CHR17_ARATH
ID CHR17_ARATH Reviewed; 1069 AA.
AC F4JY24; Q94C61;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=ISWI chromatin-remodeling complex ATPase CHR17 {ECO:0000305};
DE EC=3.6.4.- {ECO:0000305};
DE AltName: Full=Protein CHROMATIN REMODELING 17 {ECO:0000303|PubMed:22694359};
GN Name=CHR17 {ECO:0000303|PubMed:22694359};
GN OrderedLocusNames=At5g18620 {ECO:0000312|Araport:AT5G18620};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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] OF 1-748 AND 529-1069.
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, INTERACTION WITH RLT1, TISSUE SPECIFICITY, AND DISRUPTION
RP 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 [5]
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 [6]
RP INTERACTION WITH FGT1, FUNCTION, AND DISRUPTION PHENOTYPE.
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). Required for the maintenance of the plant
CC vegetative phase. In association with RLT1 or RLT2 may prevent the
CC early activation of the vegetative-to-reproductive transition by
CC regulating key genes that contribute to flower timing, such as FT,
CC SEP1, SEP3, AGL8/FUL, SOC1 and FLC (PubMed:22694359). Necessary to
CC acquire heat stress (HS) memory (PubMed:27680998).
CC {ECO:0000250|UniProtKB:O60264, ECO:0000269|PubMed:22694359,
CC ECO:0000269|PubMed:24606212, ECO:0000269|PubMed:27680998}.
CC -!- SUBUNIT: Interacts with RLT1 (PubMed:22694359). Binds to FGT1
CC (PubMed:27680998). {ECO:0000269|PubMed:22694359,
CC ECO:0000269|PubMed:27680998}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}.
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=F4JY24-1; Sequence=Displayed;
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 -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutant plants chr11-1 and chr17-1 are very
CC small and display early flowering and sterility (PubMed:22694359).
CC Premature decline of expression of HSA32, HSP18.2, HSP21, HSP22 and
CC HSP101 after HS in the double mutant plants chr11-1 and chr17-1
CC (PubMed:27680998). {ECO:0000269|PubMed:22694359,
CC ECO:0000269|PubMed:27680998}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK59663.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AC051627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92587.1; -; Genomic_DNA.
DR EMBL; AY035159; AAK59663.1; ALT_INIT; mRNA.
DR RefSeq; NP_568365.2; NM_121867.4. [F4JY24-1]
DR AlphaFoldDB; F4JY24; -.
DR SMR; F4JY24; -.
DR STRING; 3702.AT5G18620.2; -.
DR iPTMnet; F4JY24; -.
DR PaxDb; F4JY24; -.
DR PRIDE; F4JY24; -.
DR ProteomicsDB; 246960; -. [F4JY24-1]
DR EnsemblPlants; AT5G18620.1; AT5G18620.1; AT5G18620. [F4JY24-1]
DR GeneID; 831980; -.
DR Gramene; AT5G18620.1; AT5G18620.1; AT5G18620. [F4JY24-1]
DR KEGG; ath:AT5G18620; -.
DR Araport; AT5G18620; -.
DR eggNOG; KOG0385; Eukaryota.
DR HOGENOM; CLU_000315_0_0_1; -.
DR OMA; REINRWT; -.
DR PRO; PR:F4JY24; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4JY24; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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: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:1900036; P:positive regulation of cellular response to heat; 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 Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..1069
FT /note="ISWI chromatin-remodeling complex ATPase CHR17"
FT /id="PRO_0000435116"
FT DOMAIN 206..371
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 499..650
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 845..897
FT /note="SANT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 946..1007
FT /note="SANT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 322..325
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 14..37
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..78
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1034
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 219..226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ 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
