CHR20_ARATH
ID CHR20_ARATH Reviewed; 1479 AA.
AC F4HW51; F4HW52; O04048; Q9FRS5;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Protein CHROMATIN REMODELING 20 {ECO:0000303|PubMed:16547115};
DE Short=AtCHR20;
DE EC=3.6.4.-;
DE AltName: Full=ATP-dependent helicase ATRX {ECO:0000250|UniProtKB:Q61687};
DE AltName: Full=Transcriptional regulator ATRX {ECO:0000250|UniProtKB:Q61687};
DE AltName: Full=X-linked helicase II {ECO:0000250|UniProtKB:Q61687};
GN Name=ATRX {ECO:0000312|EMBL:AEE28313.1};
GN Synonyms=CHR20 {ECO:0000303|PubMed:16547115};
GN OrderedLocusNames=At1g08600 {ECO:0000312|Araport:AT1G08600};
GN ORFNames=F22O13.8 {ECO:0000312|EMBL:AAF99756.1};
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|EMBL:AEE28313.1};
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1246-1362.
RC STRAIN=cv. Columbia;
RA Pih K.T., Park J.M., Jang H.J., Kang S.G., Piao H.L., Hwang I.H.;
RT "EST of salt inducible mRNA in Arabidopsis thaliana.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, 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 [5]
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).
CC -!- FUNCTION: Involved in transcriptional regulation and chromatin
CC remodeling. Facilitates DNA replication in multiple cellular
CC environments and is required for efficient replication of a subset of
CC genomic loci. Binds to DNA tandem repeat sequences in both telomeres
CC and euchromatin and in vitro binds DNA quadruplex structures. May help
CC stabilizing G-rich regions into regular chromatin structures by
CC remodeling G4 DNA and incorporating H3.3-containing nucleosomes (By
CC similarity). Involved in DNA repair of gamma-irradiation-mediated
CC damages (PubMed:16547115). {ECO:0000250|UniProtKB:Q61687,
CC ECO:0000269|PubMed:16547115}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q61687}.
CC Chromosome, telomere {ECO:0000250|UniProtKB:Q61687}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4HW51-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4HW51-2; Sequence=VSP_057103;
CC -!- DOMAIN: The ADD domain predominantly interacts with histone H3
CC trimethylated at 'Lys-10'(H3K9me3) (and to a lesser extent H3 mono- or
CC dimethylated at 'Lys-10') and simultanously to histone H3 unmethylated
CC at 'Lys-5' (H3K4me0). The interaction with H3K9me3 is disrupted by the
CC presence of H3K4me3 suggesting a readout of the combined histone H3
CC methylation state. {ECO:0000250|UniProtKB:P46100}.
CC -!- DISRUPTION PHENOTYPE: Slight sensitivity to gamma-irradiation.
CC {ECO:0000269|PubMed:16547115}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51700.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF99756.1; Type=Erroneous gene model prediction;
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DR EMBL; AC003981; AAF99756.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28313.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28314.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28315.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28316.1; -; Genomic_DNA.
DR EMBL; U75593; AAB51700.1; ALT_FRAME; mRNA.
DR PIR; F86218; F86218.
DR PIR; T00713; T00713.
DR RefSeq; NP_001184937.1; NM_001198008.2. [F4HW51-1]
DR RefSeq; NP_001184938.1; NM_001198009.1. [F4HW51-1]
DR RefSeq; NP_001184939.1; NM_001198010.1. [F4HW51-1]
DR RefSeq; NP_172336.4; NM_100733.5. [F4HW51-2]
DR AlphaFoldDB; F4HW51; -.
DR SMR; F4HW51; -.
DR STRING; 3702.AT1G08600.4; -.
DR iPTMnet; F4HW51; -.
DR PaxDb; F4HW51; -.
DR PRIDE; F4HW51; -.
DR ProteomicsDB; 246785; -. [F4HW51-1]
DR EnsemblPlants; AT1G08600.1; AT1G08600.1; AT1G08600. [F4HW51-2]
DR EnsemblPlants; AT1G08600.2; AT1G08600.2; AT1G08600. [F4HW51-1]
DR EnsemblPlants; AT1G08600.3; AT1G08600.3; AT1G08600. [F4HW51-1]
DR EnsemblPlants; AT1G08600.4; AT1G08600.4; AT1G08600. [F4HW51-1]
DR GeneID; 837382; -.
DR Gramene; AT1G08600.1; AT1G08600.1; AT1G08600. [F4HW51-2]
DR Gramene; AT1G08600.2; AT1G08600.2; AT1G08600. [F4HW51-1]
DR Gramene; AT1G08600.3; AT1G08600.3; AT1G08600. [F4HW51-1]
DR Gramene; AT1G08600.4; AT1G08600.4; AT1G08600. [F4HW51-1]
DR KEGG; ath:AT1G08600; -.
DR Araport; AT1G08600; -.
DR TAIR; locus:2025560; AT1G08600.
DR eggNOG; KOG1015; Eukaryota.
DR HOGENOM; CLU_002089_0_0_1; -.
DR OMA; VPNVCET; -.
