RAD51_ARATH
ID RAD51_ARATH Reviewed; 342 AA.
AC P94102;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=DNA repair protein RAD51 homolog 1 {ECO:0000303|PubMed:9520262};
DE AltName: Full=Rad51-like protein 1 {ECO:0000303|PubMed:9520262};
DE Short=AtRAD51 {ECO:0000303|PubMed:9520262};
GN Name=RAD51 {ECO:0000303|PubMed:9520262};
GN OrderedLocusNames=At5g20850 {ECO:0000312|Araport:AT5G20850};
GN ORFNames=F22D1.20 {ECO:0000312|EMBL:AF296834};
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 [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8980505; DOI=10.1007/bf00019108;
RA Urban C., Smith K.N., Beier H.;
RT "Nucleotide sequences of nuclear tRNA(Cys) genes from Nicotiana and
RT Arabidopsis and expression in HeLa cell extract.";
RL Plant Mol. Biol. 32:549-552(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, DEVELOPMENTAL STAGE, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9520262; DOI=10.1007/s004380050649;
RA Doutriaux M.P., Couteau F., Bergounioux C., White C.;
RT "Isolation and characterisation of the RAD51 and DMC1 homologs from
RT Arabidopsis thaliana.";
RL Mol. Gen. Genet. 257:283-291(1998).
RN [3]
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 [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 INDUCTION.
RX PubMed=10894550; DOI=10.1038/35017595;
RA Ries G., Heller W., Puchta H., Sandermann H., Seidlitz H.K., Hohn B.;
RT "Elevated UV-B radiation reduces genome stability in plants.";
RL Nature 406:98-101(2000).
RN [6]
RP INDUCTION, SUBUNIT, TISSUE SPECIFICITY, AND INTERACTION WITH XRCC3.
RC STRAIN=cv. Columbia; TISSUE=Flower bud;
RX PubMed=12139010; DOI=10.1023/a:1016047231597;
RA Osakabe K., Yoshioka T., Ichikawa H., Toki S.;
RT "Molecular cloning and characterization of RAD51-like genes from
RT Arabidopsis thaliana.";
RL Plant Mol. Biol. 50:71-81(2002).
RN [7]
RP INDUCTION.
RX PubMed=12509526; DOI=10.1105/tpc.006577;
RA Garcia V., Bruchet H., Camescasse D., Granier F., Bouchez D., Tissier A.;
RT "AtATM is essential for meiosis and the somatic response to DNA damage in
RT plants.";
RL Plant Cell 15:119-132(2003).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15249667; DOI=10.1073/pnas.0404110101;
RA Li W., Chen C., Markmann-Mulisch U., Timofejeva L., Schmelzer E., Ma H.,
RA Reiss B.;
RT "The Arabidopsis AtRAD51 gene is dispensable for vegetative development but
RT required for meiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10596-10601(2004).
RN [9]
RP INTERACTION WITH RAD54/CHR25, AND TISSUE SPECIFICITY.
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 [10]
RP INTERACTION WITH BRCA2A AND BRCA2B.
RX PubMed=16415210; DOI=10.1104/pp.105.075838;
RA Dray E., Siaud N., Dubois E., Doutriaux M.P.;
RT "Interaction between Arabidopsis Brca2 and its partners Rad51, Dmc1, and
RT Dss1.";
RL Plant Physiol. 140:1059-1069(2006).
CC -!- FUNCTION: Binds to single and double-stranded DNA and exhibits DNA-
CC dependent ATPase activity. Unwinds duplex DNA (By similarity).
CC Component of the meiotic recombination pathway. Seems to play a role in
CC mediating chromosome homology search, chromosome pairing and synapsis
CC at early stages and probably chromosome crossing-over at later stages
CC in meiosis. Probably is involved in the repair of meiotic double strand
CC breaks (DBSs) generated by AtSPO11-1 and in homologous recombination.
CC Its function is dispensable for vegetative growth and root mitosis.
CC {ECO:0000250|UniProtKB:Q06609, ECO:0000269|PubMed:15249667}.
CC -!- SUBUNIT: Self-associates and interacts with XRCC3 (PubMed:12139010).
CC Binds to RAD54/CHR25 (PubMed:17227544). Interacts with BRCA2A and
CC BRCA2B (PubMed:16415210). Can form a tripartite complex with both
CC BRCA2B and DSS1(I) (PubMed:16415210). {ECO:0000269|PubMed:12139010,
CC ECO:0000269|PubMed:16415210, ECO:0000269|PubMed:17227544}.
