FGT1_ARATH
ID FGT1_ARATH Reviewed; 1295 AA.
AC F4IF36; O64516;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Protein FORGETTER 1 {ECO:0000303|PubMed:27680998};
DE AltName: Full=Protein EMBRYO DEFECTIVE 1135 {ECO:0000303|PubMed:15266054};
GN Name=FGT1 {ECO:0000303|PubMed:27680998};
GN Synonyms=EMB1135 {ECO:0000303|PubMed:15266054};
GN OrderedLocusNames=At1g79350 {ECO:0000312|Araport:AT1G79350};
GN ORFNames=YUP8H12R.3 {ECO:0000312|EMBL:AAC17076.1};
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=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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=15266054; DOI=10.1104/pp.104.045179;
RA Tzafrir I., Pena-Muralla R., Dickerman A., Berg M., Rogers R., Hutchens S.,
RA Sweeney T.C., McElver J., Aux G., Patton D., Meinke D.;
RT "Identification of genes required for embryo development in Arabidopsis.";
RL Plant Physiol. 135:1206-1220(2004).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18684657; DOI=10.1016/j.tplants.2008.06.003;
RA Meinke D., Muralla R., Sweeney C., Dickerman A.;
RT "Identifying essential genes in Arabidopsis thaliana.";
RL Trends Plant Sci. 13:483-491(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH BRM; CHR11 AND CHR17,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=27680998; DOI=10.7554/elife.17061;
RA Brzezinka K., Altmann S., Czesnick H., Nicolas P., Gorka M., Benke E.,
RA Kabelitz T., Jaehne F., Graf A., Kappel C., Baeurle I.;
RT "Arabidopsis FORGETTER1 mediates stress-induced chromatin memory through
RT nucleosome remodeling.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Required for normal embryo development (PubMed:15266054,
CC PubMed:18684657). Necessary to acquire heat stress (HS) memory, by
CC modulating nucleosome occupancy and regulating heat-induced gene
CC expression. Associates globally with the nucleosome-poor regions
CC flanking the transcription units of expressed genes. Binds to the
CC promoter regions, primarily to the proximal promoter just upstream of
CC the transcriptional start sites (TSS) and somewhat more weakly to the
CC region downstream of the transcription termination site (TTS), of
CC actively expressed genes (e.g. HSA32, HSP18.2 and HSP22.0) in a heat-
CC dependent fashion (PubMed:27680998). {ECO:0000269|PubMed:15266054,
CC ECO:0000269|PubMed:18684657, ECO:0000269|PubMed:27680998}.
CC -!- SUBUNIT: Interacts with SWI/SNF and ISWI chromatin remodelers such as
CC BRM, CHR11 and CHR17. Binds to histone H3.
CC {ECO:0000269|PubMed:27680998}.
CC -!- INTERACTION:
CC F4IF36; Q9FME3: TCP5; NbExp=4; IntAct=EBI-15205608, EBI-15192251;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:27680998}.
CC -!- DISRUPTION PHENOTYPE: Abnormal embryo development leading to reduced
CC cotyledons (PubMed:15266054, PubMed:18684657). Reduced maintenance of
CC heat-induced (37 degrees Celsius) gene expression leading to reduced
CC growth and survival in heat conditions (44 degrees Celsius). Abnormal
CC nucleosome dynamics at loci with altered maintenance of heat-induced
CC expression. The double mutant brm-1 fgt1-1 exhibits retarted seedling
CC development resulting in reduced development and delayed leaf
CC initiation, as well as delayed flowering time (PubMed:27680998).
CC {ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:18684657,
CC ECO:0000269|PubMed:27680998}.
CC -!- SIMILARITY: Belongs to the SBNO family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17076.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC002986; AAC17076.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36233.1; -; Genomic_DNA.
DR PIR; T01020; T01020.
DR RefSeq; NP_178053.4; NM_106583.6.
DR AlphaFoldDB; F4IF36; -.
DR IntAct; F4IF36; 7.
DR STRING; 3702.AT1G79350.1; -.
DR iPTMnet; F4IF36; -.
DR PaxDb; F4IF36; -.
DR PRIDE; F4IF36; -.
DR ProteomicsDB; 230090; -.
DR EnsemblPlants; AT1G79350.1; AT1G79350.1; AT1G79350.
DR GeneID; 844273; -.
DR Gramene; AT1G79350.1; AT1G79350.1; AT1G79350.
DR KEGG; ath:AT1G79350; -.
