NEN3_ARATH
ID NEN3_ARATH Reviewed; 506 AA.
AC Q9CA74; F4HVM5;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein NEN3 {ECO:0000303|PubMed:25081480};
DE AltName: Full=NAC45/NAC86-dependent exonuclease-domain protein 3 {ECO:0000303|PubMed:25081480};
DE EC=3.1.11.-;
GN Name=NEN3; OrderedLocusNames=At1g74390 {ECO:0000312|Araport:AT1G74390};
GN ORFNames=F1M20.7 {ECO:0000312|EMBL:AAG52378.1};
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=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 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 [4]
RP FUNCTION, AND INDUCTION BY NAC045 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 that may be involved in enuclation of
CC sieve elements. {ECO:0000305|PubMed:25081480}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q682U6};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. {ECO:0000305};
CC Name=1;
CC IsoId=Q9CA74-1; Sequence=Displayed;
CC -!- INDUCTION: Regulated by the transcription factors NAC045 and NAC086.
CC {ECO:0000269|PubMed:25081480}.
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DR EMBL; AC011765; AAG52378.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35585.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35586.2; -; Genomic_DNA.
DR EMBL; AY099717; AAM20568.1; -; mRNA.
DR EMBL; BT000288; AAN15607.1; -; mRNA.
DR PIR; F96772; F96772.
DR RefSeq; NP_001319380.1; NM_001334644.1. [Q9CA74-1]
DR RefSeq; NP_177579.1; NM_106099.3. [Q9CA74-1]
DR AlphaFoldDB; Q9CA74; -.
DR SMR; Q9CA74; -.
DR STRING; 3702.AT1G74390.1; -.
DR PaxDb; Q9CA74; -.
DR PRIDE; Q9CA74; -.
DR ProteomicsDB; 251291; -. [Q9CA74-1]
DR EnsemblPlants; AT1G74390.1; AT1G74390.1; AT1G74390. [Q9CA74-1]
DR EnsemblPlants; AT1G74390.2; AT1G74390.2; AT1G74390. [Q9CA74-1]
DR GeneID; 843780; -.
DR Gramene; AT1G74390.1; AT1G74390.1; AT1G74390. [Q9CA74-1]
DR Gramene; AT1G74390.2; AT1G74390.2; AT1G74390. [Q9CA74-1]
DR KEGG; ath:AT1G74390; -.
DR Araport; AT1G74390; -.
DR TAIR; locus:2019100; AT1G74390.
DR eggNOG; ENOG502QPPQ; Eukaryota.
DR HOGENOM; CLU_030072_0_0_1; -.
DR InParanoid; Q9CA74; -.
DR OMA; WAGHNID; -.
DR PhylomeDB; Q9CA74; -.
DR PRO; PR:Q9CA74; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CA74; baseline and differential.
DR Genevisible; Q9CA74; AT.
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 Alternative splicing; Exonuclease; Hydrolase; Magnesium; Metal-binding;
KW Nuclease; Reference proteome.
FT CHAIN 1..506
FT /note="Protein NEN3"
FT /id="PRO_0000430890"
FT DOMAIN 15..176
FT /note="Exonuclease"
FT /evidence="ECO:0000255"
FT REGION 204..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q91XB0"
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q91XB0"
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q91XB0"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q91XB0"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q91XB0"
SQ SEQUENCE 506 AA; 55633 MW; FF3D9121390D0D92 CRC64;
MASSLGGDER SEIAFFDLET AVPTKSGEPF AILEFGAILV CPRRLEELYS YSTLVRPTDL
SLISTLTKRR SGITRDGVLS AHTFSEIADK VYDILHGRIW AGHNIIRFDC VRIREAFAEI
GLSPPEPKAT IDSLSLLSQK FGKRAGDMKM ASLATYFGLG DQAHRSLDDV RMNLEVVKYC
ATVLFLESSV PDILTDMSWF SPRKSPRTRS NGKLVANGVR ESSTSSSSSP KTDPSSSSVD
ATIVKNHPIV SLLTECSESD ASSYDIEDPI DITTLIGKLR IGTLQTDAAE EAKTVRQQDE
SPPSPDSDAK DESFLGVNEV SVSSIRASLV PFYRGSLRMK LFHNDTPLHL CWHSLKVRFG
ISRKFVDHAG RPKLNIIVDA PLDLCKILDA VDAAAHNLPT DSSTNSDWRP TVIRKEGFAN
YPTARLHISS ESNGDDTLCG TQVYQKEEPL GTNQKLDVSS DNLEKLESAL LPGTLVDAFF
SLEPYSYQQM AGIRLAVKKL VILLKK