DR PRO; PR:F4HW51; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HW51; baseline and differential.
DR Genevisible; F4HW51; AT.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0043007; P:maintenance of rDNA; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:1900049; P:regulation of histone exchange; IMP:TAIR.
DR CDD; cd18069; DEXHc_ARIP4; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR025766; ADD.
DR InterPro; IPR044574; ARIP4-like.
DR InterPro; IPR044573; ARIP4_DEXHc.
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 PANTHER; PTHR45797; PTHR45797; 1.
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; PS51533; ADD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Chromatin regulator; Chromosome;
KW Coiled coil; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome; Telomere;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1479
FT /note="Protein CHROMATIN REMODELING 20"
FT /id="PRO_0000430857"
FT DOMAIN 472..601
FT /note="ADD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT DOMAIN 741..924
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1122..1290
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 483..514
FT /note="GATA-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT ZN_FING 524..577
FT /note="PHD-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT REGION 40..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1400..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 19..49
FT /evidence="ECO:0000255"
FT COILED 109..199
FT /evidence="ECO:0000255"
FT COILED 578..598
FT /evidence="ECO:0000255"
FT MOTIF 875..878
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 40..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 754..761
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VAR_SEQ 820..850
FT /note="ERRFDLLTKWRKKGGVFLMGYTNFRNLSLGR -> YKFFYERNFW (in
FT isoform 2)"
FT /id="VSP_057103"
SQ SEQUENCE 1479 AA; 168176 MW; 38097CF3BD412F3B CRC64;
MEANEESLKG KIEKLEGKEV IVESKEDEMD IIIEENREAE QEVMEVKARD GRGEQNDVLM
EENNNQGEQK DEEMQDASSR SESSDFNSDE DEQILSRRDD ELDLEKPLSE EEIDELISDL
LAVESKAAEA QEALEKESLS KVESEVREEL AQALRGDELD EAVAAEMMTF KDEWEATLDE
LETESATLLE QLDGAGIELP KLYEMIESQA PNGCYTEAWK QRAHWVGTQV TKETVESLAN
AERFLHTHRP VRKRHGKLLE EGASGFLEKK LADGAVKESL AGTSELDWSS LNKVFSEKRD
ESVSFGSKQW ASVYLASTPH QAAAMGLEFP GVNEVEEIEE IDASLADPFL ADAIDNEREL
ALTEEQKTNY IRVKEEDDIT CDRVLQLRLK RKRRKKRSKQ VIRCAAENMD DDSVYLDGNN
TTPNFAKDQV KSPETSTQVH NSEVNIEENG NFSNSDVDKM TPSTHINVDA KRDDSQNPAN
NFRCTACNKV AVEVHSHPLL EVIVCMDCKR SIEDRVSKVD DSLERHCEWC GHIADLIDCR
TCEKLFCASC IKRNIGEEYM SEAQSSGWDC CCCSPIPLQR LTLELEKAMR DKKSIELSSD
SSSDSSSDNN SVDTDADVNV TISSKKKSKK KIRRIIDDAE LGKDTRTKIA IEKARQERLR
SLQFSARYKT ISSMGDVKSI PEGAEVEVLG DAHSGYIVNV VREIGEEAVR VPRSISAKLK
VHQVTGIRFM WENIIQSISR VKSGDKGLGC ILAHTMGLGK TFQVIAFLYT AMRCVDLGLK
TALIVTPVNV LHNWRSEFEK WMPSEVKPLR IFMLGDVSRE RRFDLLTKWR KKGGVFLMGY
TNFRNLSLGR GVKDLNAARG ICNALRDGPD ILVCDEAHII KNTKADTTQA LKQVKCQRRI
ALTGSPLQNN LMEYYCMVDF VREGFLGSSP EFRNRFQNPI ENGQHMNSTA EDVKIMNQRS
HILYEQLKGF VQRMDMNVVK KDLPPKTVFV ISVKLSPLQR ILYQRFLELY GFSDGRTDER
MRKNFFAAYQ VLAQILNHPG IPQLRSEDSK NGRRGSIVDI PDDCSSDENI DYNMVTGEKQ
RTMNDLQDKV DGYLQKDWWV DLLQKNNYKV SDFSGKMILL LDILSMSADV GDKALVFSQS
IPTLDLIELY LSRVPRHGKQ GKFWKKGKDW YRIDGKTESS ERQKLVDRFN EPDNKRVKCT
LISTRAGSLG INLYAANRVI IVDGSWNPTY DLQAIFRAWR YGQKKPVFAY RLMARGTIEE
KIYKRQVTKE GLAARVVDRQ QVHRTISKEE MLHLFEFDDD DEKSEAVTEI SKQNEAGHSN
LVEQAILWTK KATLSRVGGD KLMENLLQRH GPNWISSFHE HETLLQENEE ERLTKEEKDM
AWEVYRRALE WEEVQRVPFS ESPVVPKPSP STQTEPLPQP KGFNRSRFVN RNCTRIAHQL
TLISQGLKVG SSTVCGECGR VIRWEDVIPA SKLSAVIVN
