RA51D_MOUSE
ID RA51D_MOUSE Reviewed; 329 AA.
AC O55230;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=DNA repair protein RAD51 homolog 4;
DE AltName: Full=R51H3;
DE AltName: Full=RAD51 homolog D;
DE AltName: Full=RAD51-like protein 3;
GN Name=Rad51d; Synonyms=R51h3, Rad51l3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=9570954; DOI=10.1006/geno.1998.5226;
RA Pittman D.L., Weinberg L.R., Schimenti J.C.;
RT "Identification, characterization, and genetic mapping of Rad51d, a new
RT mouse and human RAD51/RecA-related gene.";
RL Genomics 49:103-111(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9512535; DOI=10.1093/nar/26.7.1653;
RA Cartwright R., Dunn A.M., Simpson P.J., Tambini C.E., Thacker J.;
RT "Isolation of novel human and mouse genes of the recA/RAD51 recombination-
RT repair gene family.";
RL Nucleic Acids Res. 26:1653-1659(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kawabata M.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=10705376;
RX DOI=10.1002/(sici)1526-968x(200003)26:3<167::aid-gene1>3.0.co;2-m;
RA Pittman D.L., Schimenti J.C.;
RT "Midgestation lethality in mice deficient for the RecA-related gene,
RT Rad51d/Rad51l3.";
RL Genesis 26:167-173(2000).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15109494; DOI=10.1016/s0092-8674(04)00337-x;
RA Tarsounas M., Munoz P., Claas A., Smiraldo P.G., Pittman D.L., Blasco M.A.,
RA West S.C.;
RT "Telomere maintenance requires the RAD51D recombination/repair protein.";
RL Cell 117:337-347(2004).
RN [8]
RP INTERACTION WITH RAD51C AND XRCC2.
RX PubMed=14704354; DOI=10.1093/nar/gkg925;
RA Miller K.A., Sawicka D., Barsky D., Albala J.S.;
RT "Domain mapping of the Rad51 paralog protein complexes.";
RL Nucleic Acids Res. 32:169-178(2004).
CC -!- FUNCTION: Involved in the homologous recombination repair (HRR) pathway
CC of double-stranded DNA breaks arising during DNA replication or induced
CC by DNA-damaging agents. Bind to single-stranded DNA (ssDNA) and has
CC DNA-dependent ATPase activity. Part of the RAD51 paralog protein
CC complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon
CC DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of
CC RAD51 recruitment. BCDX2 binds predominantly to the intersection of the
CC four duplex arms of the Holliday junction and to junction of
CC replication forks. The BCDX2 complex was originally reported to bind
CC single-stranded DNA, single-stranded gaps in duplex DNA and
CC specifically to nicks in duplex DNA. Involved in telomere maintenance.
CC The BCDX2 subcomplex XRCC2:RAD51D can stimulate Holliday junction
CC resolution by BLM (By similarity). {ECO:0000250|UniProtKB:O75771,
CC ECO:0000269|PubMed:15109494}.
CC -!- SUBUNIT: Part of the BCDX2 complex consisting of RAD51B, RAD51C, RAD51D
CC and XRCC2; the complex has a ring-like structure arranged into a flat
CC disc around a central channel. In the absence of DNA, the BCDX2
CC subcomplex XRCC2:RAD51D formed a multimeric ring structure; in the
CC presence of single-stranded DNA it formed a filamentous structure with
CC the ssDNA. Interacts with SWSAP1 and ZSWIM7; involved in homologous
CC recombination repair. Interacts with BLM; required for stimulation of
CC BLM activity by the BCDX2 subcomplex XRCC2:RAD51D (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere
CC {ECO:0000269|PubMed:15109494}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=At least 2 isoforms are produced.;
CC Name=1;
CC IsoId=O55230-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain followed by testis. Also
CC expressed in heart, liver, kidney, spleen, lung and skeletal muscle.
CC -!- DISRUPTION PHENOTYPE: Midgestation lethal.
CC {ECO:0000269|PubMed:10705376}.
CC -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily. {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; AB007040; BAA24010.1; -; mRNA.
DR EMBL; AF034955; AAC40093.1; -; mRNA.
DR EMBL; Y15570; CAA75679.1; -; mRNA.
DR EMBL; AK017835; BAB30965.1; -; mRNA.
DR EMBL; BC049136; AAH49136.1; -; mRNA.
DR CCDS; CCDS36250.1; -. [O55230-1]
DR RefSeq; NP_035365.1; NM_011235.4. [O55230-1]
DR AlphaFoldDB; O55230; -.
