DPB4_ARATH
ID DPB4_ARATH Reviewed; 275 AA.
AC Q9ZQH2;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=DNA polymerase II subunit B4 {ECO:0000303|PubMed:25490919};
DE AltName: Full=Nuclear transcription factor Y subunit B-11 {ECO:0000303|PubMed:25490919};
DE Short=AtNF-YB11 {ECO:0000303|PubMed:25490919};
GN Name=NF-YB11 {ECO:0000303|PubMed:25490919};
GN Synonyms=DPB4 {ECO:0000303|PubMed:25490919};
GN OrderedLocusNames=At2g27470 {ECO:0000312|Araport:AT2G27470};
GN ORFNames=F10A12.15 {ECO:0000312|EMBL:AAD15599.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 [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 [4]
RP INTERACTION WITH DPB3-1, AND REPRESSION BY HEAT STRESS AND 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 [5]
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).
CC -!- FUNCTION: Component of the NF-Y/HAP transcription factor complex (By
CC similarity). The NF-Y complex stimulates the transcription of various
CC genes by recognizing and binding to a CCAAT motif in promoters (By
CC similarity). {ECO:0000250|UniProtKB:Q84W66}.
CC -!- SUBUNIT: Heterotrimeric transcription factor composed of three
CC components, NF-YA, NF-YB and NF-YC (By similarity). NF-YB and NF-YC
CC must interact and dimerize for NF-YA association and DNA binding (By
CC similarity). Binds directly with DPB3-1 (PubMed:25490919).
CC {ECO:0000250|UniProtKB:P23511, ECO:0000269|PubMed:25490919}.
CC -!- INTERACTION:
CC Q9ZQH2; Q9LN09: NF-YC10; NbExp=3; IntAct=EBI-15202674, EBI-4461992;
CC Q9ZQH2; Q9FHS0: NF-YC13; NbExp=3; IntAct=EBI-15202674, EBI-15202676;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- INDUCTION: Repressed by heat and dehydration stress.
CC {ECO:0000269|PubMed:25490919}.
CC -!- SIMILARITY: Belongs to the NFYB/HAP3 subunit family. {ECO:0000305}.
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DR EMBL; AC006232; AAD15599.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08000.1; -; Genomic_DNA.
DR EMBL; BT004083; AAO42110.1; -; mRNA.
DR PIR; C84673; C84673.
DR RefSeq; NP_180316.1; NM_128307.6.
DR AlphaFoldDB; Q9ZQH2; -.
DR SMR; Q9ZQH2; -.
DR IntAct; Q9ZQH2; 3.
DR STRING; 3702.AT2G27470.1; -.
DR PaxDb; Q9ZQH2; -.
DR PRIDE; Q9ZQH2; -.
DR ProteomicsDB; 192018; -.
DR EnsemblPlants; AT2G27470.1; AT2G27470.1; AT2G27470.
DR GeneID; 817292; -.
DR Gramene; AT2G27470.1; AT2G27470.1; AT2G27470.
DR KEGG; ath:AT2G27470; -.
DR Araport; AT2G27470; -.
DR TAIR; locus:2038648; AT2G27470.
DR eggNOG; KOG0870; Eukaryota.
DR HOGENOM; CLU_066247_7_0_1; -.
DR InParanoid; Q9ZQH2; -.
DR OMA; HKEHITI; -.
DR OrthoDB; 1572458at2759; -.
DR PhylomeDB; Q9ZQH2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZQH2; baseline and differential.
DR GO; GO:0008623; C:CHRAC; IBA:GO_Central.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0031507; P:heterochromatin assembly; IBA:GO_Central.
DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
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 Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Activator; Coiled coil; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..275
FT /note="DNA polymerase II subunit B4"
FT /id="PRO_0000455273"
FT DNA_BIND 11..17
FT /evidence="ECO:0000250|UniProtKB:P13434"
FT REGION 112..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 152..179
FT /evidence="ECO:0000255"
FT MOTIF 135..142
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 129..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..234
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..275
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 275 AA; 30550 MW; A3D27BA54D965E82 CRC64;
MESEKVVVDE LPLAIVRRVV KKKLSECSPD YDVSIHKEAL LAFSESARIF IHYLSATAND
FCKDARRQTM KADDVFKALE EMDFSEFLEP LKSSLEDFKK KNAGKKAGAA AASYPAGGAA
LKSSSGTASK PKETKKRKQE EPSTQKGARK SKIDEETKRN DEETENDNTE EENGNDEEDE
NGNDEEDEND DENTEENGND EENDDENTEE NGNDEENEKE DEENSMEENG NESEESGNED
HSMEENGSGV GEDNENEDGS VSGSGEEVES DEEDE
