NFYB6_ARATH
ID NFYB6_ARATH Reviewed; 234 AA.
AC Q84W66; Q8GV55; Q9FGJ0;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Nuclear transcription factor Y subunit B-6 {ECO:0000303|PubMed:11250072};
DE Short=AtNF-YB-6 {ECO:0000303|PubMed:11250072};
DE Short=AtNF-YB6 {ECO:0000303|PubMed:25490919};
DE AltName: Full=Protein LEAFY COTYLEDON 1-LIKE {ECO:0000303|PubMed:12509518};
GN Name=NFYB6 {ECO:0000303|PubMed:11250072};
GN Synonyms=L1L {ECO:0000303|PubMed:12509518};
GN OrderedLocusNames=At5g47670 {ECO:0000312|Araport:AT5G47670};
GN ORFNames=MNJ7.26 {ECO:0000312|EMBL:BAB09093.1};
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND FUNCTION.
RX PubMed=12509518; DOI=10.1105/tpc.006973;
RA Kwong R.W., Bui A.Q., Lee H., Kwong L.W., Fischer R.L., Goldberg R.B.,
RA Harada J.J.;
RT "LEAFY COTYLEDON1-LIKE defines a class of regulators essential for embryo
RT development.";
RL Plant Cell 15:5-18(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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] (ISOFORM 2).
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 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 [6]
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 [7]
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).
RN [8]
RP INTERACTION WITH DPB3-1, AND INDUCTION BY DEHYDRATION.
RC STRAIN=cv. Columbia;
RX PubMed=25490919; DOI=10.1105/tpc.114.132928;
RA Sato H., Mizoi J., Tanaka H., Maruyama K., Qin F., Osakabe Y., Morimoto K.,
RA Ohori T., Kusakabe K., Nagata M., Shinozaki K., Yamaguchi-Shinozaki K.;
RT "Arabidopsis DPB3-1, a DREB2A interactor, specifically enhances heat
RT stress-induced gene expression by forming a heat stress-specific
RT transcriptional complex with NF-Y subunits.";
RL Plant Cell 26:4954-4973(2014).
RN [9]
RP REVIEW.
RX PubMed=28119722; DOI=10.3389/fpls.2016.02045;
RA Zhao H., Wu D., Kong F., Lin K., Zhang H., Li G.;
RT "The Arabidopsis thaliana Nuclear Factor Y Transcription Factors.";
RL Front. Plant Sci. 7:2045-2045(2016).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 55-147, AND SUBUNIT.
RX PubMed=27871811; DOI=10.1016/j.molp.2016.11.006;
RA Gnesutta N., Saad D., Chaves-Sanjuan A., Mantovani R., Nardini M.;
RT "Crystal Structure of the Arabidopsis thaliana L1L/NF-YC3 Histone-fold
RT Dimer Reveals Specificities of the LEC1 Family of NF-Y Subunits in
RT Plants.";
RL Mol. Plant 10:645-648(2017).
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. Plays a role in
CC the regulation of the embryogenesis. Involved in the abscisic acid
CC (ABA) signaling pathway. {ECO:0000269|PubMed:12509518,
CC ECO:0000269|PubMed:17322342}.
CC -!- SUBUNIT: Heterotrimeric transcription factor composed of three
CC components, NF-YA, NF-YB and NF-YC (PubMed:27871811). NF-YB and NF-YC
CC must interact and dimerize for NF-YA association and DNA binding
CC (PubMed:27871811). Interacts with PRN1 (PubMed:17322342). Binds
CC directly with DPB3-1 (PubMed:25490919). {ECO:0000269|PubMed:17322342,
CC ECO:0000269|PubMed:25490919, ECO:0000269|PubMed:27871811}.
CC -!- INTERACTION:
CC Q84W66; Q9LX49: PRN1; NbExp=2; IntAct=EBI-1751693, EBI-1606661;
CC Q84W66-2; Q9LN09: NF-YC10; NbExp=3; IntAct=EBI-15191739, EBI-4461992;
CC Q84W66-2; Q58CM8: NFYC10; NbExp=3; IntAct=EBI-15191739, EBI-15191737;
CC Q84W66-2; Q9FGP8: NFYC7; NbExp=3; IntAct=EBI-15191739, EBI-2466133;
CC Q84W66-2; Q4PSE2: NFYC8; NbExp=3; IntAct=EBI-15191739, EBI-15191571;
CC Q84W66-2; Q8L4B2: NFYC9; NbExp=3; IntAct=EBI-15191739, EBI-2466050;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q84W66-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q84W66-2; Sequence=VSP_016045;
CC -!- TISSUE SPECIFICITY: Expressed in roots, flowers and developing
CC siliques. Present in etiolated seedlings. {ECO:0000269|PubMed:11250072,
CC ECO:0000269|PubMed:12509518, ECO:0000269|PubMed:17322342}.
