NAC31_ARATH
ID NAC31_ARATH Reviewed; 334 AA.
AC Q9S851;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Protein CUP-SHAPED COTYLEDON 3;
DE AltName: Full=NAC domain-containing protein 31;
DE Short=ANAC031;
DE AltName: Full=NAC domain-containing protein CUC3;
GN Name=NAC031; Synonyms=CUC3, NAC368; OrderedLocusNames=At1g76420;
GN ORFNames=F14G6.2, F15M4.8;
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], FUNCTION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Landsberg erecta; TISSUE=Flower;
RX PubMed=12837947; DOI=10.1105/tpc.012203;
RA Vroemen C.W., Mordhorst A.P., Albrecht C., Kwaaitaal M.A.C.J.,
RA de Vries S.C.;
RT "The CUP-SHAPED COTYLEDON3 gene is required for boundary and shoot meristem
RT formation in Arabidopsis.";
RL Plant Cell 15:1563-1577(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 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 [5]
RP INDUCTION BY BRM.
RX PubMed=16854978; DOI=10.1242/dev.02508;
RA Kwon C.S., Hibara K., Pfluger J., Bezhani S., Metha H., Aida M., Tasaka M.,
RA Wagner D.;
RT "A role for chromatin remodeling in regulation of CUC gene expression in
RT the Arabidopsis cotyledon boundary.";
RL Development 133:3223-3230(2006).
RN [6]
RP FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF GLY-25 AND PRO-30.
RX PubMed=17122068; DOI=10.1105/tpc.106.045716;
RA Hibara K., Karim M.R., Takada S., Taoka K., Furutani M., Aida M.,
RA Tasaka M.;
RT "Arabidopsis CUP-SHAPED COTYLEDON3 regulates postembryonic shoot meristem
RT and organ boundary formation.";
RL Plant Cell 18:2946-2957(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
CC -!- FUNCTION: Transcription activator. Involved in molecular mechanisms
CC regulating shoot apical meristem (SAM) formation during embryogenesis
CC and organ separation. Required for axillary meristem initiation and
CC separation of the meristem from the main stem. May act as an inhibitor
CC of cell division. {ECO:0000269|PubMed:12837947,
CC ECO:0000269|PubMed:17122068}.
CC -!- INTERACTION:
CC Q9S851; Q9SW09: RPS10A; NbExp=3; IntAct=EBI-15206626, EBI-4459297;
CC Q9S851; Q9LTF2: RPS10C; NbExp=3; IntAct=EBI-15206626, EBI-4458966;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In a general manner, present at the boundaries
CC between mersitems and araising primordia.
CC {ECO:0000269|PubMed:12837947}.
CC -!- DEVELOPMENTAL STAGE: First expressed at the globular stage, mostly in
CC the apical part of the embryo. During the triangular stage, confined to
CC the boundary of emerging cotyledons. Later restricted to the center of
CC the apical part of the embryo and to seedling apex, at the boundaries
CC of the cotyledon margins and the boundaries between the SAM and the
CC cotyledons. Localized in a one-cell-wide ring at the boundary between
CC trichomes or lateral roots and epidermis. Accumulates at the boundaries
CC between leaf primordia and the shoot meristem and between floral
CC primordia and the inflorescence meristem. Found in the adaxial axils of
CC secondary inflorescences and pedicels, and in axiallary buds. In
CC flowers, expressed in a ring at the bases of sepals and petals. In
CC carpels, confined to the boundaries between ovule primordia. In ovules,
CC localized in a ring at the boundary between the nucellus and the
CC chalaza. In the mature embryo sac, detected in the two polar nuclei of
CC the central cell. {ECO:0000269|PubMed:12837947,
CC ECO:0000269|PubMed:17122068}.
CC -!- INDUCTION: By BRM, at the chromatin level, and conferring a very
CC specific spatial expression pattern. {ECO:0000269|PubMed:16854978}.
CC -!- DOMAIN: The NAC domain includes a DNA-binding domain and a dimerization
CC domain, and confers the specificity of the transactivated target genes.
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DR EMBL; AF543194; AAP82630.1; -; Genomic_DNA.
DR EMBL; AC012394; AAF16659.1; -; Genomic_DNA.
DR EMBL; AC015450; AAG51953.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35839.1; -; Genomic_DNA.
DR PIR; H96791; H96791.
DR RefSeq; NP_177768.1; NM_106292.3.
DR AlphaFoldDB; Q9S851; -.
DR SMR; Q9S851; -.
DR BioGRID; 29194; 10.
DR IntAct; Q9S851; 6.
DR STRING; 3702.AT1G76420.1; -.
DR iPTMnet; Q9S851; -.
DR PaxDb; Q9S851; -.
DR PRIDE; Q9S851; -.
DR DNASU; 843975; -.
DR EnsemblPlants; AT1G76420.1; AT1G76420.1; AT1G76420.
DR GeneID; 843975; -.
DR Gramene; AT1G76420.1; AT1G76420.1; AT1G76420.
DR KEGG; ath:AT1G76420; -.
DR Araport; AT1G76420; -.
DR TAIR; locus:2011736; AT1G76420.
DR eggNOG; ENOG502QQ8S; Eukaryota.
DR HOGENOM; CLU_035664_4_0_1; -.
DR InParanoid; Q9S851; -.
DR OMA; HSHRHTC; -.
DR OrthoDB; 910638at2759; -.
DR PhylomeDB; Q9S851; -.
DR PRO; PR:Q9S851; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S851; baseline and differential.
DR Genevisible; Q9S851; AT.
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:0010014; P:meristem initiation; IGI:TAIR.
DR GO; GO:0010199; P:organ boundary specification between lateral organs and the meristem; IGI: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 Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..334
FT /note="Protein CUP-SHAPED COTYLEDON 3"
FT /id="PRO_0000312288"
FT DOMAIN 22..171
FT /note="NAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT DNA_BIND 121..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT MUTAGEN 25
FT /note="G->D: In cuc3-104; cup-shaped cotyledon and abnormal
FT SAM."
FT /evidence="ECO:0000269|PubMed:17122068"
FT MUTAGEN 30
FT /note="P->S: In cuc3-102; cup-shaped cotyledon and abnormal
FT SAM."
FT /evidence="ECO:0000269|PubMed:17122068"
SQ SEQUENCE 334 AA; 38018 MW; 008EF8F3F3220F07 CRC64;
MMLAVEDVLS ELAGEERNER GLPPGFRFHP TDEELITFYL ASKIFHGGLS GIHISEVDLN
RCEPWELPEM AKMGEREWYF YSLRDRKYPT GLRTNRATTA GYWKATGKDK EVFSGGGGQL
VGMKKTLVFY KGRAPRGLKT KWVMHEYRLE NDHSHRHTCK EEWVICRVFN KTGDRKNVGL
IHNQISYLHN HSLSTTHHHH HEALPLLIEP SNKTLTNFPS LLYDDPHQNY NNNNFLHGSS
GHNIDELKAL INPVVSQLNG IIFPSGNNNN DEDDFDFNLG VKTEQSSNGN EIDVRDYLEN
PLFQEASYGL LGFSSSPGPL HMLLDSPCPL GFQL
