NFYB9_ARATH
ID NFYB9_ARATH Reviewed; 238 AA.
AC Q9SFD8; C0SUX1; O81130;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Nuclear transcription factor Y subunit B-9;
DE Short=AtNF-YB-9;
DE AltName: Full=Protein LEAFY COTYLEDON 1;
GN Name=NFYB9; Synonyms=LEC1; OrderedLocusNames=At1g21970; ORFNames=T26F17.20;
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] OF 1-235.
RX PubMed=20980269; DOI=10.1093/pcp/pcq161;
RA Mitsuda N., Ikeda M., Takada S., Takiguchi Y., Kondou Y., Yoshizumi T.,
RA Fujita M., Shinozaki K., Matsui M., Ohme-Takagi M.;
RT "Efficient yeast one-/two-hybrid screening using a library composed only of
RT transcription factors in Arabidopsis thaliana.";
RL Plant Cell Physiol. 51:2145-2151(2010).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-238.
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-238, FUNCTION, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=9657152; DOI=10.1016/s0092-8674(00)81463-4;
RA Lotan T., Ohto M.-A., Yee K.M., West M.A.L., Lo R., Kwong R.W.,
RA Yamagishi K., Fischer R.L., Goldberg R.B., Harada J.J.;
RT "Arabidopsis LEAFY COTYLEDON1 is sufficient to induce embryo development in
RT vegetative cells.";
RL Cell 93:1195-1205(1998).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=11250072; DOI=10.1016/s0378-1119(01)00323-7;
RA Gusmaroli G., Tonelli C., Mantovani R.;
RT "Regulation of the CCAAT-binding NF-Y subunits in Arabidopsis thaliana.";
RL Gene 264:173-185(2001).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11867211; DOI=10.1016/s0378-1119(01)00833-2;
RA Gusmaroli G., Tonelli C., Mantovani R.;
RT "Regulation of novel members of the Arabidopsis thaliana CCAAT-binding
RT nuclear factor Y subunits.";
RL Gene 283:41-48(2002).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF ASP-85.
RX PubMed=12578989; DOI=10.1073/pnas.0437909100;
RA Lee H., Fischer R.L., Goldberg R.B., Harada J.J.;
RT "Arabidopsis LEAFY COTYLEDON1 represents a functionally specialized subunit
RT of the CCAAT binding transcription factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2152-2156(2003).
RN [9]
RP FUNCTION.
RX PubMed=15695450; DOI=10.1093/pcp/pci048;
RA Kagaya Y., Toyoshima R., Okuda R., Usui H., Yamamoto A., Hattori T.;
RT "LEAFY COTYLEDON1 controls seed storage protein genes through its
RT regulation of FUSCA3 and ABSCISIC ACID INSENSITIVE3.";
RL Plant Cell Physiol. 46:399-406(2005).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION WITH
RP PRN1.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=17322342; DOI=10.1104/pp.106.089904;
RA Warpeha K.M., Upadhyay S., Yeh J., Adamiak J., Hawkins S.I., Lapik Y.R.,
RA Anderson M.B., Kaufman L.S.;
RT "The GCR1, GPA1, PRN1, NF-Y signal chain mediates both blue light and
RT abscisic acid responses in Arabidopsis.";
RL Plant Physiol. 143:1590-1600(2007).
CC -!- FUNCTION: Component of the NF-Y/HAP transcription factor complex. The
CC NF-Y complex stimulates the transcription of various genes by
CC recognizing and binding to a CCAAT motif in promoters. Acts as a
CC central regulator of the embryogenesis. Required for the speciation of
CC cotyledon identity and the completion of embryo maturation. Controls
CC seed storage protein genes through the regulation of FUS3 and ABI3.
CC Involved in the blue light (BL) and abscisic acid (ABA) signaling
CC pathways. {ECO:0000269|PubMed:12578989, ECO:0000269|PubMed:15695450,
CC ECO:0000269|PubMed:17322342, ECO:0000269|PubMed:9657152}.
CC -!- SUBUNIT: Heterotrimeric transcription factor composed of three
CC components, NF-YA, NF-YB and NF-YC. NF-YB and NF-YC must interact and
CC dimerize for NF-YA association and DNA binding (By similarity).
CC Interacts with PRN1. {ECO:0000250, ECO:0000269|PubMed:17322342}.