CC -!- DEVELOPMENTAL STAGE: Expressed primarily during seed development.
CC {ECO:0000269|PubMed:12509518}.
CC -!- INDUCTION: Enhanced by dehydration stress.
CC {ECO:0000269|PubMed:25490919}.
CC -!- DISRUPTION PHENOTYPE: Altered response to abscisic acid (ABA).
CC {ECO:0000269|PubMed:17322342}.
CC -!- SIMILARITY: Belongs to the NFYB/HAP3 subunit family. {ECO:0000305}.
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DR EMBL; AY138461; AAN15924.1; -; mRNA.
DR EMBL; AB025628; BAB09093.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95548.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95549.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69913.1; -; Genomic_DNA.
DR EMBL; BT004183; AAO42202.1; -; mRNA.
DR RefSeq; NP_001078727.1; NM_001085258.1. [Q84W66-2]
DR RefSeq; NP_001318754.1; NM_001344740.1. [Q84W66-1]
DR RefSeq; NP_199578.2; NM_124141.4. [Q84W66-1]
DR PDB; 5G49; X-ray; 2.30 A; A=55-147.
DR PDBsum; 5G49; -.
DR AlphaFoldDB; Q84W66; -.
DR SMR; Q84W66; -.
DR BioGRID; 20066; 21.
DR IntAct; Q84W66; 12.
DR STRING; 3702.AT5G47670.1; -.
DR PaxDb; Q84W66; -.
DR PRIDE; Q84W66; -.
DR ProteomicsDB; 250592; -. [Q84W66-1]
DR EnsemblPlants; AT5G47670.1; AT5G47670.1; AT5G47670. [Q84W66-1]
DR EnsemblPlants; AT5G47670.2; AT5G47670.2; AT5G47670. [Q84W66-2]
DR EnsemblPlants; AT5G47670.3; AT5G47670.3; AT5G47670. [Q84W66-1]
DR GeneID; 834818; -.
DR Gramene; AT5G47670.1; AT5G47670.1; AT5G47670. [Q84W66-1]
DR Gramene; AT5G47670.2; AT5G47670.2; AT5G47670. [Q84W66-2]
DR Gramene; AT5G47670.3; AT5G47670.3; AT5G47670. [Q84W66-1]
DR KEGG; ath:AT5G47670; -.
DR Araport; AT5G47670; -.
DR TAIR; locus:2169028; AT5G47670.
DR eggNOG; KOG0869; Eukaryota.
DR HOGENOM; CLU_066247_4_1_1; -.
DR InParanoid; Q84W66; -.
DR OMA; AEMNMRM; -.
DR PhylomeDB; Q84W66; -.
DR PRO; PR:Q84W66; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84W66; baseline and differential.
DR Genevisible; Q84W66; AT.
DR GO; GO:0016602; C:CCAAT-binding factor complex; IBA:GO_Central.
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:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
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 3D-structure; Abscisic acid signaling pathway; Activator;
KW Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..234
FT /note="Nuclear transcription factor Y subunit B-6"
FT /id="PRO_0000204620"
FT DNA_BIND 63..69
FT /evidence="ECO:0000250|UniProtKB:P13434"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..101
FT /note="Subunit association domain (SAD)"
FT /evidence="ECO:0000250"
FT REGION 206..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_016045"
FT CONFLICT 81
FT /note="K -> R (in Ref. 4; AAO42202)"
FT /evidence="ECO:0000305"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:5G49"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:5G49"
FT HELIX 84..112
FT /evidence="ECO:0007829|PDB:5G49"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:5G49"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:5G49"
FT HELIX 135..146
FT /evidence="ECO:0007829|PDB:5G49"
SQ SEQUENCE 234 AA; 26136 MW; EC100E830E5CBB31 CRC64;
MERGGFHGYR KLSVNNTTPS PPGLAANFLM AEGSMRPPEF NQPNKTSNGG EEECTVREQD
RFMPIANVIR IMRRILPAHA KISDDSKETI QECVSEYISF ITGEANERCQ REQRKTITAE
DVLWAMSKLG FDDYIEPLTL YLHRYRELEG ERGVSCSAGS VSMTNGLVVK RPNGTMTEYG
AYGPVPGIHM AQYHYRHQNG FVFSGNEPNS KMSGSSSGAS GARVEVFPTQ QHKY
