ISW2_ARATH
ID ISW2_ARATH Reviewed; 1056 AA.
AC Q8RWY3; F4JAW0; F4JAW1; Q9SQU3;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 4.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=ISWI chromatin-remodeling complex ATPase CHR11 {ECO:0000305};
DE EC=3.6.4.- {ECO:0000305};
DE AltName: Full=ISW2-like {ECO:0000305};
DE AltName: Full=Protein CHROMATIN REMODELING 11 {ECO:0000303|PubMed:16286646};
DE AltName: Full=Sucrose nonfermenting protein 2 homolog {ECO:0000305};
GN Name=CHR11 {ECO:0000303|PubMed:16286646};
GN OrderedLocusNames=At3g06400 {ECO:0000312|Araport:AT3G06400};
GN ORFNames=F24P17.13 {ECO:0000312|EMBL:AAF08585.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 [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 [4]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=16286646; DOI=10.1073/pnas.0508186102;
RA Huanca-Mamani W., Garcia-Aguilar M., Leon-Martinez G., Grossniklaus U.,
RA Vielle-Calzada J.P.;
RT "CHR11, a chromatin-remodeling factor essential for nuclear proliferation
RT during female gametogenesis in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17231-17236(2005).
RN [5]
RP FUNCTION, INTERACTION WITH RLT1 AND RLT2, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22694359; DOI=10.1111/j.1365-313x.2012.05074.x;
RA Li G., Zhang J., Li J., Yang Z., Huang H., Xu L.;
RT "Imitation Switch chromatin remodeling factors and their interacting
RT RINGLET proteins act together in controlling the plant vegetative phase in
RT Arabidopsis.";
RL Plant J. 72:261-270(2012).
RN [6]
RP INTERACTION WITH RLT1; RLT2; PTM AND DDR4.
RX PubMed=23691993; DOI=10.1111/jipb.12069;
RA Dong J., Gao Z., Liu S., Li G., Yang Z., Huang H., Xu L.;
RT "SLIDE, the protein interacting domain of Imitation Switch remodelers,
RT binds DDT-domain proteins of different subfamilies in chromatin remodeling
RT complexes.";
RL J. Integr. Plant Biol. 55:928-937(2013).
RN [7]
RP GENE FAMILY.
RX PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA Xu R., Zhang S., Huang J., Zheng C.;
RT "Genome-wide comparative in silico analysis of the RNA helicase gene family
RT in Zea mays and Glycine max: a comparison with Arabidopsis and Oryza
RT sativa.";
RL PLoS ONE 8:E78982-E78982(2013).
RN [8]
RP FUNCTION.
RX PubMed=24606212; DOI=10.1111/tpj.12499;
RA Li G., Liu S., Wang J., He J., Huang H., Zhang Y., Xu L.;
RT "ISWI proteins participate in the genome-wide nucleosome distribution in
RT Arabidopsis.";
RL Plant J. 78:706-714(2014).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH FGT1.
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: Possesses intrinsic ATP-dependent nucleosome-remodeling
CC activity. Constitutes the catalytic subunit of several complexes
CC capable of forming ordered nucleosome arrays on chromatin (By
CC similarity). Involved in the formation of nucleosome distribution
CC patterns (PubMed:24606212). Involved in nuclear proliferation during
CC megagametogenesis and cell expansion in the sporophyte
CC (PubMed:16286646). Required for the maintenance of the plant vegetative
CC phase. In association with RLT1 or RLT2 may prevent the early
CC activation of the vegetative-to-reproductive transition by regulating
CC key genes that contribute to flower timing, such as FT, SEP1, SEP3,
CC AGL8/FUL, SOC1 and FLC (PubMed:22694359). Necessary to acquire heat
CC stress (HS) memory (PubMed:27680998). {ECO:0000250|UniProtKB:O60264,
CC ECO:0000269|PubMed:16286646, ECO:0000269|PubMed:22694359,
CC ECO:0000269|PubMed:24606212, ECO:0000269|PubMed:27680998}.
