CHR19_ARATH
ID CHR19_ARATH Reviewed; 763 AA.
AC Q9ZUL5;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Protein CHROMATIN REMODELING 19 {ECO:0000303|PubMed:16547115};
DE Short=AtCHR19;
DE EC=3.6.4.-;
DE AltName: Full=AtRAD54-like protein {ECO:0000303|PubMed:15053760};
GN Name=ETL1 {ECO:0000312|EMBL:AEC05545.1};
GN Synonyms=CHR19 {ECO:0000303|PubMed:16547115};
GN OrderedLocusNames=At2g02090 {ECO:0000312|Araport:AT2G02090};
GN ORFNames=F5O4.14 {ECO:0000312|EMBL:AAL24339.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
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 INDUCTION BY UV-C.
RC STRAIN=cv. C24;
RX PubMed=15053760; DOI=10.1111/j.1365-313x.2004.02020.x;
RA Filkowski J., Kovalchuk O., Kovalchuk I.;
RT "Genome stability of vtc1, tt4, and tt5 Arabidopsis thaliana mutants
RT impaired in protection against oxidative stress.";
RL Plant J. 38:60-69(2004).
RN [5]
RP INDUCTION BY ROSE BENGAL AND METHYL METHANE SULFONATE.
RX PubMed=15133154; DOI=10.1104/pp.104.040477;
RA Kovalchuk I., Abramov V., Pogribny I., Kovalchuk O.;
RT "Molecular aspects of plant adaptation to life in the Chernobyl zone.";
RL Plant Physiol. 135:357-363(2004).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16547115; DOI=10.1534/genetics.105.051664;
RA Shaked H., Avivi-Ragolsky N., Levy A.A.;
RT "Involvement of the Arabidopsis SWI2/SNF2 chromatin remodeling gene family
RT in DNA damage response and recombination.";
RL Genetics 173:985-994(2006).
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 IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBUNIT, INTERACTION WITH
RP SUVR2, AND SUBCELLULAR LOCATION.
RX PubMed=25420628; DOI=10.1038/cr.2014.156;
RA Han Y.F., Dou K., Ma Z.Y., Zhang S.W., Huang H.W., Li L., Cai T., Chen S.,
RA Zhu J.K., He X.J.;
RT "SUVR2 is involved in transcriptional gene silencing by associating with
RT SNF2-related chromatin-remodeling proteins in Arabidopsis.";
RL Cell Res. 24:1445-1465(2014).
CC -!- FUNCTION: DNA helicase that possesses intrinsic ATP-dependent
CC nucleosome-remodeling activity and is both required for DNA repair and
CC heterochromatin organization. Promotes DNA end resection of double-
CC strand breaks (DSBs) following DNA damage: probably acts by weakening
CC histone DNA interactions in nucleosomes flanking DSBs (By similarity).
CC Probable chromatin remodeling factor. Probable helicase-like
CC transcription factor involved in transcriptional gene silencing.
CC Associates with SUVR2 and contributes to transcriptional gene silencing
CC at RNA-directed DNA methylation (RdDM) target loci but also at RdDM-
CC independent target loci. May be involved in nucleosome positioning to
CC form ordered nucleosome arrays on chromatin (PubMed:25420628).
CC {ECO:0000250|UniProtKB:P31380, ECO:0000269|PubMed:25420628,
CC ECO:0000303|PubMed:16547115}.
CC -!- SUBUNIT: Interacts with SUVR2 and itself.
CC {ECO:0000269|PubMed:25420628}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:25420628}.
CC -!- INDUCTION: By UV-C illumination (PubMed:15053760). Accumulates in
CC response to the mutagens rose Bengal (RB) and methyl methane sulfonate
CC (MMS) (PubMed:15133154). {ECO:0000269|PubMed:15053760,
CC ECO:0000269|PubMed:15133154}.
CC -!- MISCELLANEOUS: Induction by the mutagens rose Bengal (RB) and methyl
CC methane sulfonate (MMS) is enhanced in progeny of Chernobyl plants
CC exposed to ionizing radiation thus leading to a higher resistance to
CC DNA damages. {ECO:0000269|PubMed:15133154}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AC005936; AAC97224.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05545.1; -; Genomic_DNA.
