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