CC -!- SUBUNIT: Interacts with RLT1 and RLT2 (PubMed:22694359). Interacts (via
CC C-terminus) with RLT1 (via the DDT domain), RLT2 (via the DDT domain),
CC PTM (via the DDT domain) and DDR4 (via the DDT domain)
CC (PubMed:23691993). Binds to FGT1 (PubMed:27680998).
CC {ECO:0000269|PubMed:22694359, ECO:0000269|PubMed:23691993,
CC ECO:0000269|PubMed:27680998}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624,
CC ECO:0000269|PubMed:22694359}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8RWY3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8RWY3-2; Sequence=VSP_058012;
CC -!- TISSUE SPECIFICITY: Highly expressed in growing tissues such as
CC inflorescence and flower meristems, young leaves and floral organs.
CC Expressed in roots, rosette and cauline leaves, stems, flowers,
CC inflorescences and siliques. {ECO:0000269|PubMed:22694359}.
CC -!- DEVELOPMENTAL STAGE: In developing ovule, expressed in all cells of the
CC young nucellus, including the functional megaspore. After the
CC initiation of megagametogenesis, expressed in most cells of the ovule,
CC including the integuments, the developing megagametophyte, and the
CC funiculus. In mature ovules, strongly expressed in the cellularized
CC megagametophyte. After double fertilization, expressed in the
CC developing embryo and the free nuclear endosperm until seed maturity.
CC Expressed in developing male gametophytes and mature pollen grains.
CC {ECO:0000269|PubMed:16286646}.
CC -!- DISRUPTION PHENOTYPE: Reduced heat stress (HS) memory. Premature
CC decline of expression of HSA32, HSP18.2, HSP21, HSP22 and HSP101 after
CC HS in the double mutant plants chr11-1 and chr17-1 (PubMed:27680998).
CC No visible phenotype under normal growth conditions, but the double
CC mutant plants chr11-1 and chr17-1 are very small and display early
CC flowering and sterility (PubMed:22694359).
CC {ECO:0000269|PubMed:22694359, ECO:0000269|PubMed:27680998}.
CC -!- MISCELLANEOUS: Plants silencing CHR11 display reduced plant height and
CC small cotyledonary embryos with limited cell expansion. Plants
CC silencing CHR11 specifically at the onset of female gametogenesis
CC (megagametogenesis) have defective female gametophytes arrested before
CC the completion of the mitotic haploid nuclear divisions.
CC {ECO:0000269|PubMed:16286646}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF08585.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC011623; AAF08585.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74386.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74388.1; -; Genomic_DNA.
DR EMBL; AY091030; AAM13851.1; -; mRNA.
DR RefSeq; NP_001189827.1; NM_001202898.2. [Q8RWY3-1]
DR RefSeq; NP_187291.2; NM_111515.5. [Q8RWY3-2]
DR AlphaFoldDB; Q8RWY3; -.
DR SMR; Q8RWY3; -.
DR BioGRID; 5149; 34.
DR STRING; 3702.AT3G06400.3; -.
DR iPTMnet; Q8RWY3; -.
DR PaxDb; Q8RWY3; -.
DR PRIDE; Q8RWY3; -.
DR ProteomicsDB; 238955; -. [Q8RWY3-1]
DR EnsemblPlants; AT3G06400.1; AT3G06400.1; AT3G06400. [Q8RWY3-2]
DR EnsemblPlants; AT3G06400.2; AT3G06400.2; AT3G06400. [Q8RWY3-1]
DR GeneID; 819814; -.
DR Gramene; AT3G06400.1; AT3G06400.1; AT3G06400. [Q8RWY3-2]
DR Gramene; AT3G06400.2; AT3G06400.2; AT3G06400. [Q8RWY3-1]
DR KEGG; ath:AT3G06400; -.
DR Araport; AT3G06400; -.
DR eggNOG; KOG0385; Eukaryota.