CC -!- INTERACTION:
CC Q9SFD8; Q94ID6: ERF12; NbExp=3; IntAct=EBI-2475789, EBI-4446727;
CC Q9SFD8; Q9MAI5: ERF8; NbExp=3; IntAct=EBI-2475789, EBI-2000137;
CC Q9SFD8; Q9C5X0: IAA34; NbExp=3; IntAct=EBI-2475789, EBI-3946459;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in green siliques. Present in etiolated
CC seedlings. {ECO:0000269|PubMed:11250072, ECO:0000269|PubMed:17322342}.
CC -!- DEVELOPMENTAL STAGE: Accumulates during seed development in embryo cell
CC types and in endosperm tissue. {ECO:0000269|PubMed:9657152}.
CC -!- DISRUPTION PHENOTYPE: Altered response to blue light (BL) and abscisic
CC acid (ABA). {ECO:0000269|PubMed:17322342}.
CC -!- SIMILARITY: Belongs to the NFYB/HAP3 subunit family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC39488.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF16537.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC013482; AAF16537.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30179.1; -; Genomic_DNA.
DR EMBL; AB493474; BAH30312.1; -; mRNA.
DR EMBL; BX817269; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF036684; AAC39488.1; ALT_INIT; Genomic_DNA.
DR PIR; G86352; G86352.
DR RefSeq; NP_173616.2; NM_102046.5.
DR AlphaFoldDB; Q9SFD8; -.
DR SMR; Q9SFD8; -.
DR BioGRID; 24039; 17.
DR IntAct; Q9SFD8; 4.
DR STRING; 3702.AT1G21970.1; -.
DR PaxDb; Q9SFD8; -.
DR PRIDE; Q9SFD8; -.
DR ProteomicsDB; 251170; -.
DR EnsemblPlants; AT1G21970.1; AT1G21970.1; AT1G21970.
DR GeneID; 838800; -.
DR Gramene; AT1G21970.1; AT1G21970.1; AT1G21970.
DR KEGG; ath:AT1G21970; -.
DR Araport; AT1G21970; -.
DR TAIR; locus:2201163; AT1G21970.
DR eggNOG; KOG0869; Eukaryota.
DR HOGENOM; CLU_066247_4_0_1; -.
DR InParanoid; Q9SFD8; -.
DR OMA; NGMPAFD; -.
DR OrthoDB; 1529111at2759; -.
DR PRO; PR:Q9SFD8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SFD8; baseline and differential.
DR Genevisible; Q9SFD8; AT.
DR GO; GO:0016602; C:CCAAT-binding factor complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:TAIR.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0009785; P:blue light signaling pathway; IMP:UniProtKB.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:TAIR.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010262; P:somatic embryogenesis; IMP:TAIR.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR027113; Transc_fact_NFYB/HAP3.
DR InterPro; IPR003956; Transcrpt_fac_NFYB/HAP3_CS.
DR PANTHER; PTHR11064; PTHR11064; 1.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00685; NFYB_HAP3; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Activator; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..238
FT /note="Nuclear transcription factor Y subunit B-9"
FT /id="PRO_0000204623"
FT DNA_BIND 64..70
FT /evidence="ECO:0000250"
FT REGION 91..102
FT /note="Subunit association domain (SAD)"
FT /evidence="ECO:0000250"
FT REGION 203..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 85
FT /note="D->K: Affects function."
FT /evidence="ECO:0000269|PubMed:12578989"
FT CONFLICT 17
FT /note="S -> T (in Ref. 4; BX817269)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="V -> I (in Ref. 5; AAC39488)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 238 AA; 26070 MW; 7B5444BB1DD0A7EA CRC64;
MERGAPFSHY QLPKSISELN LDQHSNNPTP MTSSVVVAGA GDKNNGIVVQ QQPPCVAREQ
DQYMPIANVI RIMRKTLPSH AKISDDAKET IQECVSEYIS FVTGEANERC QREQRKTITA
EDILWAMSKL GFDNYVDPLT VFINRYREIE TDRGSALRGE PPSLRQTYGG NGIGFHGPSH
GLPPPGPYGY GMLDQSMVMG GGRYYQNGSS GQDESSVGGG SSSSINGMPA FDHYGQYK
