RA51C_MOUSE
ID RA51C_MOUSE Reviewed; 366 AA.
AC Q924H5; B2KGK7; Q5SX32; Q8C653;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=DNA repair protein RAD51 homolog 3;
DE Short=R51H3;
DE AltName: Full=RAD51 homolog C;
DE AltName: Full=RAD51-like protein 2;
GN Name=Rad51c; Synonyms=Rad51l2;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=11410366; DOI=10.1016/s0378-1119(01)00498-x;
RA Leasure C.S., Chandler J., Gilbert D.J., Householder D.B., Stephens R.,
RA Copeland N.G., Jenkins N.A., Sharan S.K.;
RT "Sequence, chromosomal location and expression analysis of the murine
RT homologue of human RAD51L2/RAD51C.";
RL Gene 271:59-67(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head;
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 FUNCTION.
RX PubMed=20471405; DOI=10.1016/j.mrfmmm.2010.05.001;
RA Smeenk G., de Groot A.J., Romeijn R.J., van Buul P.P., Zdzienicka M.Z.,
RA Mullenders L.H., Pastink A., Godthelp B.C.;
RT "Rad51C is essential for embryonic development and haploinsufficiency
RT causes increased DNA damage sensitivity and genomic instability.";
RL Mutat. Res. 689:50-58(2010).
RN [7]
RP INTERACTION WITH HELQ.
RX PubMed=24005329; DOI=10.1038/nature12565;
RA Adelman C.A., Lolo R.L., Birkbak N.J., Murina O., Matsuzaki K., Horejsi Z.,
RA Parmar K., Borel V., Skehel J.M., Stamp G., D'Andrea A., Sartori A.A.,
RA Swanton C., Boulton S.J.;
RT "HELQ promotes RAD51 paralogue-dependent repair to avert germ cell loss and
RT tumorigenesis.";
RL Nature 502:381-384(2013).
CC -!- FUNCTION: Essential for the homologous recombination (HR) pathway of
CC DNA repair. Involved in the homologous recombination repair (HRR)
CC pathway of double-stranded DNA breaks arising during DNA replication or
CC induced by DNA-damaging agents. Part of the RAD51 paralog protein
CC complexes BCDX2 and CX3 which act at different stages of the BRCA1-
CC BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 seems to act
CC downstream of BRCA2 recruitment and upstream of RAD51 recruitment; CX3
CC seems to act downstream of RAD51 recruitment; both complexes bind
CC predominantly to the intersection of the four duplex arms of the
CC Holliday junction (HJ) and to junction of replication forks. The BCDX2
CC complex was originally reported to bind single-stranded DNA, single-
CC stranded gaps in duplex DNA and specifically to nicks in duplex DNA.
CC The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA-
CC dependent ATPase activity suggesting an involvement in early stages of
CC the HR pathway. Involved in RAD51 foci formation in response to DNA
CC damage suggesting an involvement in early stages of HR probably in the
CC invasion step. Has an early function in DNA repair in facilitating
CC phosphorylation of the checkpoint kinase CHEK2 and thereby transduction
CC of the damage signal, leading to cell cycle arrest and HR activation.
CC Participates in branch migration and HJ resolution and thus is
CC important for processing HR intermediates late in the DNA repair
CC process; the function may be linked to the CX3 complex. Part of a
CC PALB2-scaffolded HR complex containing BRCA2 and which is thought to
CC play a role in DNA repair by HR. Protects RAD51 from ubiquitin-mediated
CC degradation that is enhanced following DNA damage. Plays a role in
CC regulating mitochondrial DNA copy number under conditions of oxidative
CC stress in the presence of RAD51 and XRCC3. Contributes to DNA cross-
CC link resistance, sister chromatid cohesion and genomic stability.
CC Involved in maintaining centrosome number in mitosis.
CC {ECO:0000269|PubMed:20471405}.