DR HOGENOM; CLU_000315_0_0_1; -.
DR InParanoid; Q8RWY3; -.
DR PRO; PR:Q8RWY3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8RWY3; baseline and differential.
DR Genevisible; Q8RWY3; AT.
DR GO; GO:0005634; C:nucleus; IMP:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0140750; F:nucleosome array spacer activity; IMP:GO_Central.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0009561; P:megagametogenesis; IMP:UniProtKB.
DR GO; GO:1900036; P:positive regulation of cellular response to heat; IMP:UniProtKB.
DR GO; GO:0048510; P:regulation of timing of transition from vegetative to reproductive phase; IMP:UniProtKB.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR Gene3D; 1.10.1040.30; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; SSF101224; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chromatin regulator; Coiled coil;
KW Flowering; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..1056
FT /note="ISWI chromatin-remodeling complex ATPase CHR11"
FT /id="PRO_0000074331"
FT DOMAIN 201..366
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 494..645
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 840..892
FT /note="SANT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 941..1002
FT /note="SANT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 12..105
FT /evidence="ECO:0000255"
FT MOTIF 317..320
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 11..32
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..71
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 214..221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VAR_SEQ 820
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_058012"
FT CONFLICT 168
FT /note="D -> E (in Ref. 3; AAM13851)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1056 AA; 122558 MW; 28770AB52EBE9936 CRC64;
MARNSNSDEA FSSEEEEERV KDNEEEDEEE LEAVARSSGS DDDEVAAADE SPVSDGEAAP
VEDDYEDEED EEKAEISKRE KARLKEMQKL KKQKIQEMLE SQNASIDADM NNKGKGRLKY
LLQQTELFAH FAKSDGSSSQ KKAKGRGRHA SKITEEEEDE EYLKEEEDGL TGSGNTRLLT
QPSCIQGKMR DYQLAGLNWL IRLYENGING ILADEMGLGK TLQTISLLAY LHEYRGINGP
HMVVAPKSTL GNWMNEIRRF CPVLRAVKFL GNPEERRHIR EDLLVAGKFD ICVTSFEMAI
KEKTALRRFS WRYIIIDEAH RIKNENSLLS KTMRLFSTNY RLLITGTPLQ NNLHELWALL
NFLLPEIFSS AETFDEWFQI SGENDQQEVV QQLHKVLRPF LLRRLKSDVE KGLPPKKETI
LKVGMSQMQK QYYKALLQKD LEAVNAGGER KRLLNIAMQL RKCCNHPYLF QGAEPGPPYT
TGDHLITNAG KMVLLDKLLP KLKERDSRVL IFSQMTRLLD ILEDYLMYRG YLYCRIDGNT
GGDERDASIE AYNKPGSEKF VFLLSTRAGG LGINLATADV VILYDSDWNP QVDLQAQDRA
HRIGQKKEVQ VFRFCTESAI EEKVIERAYK KLALDALVIQ QGRLAEQKTV NKDELLQMVR
YGAEMVFSSK DSTITDEDID RIIAKGEEAT AELDAKMKKF TEDAIQFKMD DSADFYDFDD
DNKDENKLDF KKIVSDNWND PPKRERKRNY SESEYFKQTL RQGAPAKPKE PRIPRMPQLH
DFQFFNIQRL TELYEKEVRY LMQTHQKNQL KDTIDVEEPE EGGDPLTTEE VEEKEGLLEE
GFSTWSRRDF NTFLRACEKY GRNDIKSIAS EMEGKTEEEV ERYAKVFKER YKELNDYDRI
IKNIERGEAR ISRKDEIMKA IGKKLDRYRN PWLELKIQYG QNKGKLYNEE CDRFMICMIH
KLGYGNWDEL KAAFRTSSVF RFDWFVKSRT SQELARRCDT LIRLIEKENQ EFDERERQAR
KEKKLAKSAT PSKRPLGRQA SESPSSTKKR KHLSMR
