NAC20_ORYSJ
ID NAC20_ORYSJ Reviewed; 320 AA.
AC Q9FTY0; A0A0P0UXL6;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=NAC domain-containing protein 20 {ECO:0000303|PubMed:18813954};
DE Short=ONAC020 {ECO:0000303|PubMed:18813954};
DE Short=OsNAC20 {ECO:0000303|PubMed:32989010};
GN Name=NAC20 {ECO:0000303|PubMed:18813954}; Synonyms=DLN1 {ECO:0000305};
GN OrderedLocusNames=Os01g0104500 {ECO:0000312|EMBL:BAS69958.1},
GN LOC_Os01g01470 {ECO:0000305};
GN ORFNames=OsJ_00037 {ECO:0000312|EMBL:EAZ10206.1},
GN P0436E04.23 {ECO:0000312|EMBL:BAB16335.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Immature seed;
RA Yoon U.H., Kim Y.H.;
RT "Structural analysis of expressed sequence tags in immature seed of Oryza
RT sativa L.";
RL Sigmul Saengmyeong Gong Haghoeji 36:130-136(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RG The rice full-length cDNA consortium;
RT "Oryza sativa full length cDNA.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18813954; DOI=10.1007/s00438-008-0386-6;
RA Fang Y., You J., Xie K., Xie W., Xiong L.;
RT "Systematic sequence analysis and identification of tissue-specific or
RT stress-responsive genes of NAC transcription factor family in rice.";
RL Mol. Genet. Genomics 280:547-563(2008).
RN [9]
RP INTERACTION WITH NAC26, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27872632; DOI=10.3389/fpls.2016.01638;
RA Mathew I.E., Das S., Mahto A., Agarwal P.;
RT "Three rice NAC transcription factors heteromerize and are associated with
RT seed size.";
RL Front. Plant Sci. 7:1638-1638(2016).
RN [10]
RP FUNCTION, INTERACTION WITH NAC26, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=32989010; DOI=10.1104/pp.20.00984;
RA Wang J., Chen Z., Zhang Q., Meng S., Wei C.;
RT "The NAC transcription factors OsNAC20 and OsNAC26 regulate starch and
RT storage protein synthesis.";
RL Plant Physiol. 184:1775-1791(2020).
CC -!- FUNCTION: Transcription factor that acts redundantly with NAC26 to
CC regulate the expression of genes involved in the biosynthesis of starch
CC and storage proteins in grain (PubMed:32989010). Directly binds to the
CC promoters of starch synthase 1 (SS1), pullulanase (PUL), glutelin A1
CC (GLUA1), glutelins B4 and B5 (GLUB4 and GLUB5), alpha-globulin and 16
CC kDa prolamin, and activates their expression (PubMed:32989010).
CC {ECO:0000269|PubMed:32989010}.
CC -!- SUBUNIT: Forms homodimers (PubMed:32989010). Forms heterodimers with
CC NAC26 (PubMed:27872632, PubMed:32989010). {ECO:0000269|PubMed:27872632,
CC ECO:0000269|PubMed:32989010}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353,
CC ECO:0000269|PubMed:32989010}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:27872632}.
CC -!- TISSUE SPECIFICITY: Expressed in developing seeds (PubMed:27872632).
CC Expressed in developing endosperm (PubMed:32989010).
CC {ECO:0000269|PubMed:27872632, ECO:0000269|PubMed:32989010}.
CC -!- DOMAIN: The NAC domain includes a DNA binding domain and a dimerization
CC domain. {ECO:0000255|PROSITE-ProRule:PRU00353}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:32989010). The double mutant nac20 and nac26 exhibit
CC a floury grain phenotype due to decreased starch and storage protein
CC content (PubMed:32989010). {ECO:0000269|PubMed:32989010}.
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DR EMBL; GU120353; ADR66987.1; -; mRNA.
DR EMBL; JN944365; AFI71276.1; -; mRNA.
DR EMBL; AP002818; BAB16335.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF03679.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS69958.1; -; Genomic_DNA.
DR EMBL; CM000138; EAZ10206.1; -; Genomic_DNA.
DR EMBL; AK242268; BAH01242.1; -; mRNA.
DR RefSeq; XP_015621005.1; XM_015765519.1.
DR AlphaFoldDB; Q9FTY0; -.
DR SMR; Q9FTY0; -.
DR STRING; 4530.OS01T0104500-01; -.
DR PaxDb; Q9FTY0; -.
DR PRIDE; Q9FTY0; -.
DR EnsemblPlants; Os01t0104500-01; Os01t0104500-01; Os01g0104500.
DR GeneID; 4326295; -.
DR Gramene; Os01t0104500-01; Os01t0104500-01; Os01g0104500.
DR KEGG; osa:4326295; -.
DR eggNOG; ENOG502QSPY; Eukaryota.
DR HOGENOM; CLU_035664_6_0_1; -.
DR InParanoid; Q9FTY0; -.
DR OMA; LMAPPSY; -.
DR OrthoDB; 1360519at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:2000014; P:regulation of endosperm development; 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 DNA-binding; Endoplasmic reticulum; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..320
FT /note="NAC domain-containing protein 20"
FT /id="PRO_0000452670"
FT DOMAIN 14..170
FT /note="NAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT DNA_BIND 114..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
SQ SEQUENCE 320 AA; 35727 MW; E15E94F8B9DFBA2E CRC64;
MGEQQQQVER QPDLPPGFRF HPTDEEIITF YLAPKVVDSR GFCVAAIGEV DLNKCEPWDL
PGKAKMNGEK EWYFYCQKDR KYPTGMRTNR ATEAGYWKAT GKDKEIFRDH HMLIGMKKTL
VFYKGRAPKG DKTNWVMHEY RLADASPPPP PSSAEPPRQD DWAVCRIFHK SSGIKKPVPV
APHQVPAAAN YQQQQQMAMA SAGIIQVPMQ MQMPSMSDQL QMLDDFSTTA SLSLMAPPSY
STLPAGFPLQ INSGAHPQQF VGNPSMYYHQ QQQMDMAGGG FVVSEPSSLV VSPQDAADQN
NNAADISSMA CNMDAAIWKY
