; 1.
DR   SUPFAM; SSF53590; SSF53590; 1.
PE   3: Inferred from homology;
KW   Apoplast; Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..258
FT                   /note="Nucleoside hydrolase 5"
FT                   /id="PRO_5003311586"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   258 AA;  28918 MW;  406374C41AB83E64 CRC64;
     MLSPRRFILV VTILGLLGHN LTHVLNSPHR ILLDTDVDTD DFIALLYLLK LNKTEFDLVG
     ITLSANSWTN AGHGVNHIYD ILYMMGRDDI TVGVGGEGGI LEDGTILPDV GDYLPIIEQG
     MTTAGGCRYR QSIPKGRIQK IDSNYGFRKH FLPQGNRRYT PLEQPTAQKV IVDKVSEGPI
     SIFVIGSHTN LALFMMSNPH LKHNIQHIYV MGGSVRCQNP NGFCGNLFTD YTSNPYAEFN
     IFTDPFAAYQ VFRLLWFL
 
 
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