CC -!- INTERACTION:
CC P94102; Q7Y1C5: BRCA2A; NbExp=5; IntAct=EBI-307687, EBI-307680;
CC P94102; Q7Y1C4: BRCA2B; NbExp=5; IntAct=EBI-307687, EBI-307707;
CC P94102; Q0PCS3: CHR25; NbExp=3; IntAct=EBI-307687, EBI-1768899;
CC P94102; Q39009: DMC1; NbExp=4; IntAct=EBI-307687, EBI-307715;
CC P94102; Q8GYD2: MND1; NbExp=2; IntAct=EBI-307687, EBI-1554720;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in various tissues. Higher expression in
CC reproductive tissues than in vegetative tissues, with the highest
CC expression level in young flower buds. At cellular level, is expressed
CC at low levels in flower primordia, then at higher levels in young
CC anthers and at highest levels in both females and males meiocytes. Not
CC detected in gametophytes. {ECO:0000269|PubMed:12139010,
CC ECO:0000269|PubMed:15249667, ECO:0000269|PubMed:17227544,
CC ECO:0000269|PubMed:9520262}.
CC -!- DEVELOPMENTAL STAGE: Cell cycle regulated, peaking at the S phase. It
CC is also expressed at high levels in exponentially growing cells in
CC suspension cultures. {ECO:0000269|PubMed:9520262}.
CC -!- INDUCTION: By genotoxic stress and by DNA damage (gamma-radiation, UV-
CC B). Regulated by ATM in response to DNA double strand breaks (DSBs).
CC {ECO:0000269|PubMed:10894550, ECO:0000269|PubMed:12139010,
CC ECO:0000269|PubMed:12509526, ECO:0000269|PubMed:9520262}.
CC -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily. {ECO:0000305}.
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DR EMBL; U43652; AAC49555.1; -; Genomic_DNA.
DR EMBL; AJ001100; CAA04529.1; -; Genomic_DNA.
DR EMBL; U43528; AAB37762.1; -; mRNA.
DR EMBL; AF296834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92897.1; -; Genomic_DNA.
DR RefSeq; NP_568402.1; NM_122092.3.
DR AlphaFoldDB; P94102; -.
DR SMR; P94102; -.
DR BioGRID; 17483; 9.
DR DIP; DIP-31780N; -.
DR IntAct; P94102; 11.
DR STRING; 3702.AT5G20850.1; -.
DR PaxDb; P94102; -.
DR ProteomicsDB; 236500; -.
DR EnsemblPlants; AT5G20850.1; AT5G20850.1; AT5G20850.
DR GeneID; 832208; -.
DR Gramene; AT5G20850.1; AT5G20850.1; AT5G20850.
DR KEGG; ath:AT5G20850; -.
DR Araport; AT5G20850; -.
DR TAIR; locus:2147092; AT5G20850.
DR eggNOG; KOG1433; Eukaryota.
DR HOGENOM; CLU_041732_0_0_1; -.
DR InParanoid; P94102; -.
DR OMA; TFRIYLR; -.
DR OrthoDB; 877394at2759; -.
DR PhylomeDB; P94102; -.
DR PRO; PR:P94102; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P94102; baseline and differential.
DR Genevisible; P94102; AT.
DR GO; GO:0005694; C:chromosome; IDA:TAIR.
DR GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0000150; F:DNA strand exchange activity; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0006259; P:DNA metabolic process; IDA:TAIR.
DR GO; GO:0000730; P:DNA recombinase assembly; IBA:GO_Central.
DR GO; GO:0006302; P:double-strand break repair; IMP:TAIR.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IDA:TAIR.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IEA:InterPro.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0010332; P:response to gamma radiation; IEP:TAIR.
DR GO; GO:0009314; P:response to radiation; NAS:TAIR.
DR GO; GO:0042148; P:strand invasion; IBA:GO_Central.
DR CDD; cd01123; Rad51_DMC1_radA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011941; DNA_recomb/repair_Rad51.
DR InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR InterPro; IPR016467; DNA_recomb/repair_RecA-like.
DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033925; Rad51_DMC1_RadA.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR Pfam; PF08423; Rad51; 1.
DR PIRSF; PIRSF005856; Rad51; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47794; SSF47794; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02239; recomb_RAD51; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..342
FT /note="DNA repair protein RAD51 homolog 1"
FT /id="PRO_0000122926"
FT DOMAIN 51..80
FT /note="HhH"
FT DOMAIN 100..314
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 130..137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 342 AA; 37304 MW; 08067F8D85A2E77D CRC64;
MTTMEQRRNQ NAVQQQDDEE TQHGPFPVEQ LQAAGIASVD VKKLRDAGLC TVEGVAYTPR
KDLLQIKGIS DAKVDKIVEA ASKLVPLGFT SASQLHAQRQ EIIQITSGSR ELDKVLEGGI
ETGSITELYG EFRSGKTQLC HTLCVTCQLP MDQGGGEGKA MYIDAEGTFR PQRLLQIADR
FGLNGADVLE NVAYARAYNT DHQSRLLLEA ASMMIETRFA LLIVDSATAL YRTDFSGRGE
LSARQMHLAK FLRSLQKLAD EFGVAVVITN QVVAQVDGSA LFAGPQFKPI GGNIMAHATT
TRLALRKGRA EERICKVISS PCLPEAEARF QISTEGVTDC KD