CC -!- SUBUNIT: Part of the RAD51 paralog protein complexes BCDX2 and CX3; the
CC complexes have a ring-like structure arranged into a flat disc around a
CC central channel (By similarity). The BCDX2 complex consits of RAD51B,
CC RAD51C, RAD51D and XRCC2; the CX3 complex consists of RAD51C and XRCC3
CC (By similarity). The BCDX2 subcomplex RAD51B:RAD51C interacts with
CC RAD51 (By similarity). Interacts with SWSAP1; involved in homologous
CC recombination repair (By similarity). Interacts directly with PALB2
CC which may serve as a scaffold for a HR complex containing PALB2, BRCA2,
CC RAD51C, RAD51 and XRCC3 (By similarity). Interacts with HELQ
CC (PubMed:24005329). {ECO:0000250|UniProtKB:O43502,
CC ECO:0000269|PubMed:24005329}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43502}. Cytoplasm
CC {ECO:0000250|UniProtKB:O43502}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:O43502}. Mitochondrion
CC {ECO:0000250|UniProtKB:O43502}. Note=DNA damage induces an increase in
CC nuclear levels. Accumulates in DNA damage induced nuclear foci or
CC RAD51C foci which is formed during the S or G2 phase of cell cycle.
CC Accumulation at DNA lesions requires the presence of NBN/NBS1, ATM and
CC RPA. {ECO:0000250|UniProtKB:O43502}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q924H5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q924H5-2; Sequence=VSP_040206;
CC -!- TISSUE SPECIFICITY: Expressed in the heart, brain, spleen, lung, liver,
CC kidney and testis but not detected in skeletal muscle.
CC {ECO:0000269|PubMed:11410366}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos at various developmental
CC stages. The expression is found to be higher between 11 and 15 days of
CC gestation compared to day 7 or 17. {ECO:0000269|PubMed:11410366}.
CC -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily. {ECO:0000305}.
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DR EMBL; AF324883; AAK58420.1; -; Genomic_DNA.
DR EMBL; AK076551; BAC36388.1; -; mRNA.
DR EMBL; CU406989; CAQ51530.1; -; Genomic_DNA.
DR EMBL; CU406969; CAQ51530.1; JOINED; Genomic_DNA.
DR EMBL; CU406989; CAQ51531.1; -; Genomic_DNA.
DR EMBL; CU406969; CAQ51531.1; JOINED; Genomic_DNA.
DR EMBL; CU406969; CAQ52016.1; -; Genomic_DNA.
DR EMBL; CU406989; CAQ52016.1; JOINED; Genomic_DNA.
DR EMBL; CU406969; CAQ52015.1; -; Genomic_DNA.
DR EMBL; CU406989; CAQ52015.1; JOINED; Genomic_DNA.
DR EMBL; AL596130; CAI24486.1; -; Genomic_DNA.
DR EMBL; AL669902; CAI24486.1; JOINED; Genomic_DNA.
DR EMBL; AL596130; CAI24487.1; -; Genomic_DNA.
DR EMBL; AL669902; CAI24487.1; JOINED; Genomic_DNA.
DR EMBL; AL669902; CAI35963.1; -; Genomic_DNA.
DR EMBL; AL596130; CAI35963.1; JOINED; Genomic_DNA.
DR EMBL; AL669902; CAI35964.1; -; Genomic_DNA.
DR EMBL; AL596130; CAI35964.1; JOINED; Genomic_DNA.
DR EMBL; CH466556; EDL15814.1; -; Genomic_DNA.
DR EMBL; BC090648; AAH90648.1; -; mRNA.
DR EMBL; BC141034; AAI41035.1; -; mRNA.
DR CCDS; CCDS25212.1; -. [Q924H5-1]
DR CCDS; CCDS79013.1; -. [Q924H5-2]
DR RefSeq; NP_001278369.1; NM_001291440.1. [Q924H5-2]
DR RefSeq; NP_444499.1; NM_053269.3. [Q924H5-1]
DR AlphaFoldDB; Q924H5; -.
DR SMR; Q924H5; -.
DR BioGRID; 227828; 4.
DR STRING; 10090.ENSMUSP00000064079; -.
DR PhosphoSitePlus; Q924H5; -.
DR EPD; Q924H5; -.
DR MaxQB; Q924H5; -.
DR PaxDb; Q924H5; -.
DR PRIDE; Q924H5; -.
DR ProteomicsDB; 301911; -. [Q924H5-1]
DR ProteomicsDB; 301912; -. [Q924H5-2]
DR Antibodypedia; 18441; 390 antibodies from 35 providers.
