NEN1_ARATH
ID NEN1_ARATH Reviewed; 468 AA.
AC Q9FLR0;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein NEN1 {ECO:0000303|PubMed:25081480};
DE AltName: Full=NAC45/NAC86-dependent exonuclease-domain protein 1 {ECO:0000303|PubMed:25081480};
DE EC=3.1.11.-;
GN Name=NEN1 {ECO:0000303|PubMed:25081480};
GN OrderedLocusNames=At5g07710 {ECO:0000312|Araport:AT5G07710};
GN ORFNames=MBK20.17 {ECO:0000312|EMBL:BAB11450.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY NAC045
RP AND NAC086.
RX PubMed=25081480; DOI=10.1126/science.1253736;
RA Furuta K.M., Yadav S.R., Lehesranta S., Belevich I., Miyashima S.,
RA Heo J.O., Vaten A., Lindgren O., De Rybel B., Van Isterdael G.,
RA Somervuo P., Lichtenberger R., Rocha R., Thitamadee S., Taehtiharju S.,
RA Auvinen P., Beeckman T., Jokitalo E., Helariutta Y.;
RT "Plant development. Arabidopsis NAC45/86 direct sieve element morphogenesis
RT culminating in enucleation.";
RL Science 345:933-937(2014).
CC -!- FUNCTION: Probable exonuclease involved in enuclation of sieve
CC elements. {ECO:0000305|PubMed:25081480}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q682U6};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25081480}. Nucleus
CC {ECO:0000269|PubMed:25081480}. Note=Moves from the cytoplasm to the
CC nucleus during enuclation. {ECO:0000269|PubMed:25081480}.
CC -!- TISSUE SPECIFICITY: Expressed in the sieve elements and phloem pole
CC pericycle cells. {ECO:0000269|PubMed:25081480}.
CC -!- INDUCTION: Regulated by the transcription factors NAC045 and NAC086.
CC {ECO:0000269|PubMed:25081480}.
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DR EMBL; AB010070; BAB11450.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91196.1; -; Genomic_DNA.
DR RefSeq; NP_196388.1; NM_120853.4.
DR AlphaFoldDB; Q9FLR0; -.
DR SMR; Q9FLR0; -.
DR STRING; 3702.AT5G07710.1; -.
DR PaxDb; Q9FLR0; -.
DR PRIDE; Q9FLR0; -.
DR ProteomicsDB; 251187; -.
DR EnsemblPlants; AT5G07710.1; AT5G07710.1; AT5G07710.
DR GeneID; 830664; -.
DR Gramene; AT5G07710.1; AT5G07710.1; AT5G07710.
DR KEGG; ath:AT5G07710; -.
DR Araport; AT5G07710; -.
DR TAIR; locus:2160359; AT5G07710.
DR eggNOG; ENOG502QPPQ; Eukaryota.
DR HOGENOM; CLU_030072_0_0_1; -.
DR InParanoid; Q9FLR0; -.
DR OMA; PLQLCCA; -.
DR OrthoDB; 567936at2759; -.
DR PhylomeDB; Q9FLR0; -.
DR PRO; PR:Q9FLR0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLR0; baseline and differential.
DR Genevisible; Q9FLR0; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Nucleus; Reference proteome.
FT CHAIN 1..468
FT /note="Protein NEN1"
FT /id="PRO_0000430888"
FT DOMAIN 11..172
FT /note="Exonuclease"
FT /evidence="ECO:0000255"
FT ACT_SITE 159
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q91XB0"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q91XB0"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q91XB0"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q91XB0"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q91XB0"
SQ SEQUENCE 468 AA; 52167 MW; 7CD5A37DF0BB2211 CRC64;
MDPEDRSEIA FFDVETTVPK RGQRFAILEF GSILVCPKKL TELRSYTTLV QPADLSLISS
LSVRCNGIKR DDVVLAPLFA DIADTVYDIL HGRIWAGHNI LRFDCARIRE AFAEIGRQPP
EPKGAIDSLG LLTQKFGRRA GDMKMATLAR YFGLGNQTHR SLDDVRMNLE VLKYCATVLF
LESSLPYAHV DNSVSPETIS SRRRIDASRE GNTVTTSVRL PSISENSAAQ PDPFNMSVLR
NEMASDNHIQ SDILMEEEQI EPSDVVASEN TSDHEGFLTP DAMSLSNIKA MLFPFYPGSQ
MMKLKLLHGD SPLQLYCSYL KIRFGVNGKF LDNTGRRRLN FVVDLNPSLY SILEACDSNA
QKLSVDSGST SEWNPVVNPM KGFVNYPNAR IHIATEINGD EARYATEIHQ RESSGATQKL
IFSNPNNEEL ESLLTTGSVV DAFLSLEPYD YQQKAGIRLV AKKLVIQS
