CHR25_ARATH
ID CHR25_ARATH Reviewed; 910 AA.
AC Q0PCS3; F4JB43; Q9LJK7;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein CHROMATIN REMODELING 25;
DE Short=AtCHR25;
DE EC=3.6.4.-;
DE AltName: Full=DNA repair and recombination protein RAD54 {ECO:0000303|PubMed:17227544};
DE Short=AtRAD54 {ECO:0000303|PubMed:17227544};
GN Name=CHR25; Synonyms=RAD54 {ECO:0000303|PubMed:17227544};
GN OrderedLocusNames=At3g19210 {ECO:0000312|Araport:AT3G19210};
GN ORFNames=MVI11.13 {ECO:0000312|EMBL:BAB02963.1};
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:BAF03042.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE,
RP INTERACTION WITH RAD51, TISSUE SPECIFICITY, AND INDUCTION BY
RP GAMMA-IRRADIATION.
RC STRAIN=cv. Columbia; TISSUE=Flower bud;
RX PubMed=17227544; DOI=10.1111/j.1365-313x.2006.02927.x;
RA Osakabe K., Abe K., Yoshioka T., Osakabe Y., Todoriki S., Ichikawa H.,
RA Hohn B., Toki S.;
RT "Isolation and characterization of the RAD54 gene from Arabidopsis
RT thaliana.";
RL Plant J. 48:827-842(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RP RAD51.
RX PubMed=18430956; DOI=10.1534/genetics.108.086777;
RA Klutstein M., Shaked H., Sherman A., Avivi-Ragolsky N., Shema E.,
RA Zenvirth D., Levy A.A., Simchen G.;
RT "Functional conservation of the yeast and Arabidopsis RAD54-like genes.";
RL Genetics 178:2389-2397(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [4]
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 [5]
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 [6]
RP INDUCTION BY FORMALDEHYDE.
RX PubMed=20399886; DOI=10.1016/j.mrgentox.2010.04.009;
RA Li F., Liu P., Wang T., Bian P., Wu Y., Wu L., Yu Z.;
RT "Genotoxicity/mutagenicity of formaldehyde revealed by the Arabidopsis
RT thaliana plants transgenic for homologous recombination substrates.";
RL Mutat. Res. 699:35-43(2010).
RN [7]
RP INDUCTION BY LOW-ENERGY-ION IRRADIATION.
RX PubMed=21557702; DOI=10.3109/09553002.2011.574780;
RA Li F., Wang T., Xu S., Yuan H., Bian P., Wu Y., Wu L., Yu Z.;
RT "Abscopal mutagenic effect of low-energy-ions in Arabidopsis thaliana
RT seeds.";
RL Int. J. Radiat. Biol. 87:984-992(2011).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH THE GEMINIVIRUS MUNGBEAN
RP YELLOW MOSAIC VIRUS (MYMV) AND TOMATO LEAF CURL VIRUS (TOLCV)
RP REPLICATION-ASSOCIATED PROTEIN, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=cv. Columbia;
RX PubMed=22171001; DOI=10.1096/fj.11-188508;
RA Kaliappan K., Choudhury N.R., Suyal G., Mukherjee S.K.;
RT "A novel role for RAD54: this host protein modulates geminiviral DNA
RT replication.";
RL FASEB J. 26:1142-1160(2012).
RN [9]
RP INDUCTION BY HEAVY ION IRRADIATION.
RX PubMed=22683605; DOI=10.1016/j.mrfmmm.2012.05.006;
RA Wang T., Li F., Liu Q., Bian P., Wang J., Wu Y., Wu L., Li W.;
RT "Homologous recombination in Arabidopsis seeds along the track of energetic
RT carbon ions.";
RL Mutat. Res. 737:51-57(2012).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22860689; DOI=10.1111/j.1365-313x.2012.05119.x;
RA Roth N., Klimesch J., Dukowic-Schulze S., Pacher M., Mannuss A., Puchta H.;
RT "The requirement for recombination factors differs considerably between
RT different pathways of homologous double-strand break repair in somatic
RT plant cells.";
RL Plant J. 72:781-790(2012).
