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ISWI chromatin-remodeling complex ATPase CHR17 (EC 3.6.4.-) (Protein CHROMATIN REMODELING 17)

 CHR17_ARATH             Reviewed;        1069 AA.
F4JY24; Q94C61;
09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 1.
23-MAY-2018, entry version 58.
RecName: Full=ISWI chromatin-remodeling complex ATPase CHR17 {ECO:0000305};
EC=3.6.4.- {ECO:0000305};
AltName: Full=Protein CHROMATIN REMODELING 17 {ECO:0000303|PubMed:22694359};
Name=CHR17 {ECO:0000303|PubMed:22694359};
OrderedLocusNames=At5g18620 {ECO:0000312|Araport:AT5G18620};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-748 AND 529-1069.
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
FUNCTION, INTERACTION WITH RLT1, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=22694359; DOI=10.1111/j.1365-313X.2012.05074.x;
Li G., Zhang J., Li J., Yang Z., Huang H., Xu L.;
"Imitation Switch chromatin remodeling factors and their interacting
RINGLET proteins act together in controlling the plant vegetative
phase in Arabidopsis.";
Plant J. 72:261-270(2012).
[5]
FUNCTION.
PubMed=24606212; DOI=10.1111/tpj.12499;
Li G., Liu S., Wang J., He J., Huang H., Zhang Y., Xu L.;
"ISWI proteins participate in the genome-wide nucleosome distribution
in Arabidopsis.";
Plant J. 78:706-714(2014).
[6]
INTERACTION WITH FGT1, FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=27680998; DOI=10.7554/eLife.17061;
Brzezinka K., Altmann S., Czesnick H., Nicolas P., Gorka M., Benke E.,
Kabelitz T., Jaehne F., Graf A., Kappel C., Baeurle I.;
"Arabidopsis FORGETTER1 mediates stress-induced chromatin memory
through nucleosome remodeling.";
Elife 5:0-0(2016).
-!- FUNCTION: Possesses intrinsic ATP-dependent nucleosome-remodeling
activity. Constitutes the catalytic subunit of several complexes
capable of forming ordered nucleosome arrays on chromatin (By
similarity). Involved in the formation of nucleosome distribution
patterns (PubMed:24606212). Required for the maintenance of the
plant vegetative phase. In association with RLT1 or RLT2 may
prevent the early activation of the vegetative-to-reproductive
transition by regulating key genes that contribute to flower
timing, such as FT, SEP1, SEP3, AGL8/FUL, SOC1 and FLC
(PubMed:22694359). Necessary to acquire heat stress (HS) memory
(PubMed:27680998). {ECO:0000250|UniProtKB:O60264,
ECO:0000269|PubMed:22694359, ECO:0000269|PubMed:24606212,
ECO:0000269|PubMed:27680998}.
-!- SUBUNIT: Interacts with RLT1 (PubMed:22694359). Binds to FGT1
(PubMed:27680998). {ECO:0000269|PubMed:22694359,
ECO:0000269|PubMed:27680998}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00624}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences. {ECO:0000305};
Name=1;
IsoId=F4JY24-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Highly expressed in growing tissues such as
inflorescence and flower meristems, young leaves and floral
organs. Expressed in roots, rosette and cauline leaves, stems,
flowers, inflorescences and siliques.
{ECO:0000269|PubMed:22694359}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
conditions, but the double mutant plants chr11-1 and chr17-1 are
very small and display early flowering and sterility
(PubMed:22694359). Premature decline of expression of HSA32,
HSP18.2, HSP21, HSP22 and HSP101 after HS in the double mutant
plants chr11-1 and chr17-1 (PubMed:27680998).
{ECO:0000269|PubMed:22694359, ECO:0000269|PubMed:27680998}.
-!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK59663.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC051627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CP002688; AED92587.1; -; Genomic_DNA.
EMBL; AY035159; AAK59663.1; ALT_INIT; mRNA.
RefSeq; NP_568365.2; NM_121867.4. [F4JY24-1]
UniGene; At.19176; -.
ProteinModelPortal; F4JY24; -.
SMR; F4JY24; -.
STRING; 3702.AT5G18620.2; -.
iPTMnet; F4JY24; -.
PaxDb; F4JY24; -.
EnsemblPlants; AT5G18620.1; AT5G18620.1; AT5G18620. [F4JY24-1]
GeneID; 831980; -.
Gramene; AT5G18620.1; AT5G18620.1; AT5G18620. [F4JY24-1]
KEGG; ath:AT5G18620; -.
Araport; AT5G18620; -.
eggNOG; KOG0385; Eukaryota.
eggNOG; COG0553; LUCA.
