NAC8_ARATH
ID NAC8_ARATH Reviewed; 449 AA.
AC Q6NQK2; Q9C610; Q9C6M7;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=SUPPRESSOR OF GAMMA RESPONSE 1 {ECO:0000303|PubMed:19549833};
DE AltName: Full=NAC domain-containing protein 8 {ECO:0000303|PubMed:15029955};
DE Short=ANAC008 {ECO:0000303|PubMed:15029955};
DE AltName: Full=Protein SOG1;
DE AltName: Full=SUPPRESSOR OF GAMMA RADIATION 1;
GN Name=SOG1 {ECO:0000303|PubMed:19549833};
GN Synonyms=NAC008 {ECO:0000303|PubMed:15029955};
GN OrderedLocusNames=At1g25580 {ECO:0000312|Araport:AT1G25580};
GN ORFNames=F14G11.2 {ECO:0000312|EMBL:AAG50527.1},
GN F2J7.1 {ECO:0000312|EMBL:AAG50802.1};
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 [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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, AND MUTAGENESIS OF GLY-155.
RX PubMed=19549833; DOI=10.1073/pnas.0810304106;
RA Yoshiyama K., Conklin P.A., Huefner N.D., Britt A.B.;
RT "Suppressor of gamma response 1 (SOG1) encodes a putative transcription
RT factor governing multiple responses to DNA damage.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:12843-12848(2009).
RN [7]
RP FUNCTION.
RX PubMed=20634150; DOI=10.1016/j.dnarep.2010.06.006;
RA Furukawa T., Curtis M.J., Tominey C.M., Duong Y.H., Wilcox B.W.,
RA Aggoune D., Hays J.B., Britt A.B.;
RT "A shared DNA-damage-response pathway for induction of stem-cell death by
RT UVB and by gamma irradiation.";
RL DNA Repair 9:940-948(2010).
RN [8]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, LACK OF INDUCTION BY ZEOCIN,
RP PHOSPHORYLATION, AND MUTAGENESIS OF SER-350; SER-356; SER-372; SER-430 AND
RP SER-436.
RX PubMed=23907539; DOI=10.1038/embor.2013.112;
RA Yoshiyama K.O., Kobayashi J., Ogita N., Ueda M., Kimura S., Maki H.,
RA Umeda M.;
RT "ATM-mediated phosphorylation of SOG1 is essential for the DNA damage
RT response in Arabidopsis.";
RL EMBO Rep. 14:817-822(2013).
RN [9]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=24399300; DOI=10.1105/tpc.113.118943;
RA Yi D., Alvim Kamei C.L., Cools T., Vanderauwera S., Takahashi N.,
RA Okushima Y., Eekhout T., Yoshiyama K.O., Larkin J., Van den Daele H.,
RA Conklin P., Britt A., Umeda M., De Veylder L.;
RT "The Arabidopsis SIAMESE-RELATED cyclin-dependent kinase inhibitors SMR5
RT and SMR7 regulate the DNA damage checkpoint in response to reactive oxygen
RT species.";
RL Plant Cell 26:296-309(2014).
RN [10]
RP REVIEW.
RX PubMed=24736489; DOI=10.4161/psb.28889;
RA Yoshiyama K.O., Kimura S., Maki H., Britt A.B., Umeda M.;
RT "The role of SOG1, a plant-specific transcriptional regulator, in the DNA
RT damage response.";
RL Plant Signal. Behav. 9:E28889-E28889(2014).
RN [11]
RP FUNCTION.
RX PubMed=27658920; DOI=10.1111/gtc.12436;
RA Davis O.M., Ogita N., Inagaki S., Takahashi N., Umeda M.;
RT "DNA damage inhibits lateral root formation by up-regulating cytokinin
RT biosynthesis genes in Arabidopsis thaliana.";
RL Genes Cells 21:1195-1208(2016).
CC -!- FUNCTION: Transcription factor regulating the transcriptional
CC activation response to gamma irradiation (PubMed:19549833). Required
CC for stem-cell death induced by UVB or by gamma irradiation
CC (PubMed:20634150). Not required for ATM activation, but participates in
CC pathways governed by both ATM and ATR sensor kinases (PubMed:19549833).
CC Involved in DNA damage response (DDR) system that regulates cell cycle
CC arrest (PubMed:24399300). Functional homolog of animal p53
CC (PubMed:24736489). Regulates SMR5 and SMR7 transcription
CC (PubMed:24399300). Regulates DNA repair and cytokinin signaling
CC separately and plays a key role in controlling lateral root formation
CC under genotoxic stress. {ECO:0000269|PubMed:19549833,
CC ECO:0000269|PubMed:20634150, ECO:0000269|PubMed:24399300,
CC ECO:0000305|PubMed:24736489}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23907539}.
CC -!- TISSUE SPECIFICITY: Expressed in shoot and root apical meristems, in
CC lateral root primordia, in the vasculature of young leaves and in the
CC root stele. {ECO:0000269|PubMed:23907539}.
CC -!- INDUCTION: Not induced by zeocin or ionizing radiation treatment.
CC {ECO:0000269|PubMed:23907539}.
CC -!- DOMAIN: The NAC domain includes a DNA-binding domain and a dimerization
CC domain.