RN [11]
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: Dissociates RAD51 from nucleoprotein filaments formed on
CC dsDNA. Could be involved in the turnover of RAD51 protein-dsDNA
CC filaments. Addition of RAD54 overcomes inhibition of DNA strand
CC exchange by RAD51 bound to substrate dsDNA. Species preference in the
CC RAD51 dissociation and DNA strand exchange assays underlines the
CC importance of specific RAD54-RAD51 interactions. RAD51 is unable to
CC release dsDNA upon ATP hydrolysis, leaving it stuck on the heteroduplex
CC DNA product after DNA strand exchange (By similarity). Involved in DNA
CC repair and mitotic recombination (PubMed:17227544, PubMed:16547115,
CC PubMed:18430956). Functions in the homologous recombinational DNA
CC repair (RAD52) pathway (PubMed:17227544, PubMed:16547115,
CC PubMed:18430956). Required for synthesis-dependent strand annealing
CC (SDSA) during double-strand break repair (PubMed:22860689).
CC {ECO:0000250|UniProtKB:P32863, ECO:0000269|PubMed:16547115,
CC ECO:0000269|PubMed:17227544, ECO:0000269|PubMed:18430956,
CC ECO:0000269|PubMed:22860689}.
CC -!- FUNCTION: Facilitates geminiviral replication (e.g. geminivirus
CC mungbean yellow mosaic virus (MYMV) and tomato leaf curl virus
CC (ToLCV)). {ECO:0000269|PubMed:22171001}.
CC -!- SUBUNIT: Interacts with RAD51 (PubMed:17227544, PubMed:18430956). Binds
CC to the geminivirus mungbean yellow mosaic virus (MYMV) and to the
CC tomato leaf curl virus (ToLCV) replication-associated proteins
CC (PubMed:22171001). {ECO:0000269|PubMed:17227544,
CC ECO:0000269|PubMed:18430956, ECO:0000269|PubMed:22171001}.
CC -!- INTERACTION:
CC Q0PCS3; P94102: RAD51; NbExp=3; IntAct=EBI-1768899, EBI-307687;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P32863}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q0PCS3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0PCS3-2; Sequence=VSP_057104;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously, with the highest levels of
CC expression in flower buds. Present in flower buds (at protein level).
CC {ECO:0000269|PubMed:17227544}.
CC -!- INDUCTION: Induced by gamma-irradiation and by heavy ion irradiation
CC (PubMed:17227544, PubMed:22683605). Induced by the genotoxic
CC formaldehyde (FA) (PubMed:20399886). Accumulates in aerial part of low-
CC energy-ion irradiated dormant plant seeds, thus revealing an abscopal
CC mutagenic effect (PubMed:21557702). {ECO:0000269|PubMed:17227544,
CC ECO:0000269|PubMed:20399886, ECO:0000269|PubMed:21557702,
CC ECO:0000269|PubMed:22683605}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to gamma-irradiation and to
CC the cross-linking reagent cisplatin (PubMed:17227544). Reduced
CC efficiency of somatic homologous recombination (HR) (PubMed:17227544,
CC PubMed:16547115). Reduced synthesis-dependent strand annealing (SDSA)
CC frequency (PubMed:22860689). Impaired geminiviral replication (e.g.
CC tomato leaf curl virus (ToLCV)) (PubMed:22171001).
CC {ECO:0000269|PubMed:16547115, ECO:0000269|PubMed:17227544,
CC ECO:0000269|PubMed:22171001, ECO:0000269|PubMed:22860689}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02963.1; Type=Erroneous gene model prediction;
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DR EMBL; AB250666; BAF03042.1; -; mRNA.
DR EMBL; DQ912973; ABJ99465.1; -; mRNA.
DR EMBL; AP000419; BAB02963.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76208.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76209.1; -; Genomic_DNA.
DR RefSeq; NP_001189933.1; NM_001203004.1. [Q0PCS3-2]
DR RefSeq; NP_188552.3; NM_112808.4. [Q0PCS3-1]
DR AlphaFoldDB; Q0PCS3; -.
DR SMR; Q0PCS3; -.
DR BioGRID; 6788; 5.
DR IntAct; Q0PCS3; 4.
DR STRING; 3702.AT3G19210.1; -.
DR iPTMnet; Q0PCS3; -.
DR PaxDb; Q0PCS3; -.
DR PRIDE; Q0PCS3; -.