KO; K11654; -.
PRO; PR:F4JY24; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; F4JY24; baseline and differential.
GO; GO:0016589; C:NURF complex; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; IEA:InterPro.
GO; GO:0016584; P:nucleosome positioning; IMP:UniProtKB.
GO; GO:1900036; P:positive regulation of cellular response to heat; IMP:UniProtKB.
CDD; cd00079; HELICc; 1.
CDD; cd00167; SANT; 1.
Gene3D; 1.10.1040.30; -; 1.
Gene3D; 3.40.50.10810; -; 1.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR029915; ISWI.
InterPro; IPR015194; ISWI_HAND-dom.
InterPro; IPR036306; ISWI_HAND-dom_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR001005; SANT/Myb.
InterPro; IPR017884; SANT_dom.
InterPro; IPR015195; SLIDE.
InterPro; IPR038718; SNF2-like_sf.
InterPro; IPR000330; SNF2_N.
PANTHER; PTHR10799:SF887; PTHR10799:SF887; 1.
Pfam; PF09110; HAND; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF09111; SLIDE; 1.
Pfam; PF00176; SNF2_N; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SMART; SM00717; SANT; 2.
SUPFAM; SSF101224; SSF101224; 1.
SUPFAM; SSF46689; SSF46689; 2.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51293; SANT; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Chromatin regulator; Coiled coil;
Complete proteome; Hydrolase; Nucleotide-binding; Nucleus;
Reference proteome; Repeat.
CHAIN 1 1069 ISWI chromatin-remodeling complex ATPase
CHR17.
/FTId=PRO_0000435116.
DOMAIN 206 371 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 499 650 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 845 897 SANT 1. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
DOMAIN 946 1007 SANT 2. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
NP_BIND 219 226 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 322 325 DEAH box. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
COMPBIAS 8 85 Glu-rich. {ECO:0000255|PROSITE-
ProRule:PRU00007}.
SEQUENCE 1069 AA; 123888 MW; D55EC375434B9153 CRC64;
MARASKREVS SDEAYSSEEE EQVNDQANVE EDDDELEAVA RSAGSDEEDV APDEAPVSDD
EVVPVEDDAE EDEEDEEKAE ISKREKARLK EMQKMKKQKI QQILDSQNAS IDADMNNKGK
GRIKYLLQQT ELFAHFAKSD PSPSQKKGKG RGRHSSKLTE EEEDEECLKE EEGGIVGSGG
TRLLTQPACI QGKLRDYQLA GLNWLIRLYE NGINGILADE MGLGKTLQTI SLLAYLHEYR
GINGPHMVVA PKSTLGNWMN EIRRFCPVLR AVKFLGNPEE RRHIREELLV AGKFDICVTS
FEMAIKEKTT LRRFSWRYII IDEAHRIKNE NSLLSKTMRL FSTNYRLLIT GTPLQNNLHE
LWALLNFLLP EVFSSAETFD EWFQISGEND QQEVVQQLHK VLRPFLLRRL KSDVEKGLPP
KKETILKVGM SQMQKQYYKA LLQKDLEVVN GGGERKRLLN IAMQLRKCCN HPYLFQGAEP
GPPYTTGDHL VTNAGKMVLL DKLLPKLKDR DSRVLIFSQM TRLLDILEDY LMYRGYQYCR
IDGNTGGDER DASIEAYNKP GSEKFVFLLS TRAGGLGINL ATADVVILYD SDWNPQVDLQ
AQDRAHRIGQ KKEVQVFRFC TENAIEAKVI ERAYKKLALD ALVIQQGRLA EQKTVNKDEL
LQMVRYGAEM VFSSKDSTIT DEDIDRIIAK GEEATAELDA KMKKFTEDAI QFKMDDSADF
YDFDDDNKDE SKVDFKKIVS ENWNDPPKRE RKRNYSEVEY FKQTLRQGAP AKPKEPRIPR
MPQLHDFQFF NIQRLTELYE KEVRYLMQAH QKTQMKDTIE VDEPEEVGDP LTAEEVEEKE
LLLEEGFSTW SRRDFNAFIR ACEKYGRNDI KSIASEMEGK TEEEVERYAQ VFQVRYKELN
DYDRIIKNIE RGEARISRKD EIMKAIGKKL DRYRNPWLEL KIQYGQNKGK LYNEECDRFM
ICMVHKLGYG NWDELKAAFR TSPLFRFDWF VKSRTTQELA RRCDTLIRLI EKENQEFDER
ERQARKEKKL SKSATPSKRP SGRQANESPS SLLKKRKQLS MDDYGKRRK


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