NUDT3_ARATH
ID NUDT3_ARATH Reviewed; 772 AA.
AC Q8L831; Q8GY80; Q93ZN1; Q9MA07;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Nudix hydrolase 3;
DE Short=AtNUDT3;
DE EC=3.6.1.-;
GN Name=NUDT3; Synonyms=NUDX3; OrderedLocusNames=At1g79690;
GN ORFNames=F20B17.11;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [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).
CC -!- FUNCTION: Probably mediates the hydrolysis of some nucleoside
CC diphosphate derivatives. {ECO:0000250}.
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 -!- INTERACTION:
CC Q8L831; Q9ZWS7: ARR7; NbExp=2; IntAct=EBI-1807753, EBI-1100917;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8L831-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8L831-2; Sequence=VSP_014284, VSP_014285;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems and, at lower level,
CC leaves. {ECO:0000269|PubMed:15878881}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL08298.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC010793; AAF68108.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36287.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58081.1; -; Genomic_DNA.
DR EMBL; AK117805; BAC42449.1; -; mRNA.
DR EMBL; AY056442; AAL08298.1; ALT_FRAME; mRNA.
DR EMBL; AY120774; AAM53332.1; -; mRNA.
DR EMBL; BT000142; AAN15461.1; -; mRNA.
DR RefSeq; NP_001320544.1; NM_001334912.1. [Q8L831-1]
DR RefSeq; NP_565218.1; NM_106618.5. [Q8L831-1]
DR AlphaFoldDB; Q8L831; -.
DR SMR; Q8L831; -.
DR BioGRID; 29526; 2.
DR IntAct; Q8L831; 1.
DR STRING; 3702.AT1G79690.1; -.
DR MEROPS; M49.005; -.
DR MetOSite; Q8L831; -.
DR PaxDb; Q8L831; -.
DR PRIDE; Q8L831; -.
DR ProteomicsDB; 248734; -. [Q8L831-1]
DR EnsemblPlants; AT1G79690.1; AT1G79690.1; AT1G79690. [Q8L831-1]
DR EnsemblPlants; AT1G79690.2; AT1G79690.2; AT1G79690. [Q8L831-1]
DR GeneID; 844308; -.
DR Gramene; AT1G79690.1; AT1G79690.1; AT1G79690. [Q8L831-1]
DR Gramene; AT1G79690.2; AT1G79690.2; AT1G79690. [Q8L831-1]
DR KEGG; ath:AT1G79690; -.
DR Araport; AT1G79690; -.
DR TAIR; locus:2019848; AT1G79690.
DR eggNOG; ENOG502QT89; Eukaryota.
DR HOGENOM; CLU_020444_0_0_1; -.
DR InParanoid; Q8L831; -.
DR OMA; INYGPWD; -.
DR PhylomeDB; Q8L831; -.
DR BRENDA; 3.4.14.4; 399.
DR PRO; PR:Q8L831; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L831; baseline and differential.
DR Genevisible; Q8L831; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IDA:TAIR.
DR GO; GO:0006508; P:proteolysis; IEA:UniProt.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR039461; Peptidase_M49.
DR PANTHER; PTHR23422; PTHR23422; 1.
DR Pfam; PF00293; NUDIX; 1.
DR Pfam; PF03571; Peptidase_M49; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..772
FT /note="Nudix hydrolase 3"
FT /id="PRO_0000057123"
FT DOMAIN 30..172
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 69..90
FT /note="Nudix box"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT VAR_SEQ 108..114
FT /note="CVTNDGK -> WFVSWPI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_014284"
FT VAR_SEQ 115..772
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_014285"
FT CONFLICT 657
FT /note="V -> F (in Ref. 4; AAL08298)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 772 AA; 86857 MW; CC2F53E406D72A90 CRC64;
MAEEHFDVLT KSGEKTGVSK PRGEVHRDGD YHRAVHVWIF VETTQQLLLQ LRSDDKDSWP
GQWDISSAGH ISAGDTSLLS AQRELEEELG VKLPKDAFEK IFVFLQECVT NDGKFINNEF
NDVYLVTILH PIPLEAFTLQ KEEVSAVKYV PYEEYRNFLS KEDPAYVPYD VNGEYGKLFD
IIRQRCQVNT EARSLSLQKQ LQRYSPVTLE AKLTELSEAD QKALGLIVKA AKIMDDIFYE
QVWNSNPALR DWLKDHANAS KLDKLKWDYF TINKSPWSSL DENEAFLSTA DSAVKLLPGA
TKAIAGWKGL EYRAAFPVTK PPGANFYPPD MDKMEFTLWL NGLTEEQKHA ATGFFSVIKR
RSEANLDASD HLASSTKKLP DSNSDLYSIP YSEIYRPFLK KASEFLQKAG DLVSSPSLKK
LLHSKAEAFL SNEYYESDIA WMDLDSKLDI TIGPYETYED EIFGYKATFE TFIGIRDDKA
TADLKLFGDN LKLLEDNLPL ESVYKSTDVS AAPIRVIQLI YNSGDVKGPQ TVAYNLPNDE
KIVKDRGTSM VMLKNVQEAK FEHILKPIAE ITISKEQRGL VDFDSFFTHT ICHECCHGIG
PHTITLPGGQ TSTVRKELQE VHSAMEEAKA DIVGLWALKF LITKGLLSKS MVESMYVSFL
AGCFRSIRFG LTEAHGKGQA LQFNYLYEKG AFVFHEDSTF SVDFAKIEGA VESLSHEILT
IQGKGDKNAA TLLLNKYCTI TGPLKTALEN LERVKVPVDI SPTFPLAEAL MN
