IWS1_ARATH
ID IWS1_ARATH Reviewed; 502 AA.
AC F4ICK8; Q9FVQ8;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Protein IWS1 homolog 1 {ECO:0000305};
DE Short=AtIWS1 {ECO:0000303|PubMed:20139304};
DE AltName: Full=Interacts with SPT6 protein 1 {ECO:0000305};
DE AltName: Full=Protein HIGH NITROGEN INSENSITIVE 9;
DE AltName: Full=Protein SUPPRESSOR OF BES-1-D 1 {ECO:0000305};
GN Name=IWS1 {ECO:0000303|PubMed:20139304};
GN Synonyms=HIN9, SEB1 {ECO:0000303|PubMed:20139304};
GN OrderedLocusNames=At1g32130 {ECO:0000312|Araport:AT1G32130,
GN ECO:0000312|EMBL:AEE31438.1};
GN ORFNames=F3C3.8 {ECO:0000312|EMBL:AAG23443.1};
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [4]
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 [5]
RP FUNCTION, INTERACTION WITH BZR2/BES1 AND SPT6, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. En-2;
RX PubMed=20139304; DOI=10.1073/pnas.0909198107;
RA Li L., Ye H., Guo H., Yin Y.;
RT "Arabidopsis IWS1 interacts with transcription factor BES1 and is involved
RT in plant steroid hormone brassinosteroid regulated gene expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:3918-3923(2010).
RN [6]
RP FUNCTION.
RX PubMed=21788519; DOI=10.1073/pnas.1017863108;
RA Widiez T., El Kafafi E.S., Girin T., Berr A., Ruffel S., Krouk G.,
RA Vayssieres A., Shen W.H., Coruzzi G.M., Gojon A., Lepetit M.;
RT "High nitrogen insensitive 9 (HNI9)-mediated systemic repression of root
RT NO3- uptake is associated with changes in histone methylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13329-13334(2011).
RN [7]
RP INTERACTION WITH ASHH2/SDG8, AND SUBCELLULAR LOCATION.
RX PubMed=24838002; DOI=10.1093/mp/ssu056;
RA Wang X., Chen J., Xie Z., Liu S., Nolan T., Ye H., Zhang M., Guo H.,
RA Schnable P.S., Li Z., Yin Y.;
RT "Histone lysine methyltransferase SDG8 is involved in brassinosteroid-
RT regulated gene expression in Arabidopsis thaliana.";
RL Mol. Plant 7:1303-1315(2014).
CC -!- FUNCTION: Transcription factor involved in RNA polymerase II (RNAPII)
CC transcription regulation. Involved in transcription elongation. May
CC function at post-recruitment and elongation steps of transcription. May
CC be recruited by BZR2/BES1 to target genes and promote their expression
CC during transcription elongation process. Required for brassinosteroid
CC (BR)-induced gene expression (PubMed:20139304). Required the for
CC regulation of numerous nitrogen-responsive genes in roots. Acts in
CC roots to repress NRT2.1 transcription in response to high nitrogen
CC supply. This repression is associated with an IWS1-dependent increase
CC of trimethylation on 'Lys-27' H3K27me3 at the NRT2.1 locus
CC (PubMed:21788519). {ECO:0000269|PubMed:20139304,
CC ECO:0000269|PubMed:21788519}.
CC -!- SUBUNIT: Interacts with BZR2/BES1 and SPT6 (via N-terminus)
CC (PubMed:20139304). Interacts with ASHH2/SDG8 (PubMed:24838002).
CC {ECO:0000269|PubMed:20139304, ECO:0000269|PubMed:24838002}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649,
CC ECO:0000269|PubMed:20139304, ECO:0000269|PubMed:24838002}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=F4ICK8-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Semi-dwarf phenotype. Stunted growth
CC characterized by reduced leaf petiole lengths and small leaves. Altered
CC responses to brassinosteroid (BR). {ECO:0000269|PubMed:20139304}.
CC -!- SIMILARITY: Belongs to the IWS1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG23443.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC084165; AAG23443.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31438.1; -; Genomic_DNA.
DR PIR; F86445; F86445.
DR RefSeq; NP_174492.2; NM_102946.4. [F4ICK8-1]
DR AlphaFoldDB; F4ICK8; -.
DR SMR; F4ICK8; -.
DR STRING; 3702.AT1G32130.1; -.
DR iPTMnet; F4ICK8; -.
DR PaxDb; F4ICK8; -.
DR PRIDE; F4ICK8; -.
DR ProteomicsDB; 238963; -. [F4ICK8-1]
DR EnsemblPlants; AT1G32130.1; AT1G32130.1; AT1G32130. [F4ICK8-1]
DR GeneID; 840105; -.
DR Gramene; AT1G32130.1; AT1G32130.1; AT1G32130. [F4ICK8-1]
DR KEGG; ath:AT1G32130; -.
DR Araport; AT1G32130; -.
DR TAIR; locus:2031715; AT1G32130.
DR eggNOG; KOG1793; Eukaryota.
DR HOGENOM; CLU_040584_2_1_1; -.
DR InParanoid; F4ICK8; -.
DR OMA; EDMRRYD; -.
DR PRO; PR:F4ICK8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4ICK8; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; TAS:TAIR.
DR Gene3D; 1.20.930.10; -; 1.
DR InterPro; IPR044204; IWS1/2.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR PANTHER; PTHR47350; PTHR47350; 1.
DR Pfam; PF08711; Med26; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Brassinosteroid signaling pathway; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..502
FT /note="Protein IWS1 homolog 1"
FT /id="PRO_0000437492"
FT DOMAIN 287..370
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 185
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19245862"
SQ SEQUENCE 502 AA; 57425 MW; 7B78E054F2C264BC CRC64;
MGFEDDPYRD VDGEPIVDFD DFGNDREPST EPLQDFDEDL ADDIGDWDGE GSQTPVYDND
KVAKPRKRLV KKSSSERVTI DVPELIDEDV DDAEFDEFMG GRGGGSTDYD DKVGRKRKKE
KERSSSGSGK EKRHKFPNRG ERKSEEIDEM WKSIAHNPEN DEEGVRTMDD DNFIDDTGLD
PSERYGGDAG DRSPTHYPQA EEGEDEDEVN NLFKMGKKKK KTERNPAEIA LLVENVMAEL
EVTAEEDAEL NRQGKPAINK LKKLSLLTDV LGKKQLQTEF LDHGVLTLLK NWLEPLPDGS
LPNINIRAAI LRVLTDFPID LDQYDRREQL KKSGLGKVIM FLSKSDEETN SNRRLAKDLV
DKWSRPIFNK STRFEDMRNL DEDRVPYRRP PVKKPSNKAT MESRDGDFDL EIRERKTGLT
SGQSSRGDRQ MTMRPEATPL DFLIRPQSKI DPDEIIARAK QVSQDQRRVK MNKKLQQLKG
TKKKRLQATK VSVEGRGMIK YL
