NUDT8_ARATH
ID NUDT8_ARATH Reviewed; 369 AA.
AC Q8L7W2; Q8LAJ0; Q9LVT5;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Nudix hydrolase 8;
DE Short=AtNUDT8;
DE EC=3.6.1.-;
GN Name=NUDT8; Synonyms=NUDX8; OrderedLocusNames=At5g47240; ORFNames=MQL5.10;
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=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 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.
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=15878881; DOI=10.1074/jbc.m503536200;
RA Ogawa T., Ueda Y., Yoshimura K., Shigeoka S.;
RT "Comprehensive analysis of cytosolic nudix hydrolases in Arabidopsis
RT thaliana.";
RL J. Biol. Chem. 280:25277-25283(2005).
RN [6]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25436909; DOI=10.1371/journal.pone.0114119;
RA Fonseca J.P., Dong X.;
RT "Functional characterization of a Nudix hydrolase AtNUDX8 upon pathogen
RT attack indicates a positive role in plant immune responses.";
RL PLoS ONE 9:E114119-E114119(2014).
CC -!- FUNCTION: Probably mediates the hydrolysis of some nucleoside
CC diphosphate derivatives (By similarity). May be involved in plant
CC immunity and act as a positive regulator of defense response through
CC salicylic acid (SA) signaling (PubMed:25436909). {ECO:0000250,
CC ECO:0000269|PubMed:25436909}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems and, at lower level,
CC leaves. {ECO:0000269|PubMed:15878881}.
CC -!- INDUCTION: Circadian regulation with a peak after 8 hours of light.
CC Induced by abscisic acid (ABA). Down-regulated by salicylic acid (SA).
CC {ECO:0000269|PubMed:25436909}.
CC -!- DISRUPTION PHENOTYPE: Small and stunted plant phenotype when grown on
CC 12/12 hour photoperiod light. No visible phenotype when grown under
CC short or long day light (8/16 hours or 16/8 hours of light/dark).
CC {ECO:0000269|PubMed:25436909}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97158.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB018117; BAA97158.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95490.1; -; Genomic_DNA.
DR EMBL; AY125502; AAM78094.1; -; mRNA.
DR EMBL; BT000563; AAN18132.1; -; mRNA.
DR EMBL; AY087784; AAM65320.1; -; mRNA.
DR RefSeq; NP_568680.1; NM_124095.4.
DR AlphaFoldDB; Q8L7W2; -.
DR SMR; Q8L7W2; -.
DR STRING; 3702.AT5G47240.1; -.
DR PaxDb; Q8L7W2; -.
DR PRIDE; Q8L7W2; -.
DR ProteomicsDB; 248889; -.
DR EnsemblPlants; AT5G47240.1; AT5G47240.1; AT5G47240.
DR GeneID; 834771; -.
DR Gramene; AT5G47240.1; AT5G47240.1; AT5G47240.
DR KEGG; ath:AT5G47240; -.
DR Araport; AT5G47240; -.
DR TAIR; locus:2171544; AT5G47240.
DR eggNOG; KOG0648; Eukaryota.
DR HOGENOM; CLU_054299_0_0_1; -.
DR InParanoid; Q8L7W2; -.
DR PhylomeDB; Q8L7W2; -.
DR PRO; PR:Q8L7W2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L7W2; baseline and differential.
DR Genevisible; Q8L7W2; AT.
DR GO; GO:0005829; C:cytosol; ISM:TAIR.
DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IBA:GO_Central.
DR GO; GO:0035529; F:NADH pyrophosphatase activity; IBA:GO_Central.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR003293; Nudix_hydrolase6-like.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR040618; Pre-Nudix.
DR PANTHER; PTHR13994; PTHR13994; 1.
DR Pfam; PF00293; NUDIX; 1.
DR Pfam; PF18290; Nudix_hydro; 1.
DR PRINTS; PR01356; GFGPROTEIN.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..369
FT /note="Nudix hydrolase 8"
FT /id="PRO_0000057128"
FT DOMAIN 188..318
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 225..246
FT /note="Nudix box"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 13..14
FT /note="KG -> RE (in Ref. 4; AAM65320)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="R -> RLR (in Ref. 4; AAM65320)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="E -> K (in Ref. 4; AAM65320)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="C -> S (in Ref. 3; AAM78094/AAN18132)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 41314 MW; 22BDDE2FB38D362E CRC64;
MDSVSLSEVT VIKGTTHLGF MHSFRQPFCG VKISPKFYLS KVDGPKAISS SSNTKSQFVY
GGGSIAATSD SGYKMNGVNL KSRTLMSSAV KERSLLDAYD DEYGGVIVDH GKLPSNPYAF
ASMLRASLSD WRRKGKKGVW LKLPVEQSEL VPIAIKEGFE YHHAEKGYVM LTYWIPEEEP
SMLPANASHQ VGVGGFVLNQ HKEVLVVQEK YCAPSITGLW KLPTGFINES EEIFSGAVRE
VKEETGVDTE FSEVIAFRHA HNVAFEKSDL FFICMLRPLS DKIIIDALEI KAAKWMPLAE
FVEQPMIRGD KMFKRVIEIC EARLSHRYCG LSPHRLVSTF DGKPSSLYYN VVDDDHDPSH
SNCSTEFYR