DR SMR; O55230; -.
DR BioGRID; 202567; 5.
DR IntAct; O55230; 1.
DR MINT; O55230; -.
DR STRING; 10090.ENSMUSP00000018985; -.
DR PhosphoSitePlus; O55230; -.
DR EPD; O55230; -.
DR PaxDb; O55230; -.
DR PRIDE; O55230; -.
DR ProteomicsDB; 301913; -. [O55230-1]
DR Antibodypedia; 15549; 376 antibodies from 33 providers.
DR DNASU; 19364; -.
DR Ensembl; ENSMUST00000018985; ENSMUSP00000018985; ENSMUSG00000018841. [O55230-1]
DR GeneID; 19364; -.
DR KEGG; mmu:19364; -.
DR UCSC; uc007knm.2; mouse. [O55230-1]
DR CTD; 5892; -.
DR MGI; MGI:1261809; Rad51d.
DR VEuPathDB; HostDB:ENSMUSG00000018841; -.
DR eggNOG; KOG1433; Eukaryota.
DR GeneTree; ENSGT00940000159095; -.
DR HOGENOM; CLU_058452_0_0_1; -.
DR InParanoid; O55230; -.
DR OMA; QRIHTFR; -.
DR OrthoDB; 1214879at2759; -.
DR PhylomeDB; O55230; -.
DR TreeFam; TF101219; -.
DR Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-MMU-5693579; Homologous DNA Pairing and Strand Exchange.
DR Reactome; R-MMU-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR BioGRID-ORCS; 19364; 24 hits in 111 CRISPR screens.
DR ChiTaRS; Rad51c; mouse.
DR PRO; PR:O55230; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O55230; protein.
DR Bgee; ENSMUSG00000018841; Expressed in granulocyte and 237 other tissues.
DR ExpressionAtlas; O55230; baseline and differential.
DR Genevisible; O55230; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0033063; C:Rad51B-Rad51C-Rad51D-XRCC2 complex; ISS:UniProtKB.
DR GO; GO:0005657; C:replication fork; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISS:UniProtKB.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:Ensembl.
DR GO; GO:0000400; F:four-way junction DNA binding; ISO:MGI.
DR GO; GO:0043015; F:gamma-tubulin binding; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
DR GO; GO:0051276; P:chromosome organization; IMP:MGI.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0036297; P:interstrand cross-link repair; IMP:MGI.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
DR GO; GO:0042148; P:strand invasion; ISS:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; IGI:BHF-UCL.
DR GO; GO:0000722; P:telomere maintenance via recombination; ISS:BHF-UCL.
DR CDD; cd01123; Rad51_DMC1_radA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR InterPro; IPR016467; DNA_recomb/repair_RecA-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033925; Rad51_DMC1_RadA.
DR InterPro; IPR020588; RecA_ATP-bd.
DR Pfam; PF08423; Rad51; 1.
DR PIRSF; PIRSF005856; Rad51; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50162; RECA_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chromosome; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; Telomere.
FT CHAIN 1..329
FT /note="DNA repair protein RAD51 homolog 4"
FT /id="PRO_0000122943"
FT REGION 1..83
FT /note="preferentially binds ssDNA"
FT /evidence="ECO:0000250"
FT REGION 4..77
FT /note="Interaction with XRCC2"
FT /evidence="ECO:0000269|PubMed:14704354"
FT REGION 77..328
FT /note="Interaction with RAD51C"
FT /evidence="ECO:0000269|PubMed:14704354"
FT BINDING 107..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 329 AA; 35260 MW; 6E463822408EF484 CRC64;
MGMLRAGLCP GLTEETVQLL RGRKIKTVAD LAAADLEEVA QKCGLSYKAL VALRRVLLAQ
FSAFPLNGAD LYEELKTSTA ILSTGIGSLD KLLDAGLYTG EVTEIVGGPG SGKTQVCLCV
AANVAHSLQQ NVLYVDSNGG MTASRLLQLL QARTQDEEKQ ASALQRIQVV RSFDIFRMLD
MLQDLRGTIA QQEATSSGAV KVVIVDSVTA VVAPLLGGQQ REGLALMMQL ARELKILARD
LGVAVVVTNH LTRDWDGRRF KPALGRSWSF VPSTRILLDV TEGAGTLGSS QRTVCLTKSP
RQPTGLQEMI DIGTLGTEEQ SPELPGKQT
