NAC16_ARATH
ID NAC16_ARATH Reviewed; 564 AA.
AC A4FVP6; Q8LFG7; Q9XIC4;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=NAC domain-containing protein 16 {ECO:0000303|PubMed:15029955};
DE Short=ANAC016 {ECO:0000303|PubMed:15029955};
DE AltName: Full=Protein NTM1-like 3 {ECO:0000303|PubMed:17158162};
GN Name=NAC016 {ECO:0000312|EMBL:AEE31682.1};
GN Synonyms=NTL3 {ECO:0000303|PubMed:17158162};
GN OrderedLocusNames=At1g34180 {ECO:0000312|Araport:AT1G34180};
GN ORFNames=F23M19.14 {ECO:0000312|EMBL:AAD39614.1};
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;
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15029955; DOI=10.1093/dnares/10.6.239;
RA Ooka H., Satoh K., Doi K., Nagata T., Otomo Y., Murakami K., Matsubara K.,
RA Osato N., Kawai J., Carninci P., Hayashizaki Y., Suzuki K., Kojima K.,
RA Takahara Y., Yamamoto K., Kikuchi S.;
RT "Comprehensive analysis of NAC family genes in Oryza sativa and Arabidopsis
RT thaliana.";
RL DNA Res. 10:239-247(2003).
RN [7]
RP GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17158162; DOI=10.1093/nar/gkl1068;
RA Kim S.Y., Kim S.G., Kim Y.S., Seo P.J., Bae M., Yoon H.K., Park C.M.;
RT "Exploring membrane-associated NAC transcription factors in Arabidopsis:
RT implications for membrane biology in genome regulation.";
RL Nucleic Acids Res. 35:203-213(2007).
RN [8]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=23926065; DOI=10.1093/pcp/pct113;
RA Kim Y.S., Sakuraba Y., Han S.H., Yoo S.C., Paek N.C.;
RT "Mutation of the Arabidopsis NAC016 transcription factor delays leaf
RT senescence.";
RL Plant Cell Physiol. 54:1660-1672(2013).
CC -!- FUNCTION: Transcriptional activator activated by proteolytic cleavage
CC through regulated intramembrane proteolysis (RIP) (By similarity).
CC Transcriptional activator that promotes leaf senescence by up-
CC regulating senescence-associated genes in response to developmental and
CC stress-induced senescence signals. Functions in salt and oxidative
CC stress-responsive signaling pathways. Binds to the promoter of
CC NAC029/NAP and NAC059/ORS1 genes (PubMed:23926065).
CC {ECO:0000250|UniProtKB:Q949N0, ECO:0000269|PubMed:23926065}.
CC -!- INTERACTION:
CC A4FVP6; O80995: PDF1.3; NbExp=3; IntAct=EBI-25522702, EBI-25522494;
CC A4FVP6; Q9LVI4: TIFY6B; NbExp=3; IntAct=EBI-25522702, EBI-1792431;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q949N0}; Single-
CC pass membrane protein {ECO:0000255}. Nucleus
CC {ECO:0000250|UniProtKB:Q949N0, ECO:0000255|PROSITE-ProRule:PRU00353}.
CC Note=Localized primarily in plasma membrane or endoplasmic reticulum
CC membrane as dormant form and, upon specific stress or signal, is
CC processed into a transcriptionally active and nuclear form after a
CC proteolytic cleavage through regulated intramembrane proteolysis (RIP).
CC {ECO:0000250|UniProtKB:Q949N0}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, shoot apex,
CC stems and flowers. {ECO:0000269|PubMed:17158162}.
CC -!- DEVELOPMENTAL STAGE: Induced during normal senescence.
CC {ECO:0000269|PubMed:23926065}.
CC -!- INDUCTION: By cold, salt, drought stress and methyl methanesulfonate
CC (MMS) treatment. {ECO:0000269|PubMed:17158162}.
CC -!- DOMAIN: The NAC domain includes a DNA binding domain and a dimerization
CC domain. {ECO:0000255|PROSITE-ProRule:PRU00353}.