DR Araport; AT1G79350; -.
DR TAIR; locus:2207365; AT1G79350.
DR eggNOG; KOG1513; Eukaryota.
DR HOGENOM; CLU_000212_2_1_1; -.
DR InParanoid; F4IF36; -.
DR OMA; ARHSHKR; -.
DR OrthoDB; 141580at2759; -.
DR PRO; PR:F4IF36; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4IF36; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:TAIR.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IMP:GO_Central.
DR GO; GO:0010286; P:heat acclimation; IMP:TAIR.
DR GO; GO:1900036; P:positive regulation of cellular response to heat; IMP:UniProtKB.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR026937; SBNO_Helicase_C_dom.
DR InterPro; IPR026741; SNO.
DR InterPro; IPR039187; SNO_AAA.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12706; PTHR12706; 1.
DR Pfam; PF13872; AAA_34; 1.
DR Pfam; PF13871; Helicase_C_4; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Metal-binding; Nucleus; Reference proteome;
KW Stress response; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1295
FT /note="Protein FORGETTER 1"
FT /id="PRO_0000438548"
FT ZN_FING 691..741
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 643..650
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..106
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..179
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..688
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1295 AA; 143617 MW; F779A2AE8BDC754D CRC64;
MTQSPVQPPP PLPAQPHSAA GGVIRGDVQV RCAGCRVILR VKTGVVEFSC PTCQLPQMLP
PELLSRARPQ FPQSPQQPPQ PIQTLPPPIQ QQLKPLNLPR PPVPAHGIDP TKMQLPCANC
QAILNVPHGL TRFSCPQCHV ELAVDVSKLN RSLTASQSHS NPPTPAAPTV PPPPPPEEVN
EEAIEVEREE DEGGTAGETF MDYRPPKLSI GPPHPDPIVE TSSLSAVQPP EPTYDLKIKE
ELERSKALSC LQIETLVYAC QRHLQHLADG TRAGFFVGDG AGVGKGRTIA GLIWENWKHG
RRKALWISIG SDLKYDARRD LDDVGATCVG VNPLNKLPYS KLDSKNVGIK EGVVFLTYNS
LIASSEKGRS RLQQLVQWCG PEFDGLLIFD ECHKAKNLVP EAGSQPTRIG QAVVDIQDKI
PQARVIYCSA TGASEPRNMG YMVRLGLWGA GTSFSDFNKF LGALDKGGTG ALELVAMDMK
ARGMYVCRTL SYKGAEFEIV EARLEAGMEA MYNKSAEFWA ELRIELLSAS AFLPNEKPNS
SQLWRLYWSS HQRFFRHLCM SAKVPVTVRL AKKALSTNKC VVIGLQSTGE ARTEEAVNKY
GLELDDFVSG PRELLLKFVE ENYPLPEQPE PLSEDDSVKE LQRKRHSASP GVSIRGRVRK
MAKWKPDSDN ESDLESEADS ADDSNDSDDE FQICQICSGE DERKKLLHCS ECDKLFHPDC
VVPPVIDLPS EAWICFSCKE KTEEYIQARR LYIAELQKRY EAALERKSKI IEIIRSLNLP
NNPLDDIVDQ LGGPEKVAEM TGRRGMLVRA SNGKGVTYQA RNTKDITMEM VNMHEKQLFM
DGKKLVAIIS EAGSAGVSLQ ADRRAVNQKR RVHLTLELPW SADRAIQQFG RTHRSNQTSA
PEYRLLFTNL GGERRFASIV AKRLETLGAL TQGDRRAGPS GPSLSAYNYD SNFGKKSLMV
MYRGIMEQEK LPVLPPGCSI DEPETVKEFL TKARAALVAV GIVRDSVLAN GKDVGRFSGR
IIDSDMHDVG RFLNRLLGLP PDIQNRLFEL FTSILDVLVH NARIEGSFDS GIVDMKANSV
ELLSTPKTVH VDQMSGASTM LFTFTLDRGV TWESASSMLE GKRRDGLGSA NDGFFESKRE
WLGRRHFILA FESAASGLFK IVRPAVGESI REMSLSELKT KYRKLSSLEK ARTGWEDEYE
VSSKQCMHGP KCKLGEYCTV GRRIQEVNVV GGLILPIWGT IEKALSKQAR HSHKRIRVIR
IETTTDNQRI VGLSIPNAAV ETVLQDLAWV QEIDD
