NAC19_ARATH
ID NAC19_ARATH Reviewed; 317 AA.
AC Q9C932;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=NAC domain-containing protein 19;
DE Short=ANAC019;
DE AltName: Full=Abscisic-acid-responsive NAC;
DE Short=ANAC;
GN Name=NAC019; Synonyms=ANAC; OrderedLocusNames=At1g52890;
GN ORFNames=F14G24.16;
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 [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP INDUCTION, AND INTERACTION WITH RHA2A; RHA2B; RHA3A; RHA3B AND RHG1A.
RX PubMed=12646039; DOI=10.1042/bj20021123;
RA Greve K., La Cour T., Jensen M.K., Poulsen F.M., Skriver K.;
RT "Interactions between plant RING-H2 and plant-specific NAC
RT (NAM/ATAF1/2/CUC2) proteins: RING-H2 molecular specificity and cellular
RT localization.";
RL Biochem. J. 371:97-108(2003).
RN [2]
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 [3]
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 [4]
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 [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, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15319476; DOI=10.1105/tpc.104.022699;
RA Tran L.-S.H., Nakashima K., Sakuma Y., Simpson S.D., Fujita Y.,
RA Maruyama K., Fujita M., Seki M., Shinozaki K., Yamaguchi-Shinozaki K.;
RT "Isolation and functional analysis of Arabidopsis stress-inducible NAC
RT transcription factors that bind to a drought-responsive cis-element in the
RT early responsive to dehydration stress 1 promoter.";
RL Plant Cell 16:2481-2498(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-163.
RX PubMed=15083810; DOI=10.1038/sj.embor.7400093;
RA Ernst H.A., Olsen A.N., Larsen S., Lo Leggio L.;
RT "Structure of the conserved domain of ANAC, a member of the NAC family of
RT transcription factors.";
RL EMBO Rep. 5:297-303(2004).
CC -!- FUNCTION: Transcription factors that bind specifically to the 5'-
CC CATGTG-3' motif. {ECO:0000269|PubMed:15319476}.
CC -!- SUBUNIT: Dimer. Interacts with RHA2A, RHA2B or RHG1A, but not with
CC RHA3A or RHA3B. {ECO:0000269|PubMed:12646039}.
CC -!- INTERACTION:
CC Q9C932; Q9ZT50: RHA2A; NbExp=3; IntAct=EBI-1786615, EBI-2025293;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353,
CC ECO:0000269|PubMed:12646039}.
CC -!- TISSUE SPECIFICITY: Expressed in stems, flowers, cauline leaves and
CC rosettes. {ECO:0000269|PubMed:12646039, ECO:0000269|PubMed:15319476}.
CC -!- INDUCTION: Induced by drought, high salinity and abscisic acid (ABA).
CC Slightly up-regulated by jasmonic acid. Not induced by cold treatment.
CC {ECO:0000269|PubMed:12646039, ECO:0000269|PubMed:15319476}.
CC -!- DOMAIN: The NAC domain includes a DNA-binding domain and a dimerization
CC domain.
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DR EMBL; AC019018; AAG52283.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32864.1; -; Genomic_DNA.
DR EMBL; AY065268; AAL38744.1; -; mRNA.
DR EMBL; AY117224; AAM51299.1; -; mRNA.
DR PIR; B96570; B96570.
DR RefSeq; NP_175697.1; NM_104167.6.
DR PDB; 1UT4; X-ray; 2.50 A; A/B=1-168.
DR PDB; 1UT7; X-ray; 1.90 A; A/B=1-168.
DR PDB; 3SWM; X-ray; 4.25 A; A/B/C/D=1-168.
DR PDB; 3SWP; X-ray; 4.11 A; A/B/C/D=1-168.
DR PDB; 4DUL; X-ray; 3.00 A; A/B=1-168.
DR PDBsum; 1UT4; -.
DR PDBsum; 1UT7; -.
DR PDBsum; 3SWM; -.
DR PDBsum; 3SWP; -.
DR PDBsum; 4DUL; -.
DR AlphaFoldDB; Q9C932; -.
DR SMR; Q9C932; -.
DR BioGRID; 26947; 18.
DR IntAct; Q9C932; 6.
DR STRING; 3702.AT1G52890.1; -.
DR PaxDb; Q9C932; -.
DR PRIDE; Q9C932; -.
DR ProteomicsDB; 251032; -.
DR DNASU; 841722; -.
DR EnsemblPlants; AT1G52890.1; AT1G52890.1; AT1G52890.
DR GeneID; 841722; -.
DR Gramene; AT1G52890.1; AT1G52890.1; AT1G52890.
DR KEGG; ath:AT1G52890; -.
DR Araport; AT1G52890; -.
DR TAIR; locus:2011531; AT1G52890.
DR eggNOG; ENOG502QRBC; Eukaryota.
DR HOGENOM; CLU_035664_8_4_1; -.
DR InParanoid; Q9C932; -.
DR OMA; VPNLEYN; -.
DR OrthoDB; 925823at2759; -.
DR PhylomeDB; Q9C932; -.
DR EvolutionaryTrace; Q9C932; -.
DR PRO; PR:Q9C932; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C932; baseline and differential.
DR Genevisible; Q9C932; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
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 3D-structure; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..317
FT /note="NAC domain-containing protein 19"
FT /id="PRO_0000132309"
FT DOMAIN 14..162
FT /note="NAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1UT4"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1UT7"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:1UT7"
FT HELIX 32..36
FT /evidence="ECO:0007829|PDB:1UT7"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1UT7"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1UT7"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1UT7"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:1UT7"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1UT7"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:1UT7"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1UT7"
FT STRAND 93..106
FT /evidence="ECO:0007829|PDB:1UT7"
FT STRAND 109..123
FT /evidence="ECO:0007829|PDB:1UT7"
FT STRAND 128..139
FT /evidence="ECO:0007829|PDB:1UT7"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:1UT7"
SQ SEQUENCE 317 AA; 35815 MW; 167EE787F05E3B45 CRC64;
MGIQETDPLT QLSLPPGFRF YPTDEELMVQ YLCRKAAGYD FSLQLIAEID LYKFDPWVLP
NKALFGEKEW YFFSPRDRKY PNGSRPNRVA GSGYWKATGT DKIISTEGQR VGIKKALVFY
IGKAPKGTKT NWIMHEYRLI EPSRRNGSTK LDDWVLCRIY KKQSSAQKQV YDNGIANARE
FSNNGTSSTT SSSSHFEDVL DSFHQEIDNR NFQFSNPNRI SSLRPDLTEQ KTGFHGLADT
SNFDWASFAG NVEHNNSVPE LGMSHVVPNL EYNCGYLKTE EEVESSHGFN NSGELAQKGY
GVDSFGYSGQ VGGFGFM