DR EMBL; AY059857; AAL24339.1; -; mRNA.
DR EMBL; BT002576; AAO00936.1; -; mRNA.
DR PIR; H84432; H84432.
DR RefSeq; NP_178318.1; NM_126270.2.
DR AlphaFoldDB; Q9ZUL5; -.
DR SMR; Q9ZUL5; -.
DR BioGRID; 143; 10.
DR IntAct; Q9ZUL5; 3.
DR STRING; 3702.AT2G02090.1; -.
DR iPTMnet; Q9ZUL5; -.
DR PaxDb; Q9ZUL5; -.
DR PRIDE; Q9ZUL5; -.
DR ProteomicsDB; 246784; -.
DR EnsemblPlants; AT2G02090.1; AT2G02090.1; AT2G02090.
DR GeneID; 814740; -.
DR Gramene; AT2G02090.1; AT2G02090.1; AT2G02090.
DR KEGG; ath:AT2G02090; -.
DR Araport; AT2G02090; -.
DR TAIR; locus:2051678; AT2G02090.
DR eggNOG; KOG0389; Eukaryota.
DR HOGENOM; CLU_000315_16_6_1; -.
DR InParanoid; Q9ZUL5; -.
DR OMA; STRNCES; -.
DR OrthoDB; 61251at2759; -.
DR PhylomeDB; Q9ZUL5; -.
DR PRO; PR:Q9ZUL5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUL5; baseline and differential.
DR Genevisible; Q9ZUL5; AT.
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:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; 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:0006974; P:cellular response to DNA damage stimulus; IEP:UniProtKB.
DR GO; GO:0071494; P:cellular response to UV-C; IEP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; Coiled coil; DNA damage; DNA repair;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; RNA-mediated gene silencing; Transcription;
KW Transcription regulation.
FT CHAIN 1..763
FT /note="Protein CHROMATIN REMODELING 19"
FT /id="PRO_0000430856"
FT DOMAIN 226..404
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 592..742
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 462..482
FT /evidence="ECO:0000255"
FT MOTIF 353..356
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 520..527
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 116..131
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 239..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 763 AA; 86277 MW; 695ABE5DF361F528 CRC64;
MKRDFDEISE EEWSQHSFNA SRVLKRPRTP KKTRAATNPT PSIESFAFRR PSTAMTIESN
SSDGDCVEIE DLGDSDSDVK IVNGEDLLLE DEEEVEETKV VMRAARVGRR FVIEDEEASD
DDDDEAESSA SEDEFGGGGG GSGGRRGEDE DVVGKALQKC AKISADLRKE LYGTSSGVTD
RYSEVETSTV RIVTQNDIDD ACKAEDSDFQ PILKPYQLVG VNFLLLLYKK GIEGAILADE
MGLGKTIQAI TYLTLLSRLN NDPGPHLVVC PASVLENWER ELRKWCPSFT VLQYHGAARA
AYSRELNSLS KAGKPPPFNV LLVCYSLFER HSEQQKDDRK VLKRWRWSCV LMDEAHALKD
KNSYRWKNLM SVARNANQRL MLTGTPLQND LHELWSLLEF MLPDIFTTEN VDLKKLLNAE
DTELITRMKS ILGPFILRRL KSDVMQQLVP KIQRVEYVLM ERKQEDAYKE AIEEYRAASQ
ARLVKLSSKS LNSLAKALPK RQISNYFTQF RKIANHPLLI RRIYSDEDVI RIARKLHPIG
AFGFECSLDR VIEEVKGFND FRIHQLLFQY GVNDTKGTLS DKHVMLSAKC RTLAELLPSM
KKSGHRVLIF SQWTSMLDIL EWTLDVIGVT YRRLDGSTQV TDRQTIVDTF NNDKSIFACL
LSTRAGGQGL NLTGADTVII HDMDFNPQID RQAEDRCHRI GQTKPVTIFR LVTKSTVDEN
IYEIAKRKLV LDAAVLESGV HVDDNGDTPE KTMGEILASL LMG