CC -!- PTM: Phosphorylated in a DNA stress-independent manner
CC (PubMed:23907539, PubMed:24399300). Hyperphosphorylated on SQ motifs
CC upon double-strand breaks, H(2)O(2) or zeocin treatments
CC (PubMed:23907539, PubMed:24399300). Hyperphosphorylation is required
CC for SOG1 function, and unlike constitutive phosphorylation, is ATM
CC dependent (PubMed:23907539). {ECO:0000269|PubMed:23907539,
CC ECO:0000269|PubMed:24399300}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50527.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG50802.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC079281; AAG50802.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC084221; AAG50527.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30644.1; -; Genomic_DNA.
DR EMBL; BT010450; AAQ62870.1; -; mRNA.
DR EMBL; AK221266; BAD93935.1; -; mRNA.
DR EMBL; AK228316; BAF00259.1; -; mRNA.
DR PIR; C86386; C86386.
DR RefSeq; NP_564238.2; NM_102369.3.
DR AlphaFoldDB; Q6NQK2; -.
DR SMR; Q6NQK2; -.
DR BioGRID; 24382; 1.
DR STRING; 3702.AT1G25580.1; -.
DR iPTMnet; Q6NQK2; -.
DR PaxDb; Q6NQK2; -.
DR PRIDE; Q6NQK2; -.
DR ProteomicsDB; 251239; -.
DR EnsemblPlants; AT1G25580.1; AT1G25580.1; AT1G25580.
DR GeneID; 839145; -.
DR Gramene; AT1G25580.1; AT1G25580.1; AT1G25580.
DR KEGG; ath:AT1G25580; -.
DR Araport; AT1G25580; -.
DR TAIR; locus:2031170; AT1G25580.
DR eggNOG; ENOG502QYVC; Eukaryota.
DR HOGENOM; CLU_025101_0_0_1; -.
DR InParanoid; Q6NQK2; -.
DR OMA; ACPRCNH; -.
DR OrthoDB; 834330at2759; -.
DR PhylomeDB; Q6NQK2; -.
DR PRO; PR:Q6NQK2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6NQK2; baseline and differential.
DR Genevisible; Q6NQK2; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0000077; P:DNA damage checkpoint signaling; IMP:TAIR.
DR GO; GO:0040020; P:regulation of meiotic nuclear division; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0010332; P:response to gamma radiation; IMP:TAIR.
DR Gene3D; 2.170.150.80; -; 1.
DR InterPro; IPR003441; NAC-dom.
DR InterPro; IPR036093; NAC_dom_sf.
DR InterPro; IPR044799; SOG1-like.
DR PANTHER; PTHR31079; PTHR31079; 1.
DR Pfam; PF02365; NAM; 1.
DR SUPFAM; SSF101941; SSF101941; 1.
DR PROSITE; PS51005; NAC; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..449
FT /note="SUPPRESSOR OF GAMMA RESPONSE 1"
FT /id="PRO_0000376616"
FT DOMAIN 58..211
FT /note="NAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT DNA_BIND 167..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT REGION 324..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 155
FT /note="G->R: In sog1-1; loss of rapid transcriptional
FT response to gamma radiation."
FT /evidence="ECO:0000269|PubMed:19549833"
FT MUTAGEN 350
FT /note="S->A: Loss of hyperphosphorylation; when associated
FT with A-356; A-372; A-430 and A-436."
FT /evidence="ECO:0000269|PubMed:23907539"
FT MUTAGEN 356
FT /note="S->A: Loss of hyperphosphorylation; when associated
FT with A-350; A-372; A-430 and A-436."
FT /evidence="ECO:0000269|PubMed:23907539"
FT MUTAGEN 372
FT /note="S->A: Loss of hyperphosphorylation; when associated
FT with A-350; A-356; A-430 and A-436."
FT /evidence="ECO:0000269|PubMed:23907539"
FT MUTAGEN 430
FT /note="S->A: Loss of hyperphosphorylation; when associated
FT with A-356; A-372; A-430 and A-436."
FT /evidence="ECO:0000269|PubMed:23907539"
FT MUTAGEN 436
FT /note="S->A: Loss of hyperphosphorylation; when associated
FT with A-356; A-372; A-430 and A-430."
FT /evidence="ECO:0000269|PubMed:23907539"
SQ SEQUENCE 449 AA; 50289 MW; 56929C0ED10009EA CRC64;
MAGRSWLIDS NRIATKIMSA SASSDPRQVV WKSNPSRHCP KCQHVIDNSD VVDDWPGLPR
GVKFDPSDPE IIWHLLAKSG LSGLSSHPFI DEFIPTVNQD DGICYTHPKN LPGVKSDGTV
SHFFHKAIKA YSTGTRKRRK IHDDDFGDVR WHKTGRTKPV VLDGVQRGCK KIMVLYGGKA
VKTNWVMHQY HLGIEEDEKE GDYVVSKIFY QQPQQLVVKR GDKAEQEVSE DIFAAVTPTA
DPVTPKLATP EPRNAVRICS DSHIASDYVT PSDYVSAHEV SLAETSEVMC MEDEVQSIQP
NHERPSSGPE LEHGLENGAK EMLDDKEEQE KDRDNENQGE EDPTWFDSGS QFILNSQQLV
EALSLCDDLL GSQDREENTN SGSLKDKQPC IADYAHLGPE DFKRDLEECQ KIVLDPSNIE
LDTPPEFRLS QLEFGSQDSF LAWGTGKTD