CC -!- DISRUPTION PHENOTYPE: Stay-green phenotype during senescence, salt
CC stress and oxidative stress. {ECO:0000269|PubMed:23926065}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD39614.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEE31683.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007454; AAD39614.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31682.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31683.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BT030344; ABO38757.1; -; mRNA.
DR EMBL; AB493493; BAH30331.1; -; mRNA.
DR EMBL; AY084860; AAM67294.1; -; mRNA.
DR PIR; A86466; A86466.
DR RefSeq; NP_001077648.1; NM_001084179.1.
DR RefSeq; NP_564439.1; NM_103141.4.
DR AlphaFoldDB; A4FVP6; -.
DR SMR; A4FVP6; -.
DR IntAct; A4FVP6; 2.
DR STRING; 3702.AT1G34180.2; -.
DR iPTMnet; A4FVP6; -.
DR PaxDb; A4FVP6; -.
DR PRIDE; A4FVP6; -.
DR ProteomicsDB; 251227; -.
DR EnsemblPlants; AT1G34180.1; AT1G34180.1; AT1G34180.
DR GeneID; 840317; -.
DR Gramene; AT1G34180.1; AT1G34180.1; AT1G34180.
DR KEGG; ath:AT1G34180; -.
DR Araport; AT1G34180; -.
DR TAIR; locus:2026114; AT1G34180.
DR eggNOG; ENOG502QT9T; Eukaryota.
DR HOGENOM; CLU_030918_1_0_1; -.
DR OMA; NQLNNFM; -.
DR OrthoDB; 659212at2759; -.
DR PhylomeDB; A4FVP6; -.
DR PRO; PR:A4FVP6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; A4FVP6; baseline and differential.
DR Genevisible; A4FVP6; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:1900057; P:positive regulation of leaf senescence; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR Gene3D; 2.170.150.80; -; 1.
DR InterPro; IPR003441; NAC-dom.
DR InterPro; IPR036093; NAC_dom_sf.
DR Pfam; PF02365; NAM; 1.
DR SUPFAM; SSF101941; SSF101941; 1.
DR PROSITE; PS51005; NAC; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Membrane; Nucleus; Reference proteome;
KW Stress response; Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..564
FT /note="NAC domain-containing protein 16"
FT /id="PRO_0000432442"
FT TRANSMEM 535..555
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 16..166
FT /note="NAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT DNA_BIND 115..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT CONFLICT 45
FT /note="V -> I (in Ref. 5; AAM67294)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="V -> I (in Ref. 5; AAM67294)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="G -> V (in Ref. 5; AAM67294)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="K -> I (in Ref. 5; AAM67294)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 564 AA; 63407 MW; A139CB879621F8A6 CRC64;
MVDSSRDSCF KAGKFSAPGF RFHPTDEELV VYYLKRKICC KKLRVNAIGV VDVYKVDPSE
LPGLSMLKTG DRQWFFFTPR NRKYPNAARS SRGTATGYWK ATGKDRVIEY NSRSVGLKKT
LVFYRGRAPN GERTDWVMHE YTMDEEELGR CKNAKEYYAL YKLYKKSGAG PKNGEQYGAP
FQEEEWVDSD SEDADSVAVP DYPVVRYENG PCVDDTKFCN PVKLQLEDIE KLLNEIPDAP
GVNQRQFDEF VGVPQGNSAE VIQSTLLNNS SGEYIDPRTN GMFLPNGQLY NRDSSFQSHL
NSFEATSGMA PLLDNEKEEY IEMNDLLIPE LGASSTEKST EFLNHGEFGD VNEYDQLFND
ISVFQGTSTD LSCLSNFTNN TSGQRQQLLY EQFQYQTPEN QLNNYMHPST TLNQFTDNMW
FKDDQAALYV QPPQSSSGAF TSQSTGVMPE SMNPTMSVNP QYKEGQNGGG TRSQFSSALW
ELLESIPSTP ASACEGPLNQ TFVRMSSFSR IRFNGTSVTS RKVTVAKKRI SNRGFLLLSI
MGALCAIFWV FKATVGVMGR PLLS