DR DNASU; 114714; -.
DR Ensembl; ENSMUST00000007790; ENSMUSP00000007790; ENSMUSG00000007646. [Q924H5-2]
DR Ensembl; ENSMUST00000067692; ENSMUSP00000064079; ENSMUSG00000007646. [Q924H5-1]
DR GeneID; 114714; -.
DR KEGG; mmu:114714; -.
DR UCSC; uc007ktp.2; mouse. [Q924H5-1]
DR UCSC; uc056ynv.1; mouse. [Q924H5-2]
DR CTD; 5889; -.
DR MGI; MGI:2150020; Rad51c.
DR VEuPathDB; HostDB:ENSMUSG00000007646; -.
DR eggNOG; KOG1434; Eukaryota.
DR GeneTree; ENSGT00940000156805; -.
DR HOGENOM; CLU_041732_1_1_1; -.
DR InParanoid; Q924H5; -.
DR OMA; RLILYWN; -.
DR OrthoDB; 1345899at2759; -.
DR PhylomeDB; Q924H5; -.
DR TreeFam; TF101220; -.
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 Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 114714; 22 hits in 109 CRISPR screens.
DR ChiTaRS; Rad51c; mouse.
DR PRO; PR:Q924H5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q924H5; protein.
DR Bgee; ENSMUSG00000007646; Expressed in secondary oocyte and 153 other tissues.
DR ExpressionAtlas; Q924H5; baseline and differential.
DR Genevisible; Q924H5; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0048476; C:Holliday junction resolvase complex; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0033063; C:Rad51B-Rad51C-Rad51D-XRCC2 complex; ISS:UniProtKB.
DR GO; GO:0033065; C:Rad51C-XRCC3 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:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IMP:MGI.
DR GO; GO:0000400; F:four-way junction DNA binding; ISO:MGI.
DR GO; GO:0006310; P:DNA recombination; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0007066; P:female meiosis sister chromatid cohesion; IMP:MGI.
DR GO; GO:0007141; P:male meiosis I; IMP:MGI.
DR GO; GO:0000707; P:meiotic DNA recombinase assembly; IBA:GO_Central.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0000722; P:telomere maintenance via recombination; IGI:BHF-UCL.
DR CDD; cd01123; Rad51_DMC1_radA; 1.
DR Gene3D; 3.40.50.300; -; 1.
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 SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50162; RECA_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..366
FT /note="DNA repair protein RAD51 homolog 3"
FT /id="PRO_0000401939"
FT REGION 1..117
FT /note="Required for Holliday junction resolution activity"
FT REGION 70..127
FT /note="Interaction with RAD51B, RAD51D and XRCC3"
FT REGION 343..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 356..360
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT BINDING 116..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43502"
FT VAR_SEQ 1..40
FT /note="MQRELVGYPLSPAVRGKLVAAGFQTAEDVLEVKPSELSKE -> MLYRVHLA
FT WLPSPRLRPLFLFLCSLSGYIRNVTRTSETRRQPYMKPVCGISSAAARPQ (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_040206"
FT CONFLICT 8
FT /note="Y -> F (in Ref. 3; CAQ51530/CAQ52015 and 5;
FT AAI41035)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="Q -> K (in Ref. 2; BAC36388)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 366 AA; 40675 MW; 8B110BE7738BFCC7 CRC64;
MQRELVGYPL SPAVRGKLVA AGFQTAEDVL EVKPSELSKE VGISKEEALE TLQILRRECL
TNKPRCAGTS VANEKCTALE LLEQEHTQGF IITFCSALDN ILGGGIPLMK TTEVCGVPGV
GKTQLCMQLA VDVQIPECFG GVAGEAVFID TEGSFMVDRV VSLATACIQH LHLIAGTHTE
EEHQKALKDF TLENILSHIY YFRCHDYTEL LAQVYLLPDF LSDHPKVQLV IIDGIAFPFR
HDLEDLSLRT RLLNGLAQQM ISLANNHRLA VILTNQMTTK IDKNQALLVP ALGESWGHAA
TIRLIFHWEQ KQRFATLYKS PSQKESTIPF QITPQGFRDA VVTAASSQTE SSLNFRKRSR
EPEEEC