DR ProteomicsDB; 247002; -. [Q0PCS3-1]
DR EnsemblPlants; AT3G19210.1; AT3G19210.1; AT3G19210. [Q0PCS3-1]
DR EnsemblPlants; AT3G19210.2; AT3G19210.2; AT3G19210. [Q0PCS3-2]
DR GeneID; 821455; -.
DR Gramene; AT3G19210.1; AT3G19210.1; AT3G19210. [Q0PCS3-1]
DR Gramene; AT3G19210.2; AT3G19210.2; AT3G19210. [Q0PCS3-2]
DR KEGG; ath:AT3G19210; -.
DR Araport; AT3G19210; -.
DR TAIR; locus:2094083; AT3G19210.
DR eggNOG; KOG0390; Eukaryota.
DR HOGENOM; CLU_000315_10_4_1; -.
DR InParanoid; Q0PCS3; -.
DR PhylomeDB; Q0PCS3; -.
DR PRO; PR:Q0PCS3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0PCS3; baseline and differential.
DR Genevisible; Q0PCS3; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0015616; F:DNA translocase activity; 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:0051701; P:biological process involved in interaction with host; IPI:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071480; P:cellular response to gamma radiation; IEP:UniProtKB.
DR GO; GO:0071248; P:cellular response to metal ion; IEP:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:TAIR.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IDA:TAIR.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR GO; GO:0010332; P:response to gamma radiation; IEP:TAIR.
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; 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 Alternative splicing; ATP-binding; Cell cycle; Cell division; Coiled coil;
KW DNA damage; DNA repair; DNA-binding; Helicase; Host-virus interaction;
KW Hydrolase; Mitosis; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..910
FT /note="Protein CHROMATIN REMODELING 25"
FT /id="PRO_0000430859"
FT DOMAIN 198..371
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 538..696
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 396..417
FT /evidence="ECO:0000255"
FT MOTIF 322..325
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 211..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VAR_SEQ 447..458
FT /note="STLYNHFISSKN -> TTYNGCLCMQ (in isoform 2)"
FT /id="VSP_057104"
SQ SEQUENCE 910 AA; 101858 MW; 3423B9EC60C0D8AE CRC64;
MEEEDEEILS SSDCDDSSDS YKDDSQDSEG ENDNPECEDL AVVSLSSDAD RKSKNVKDLL
RGNLVVQRQP LLPRVLSVSD GAAVCRKPFK PPCSHGYDST GQLSRRLSAR KRFVPWGSST
PVVVALPTKL EASTNIERDE EEEVVCLPPD IEPLVLWQSE EDGMSNVTTI MVHSVLVKFL
RPHQREGVQF MFDCVSGLHG SANINGCILA DDMGLGKTLQ SITLLYTLLC QGFDGTPMVK
KAIIVTPTSL VSNWEAEIKK WVGDRIQLIA LCESTRDDVL SGIDSFTRPR SALQVLIISY
ETFRMHSSKF CQSESCDLLI CDEAHRLKND QTLTNRALAS LTCKRRVLLS GTPMQNDLEE
FFAMVNFTNP GSLGDAAHFR HYYEAPIICG REPTATEEEK NLAADRSAEL SSKVNQFILR
RTNALLSNHL PPKIIEVVCC KMTTLQSTLY NHFISSKNLK RALADNAKQT KVLAYITALK
KLCNHPKLIY DTIKSGNPGT VGFENCLEFF PAEMFSGRSG AWTGGDGAWV ELSGKMHVLS
RLLANLRRKT DDRIVLVSNY TQTLDLFAQL CRERRYPFLR LDGSTTISKR QKLVNRLNDP
TKDEFAFLLS SKAGGCGLNL IGANRLVLFD PDWNPANDKQ AAARVWRDGQ KKRVYVYRFL
STGTIEEKVY QRQMSKEGLQ KVIQHEQTDN STRQGNLLST EDLRDLFSFH GDVRSEIHEK
MSCSRCQNDA SGTENIEEGN ENNVDDNACQ IDQEDIGGFA KDAGCFNLLK NSERQVGTPL
EEDLGSWGHH FTSKSVPDAI LQASAGDEVT FVFTNQVDGK LVPIESNVSP KTVESEEHNR
NQPVNKRAFN KPQQRPREPL QPLSLNETTK RVKLSTYKRL HGNSNIDDAQ IKMSLQRPNL
VSVNHDDDFV
