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DNA repair protein RAD51 homolog 3 (R51H3) (RAD51 homolog C) (RAD51-like protein 2)

 RA51C_MOUSE             Reviewed;         366 AA.
Q924H5; B2KGK7; Q5SX32; Q8C653;
30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
12-SEP-2018, entry version 134.
RecName: Full=DNA repair protein RAD51 homolog 3;
Short=R51H3;
AltName: Full=RAD51 homolog C;
AltName: Full=RAD51-like protein 2;
Name=Rad51c; Synonyms=Rad51l2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
STRAIN=C57BL/6J;
PubMed=11410366; DOI=10.1016/S0378-1119(01)00498-X;
Leasure C.S., Chandler J., Gilbert D.J., Householder D.B.,
Stephens R., Copeland N.G., Jenkins N.A., Sharan S.K.;
"Sequence, chromosomal location and expression analysis of the murine
homologue of human RAD51L2/RAD51C.";
Gene 271:59-67(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Head;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION.
PubMed=20471405; DOI=10.1016/j.mrfmmm.2010.05.001;
Smeenk G., de Groot A.J., Romeijn R.J., van Buul P.P.,
Zdzienicka M.Z., Mullenders L.H., Pastink A., Godthelp B.C.;
"Rad51C is essential for embryonic development and haploinsufficiency
causes increased DNA damage sensitivity and genomic instability.";
Mutat. Res. 689:50-58(2010).
-!- FUNCTION: Essential for the homologous recombination (HR) pathway
of DNA repair. Involved in the homologous recombination repair
(HRR) pathway of double-stranded DNA breaks arising during DNA
replication or induced by DNA-damaging agents. Part of the RAD21
paralog protein complexes BCDX2 and CX3 which act at different
stages of the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage,
BCDX2 seems to act downstream of BRCA2 recruitment and upstream of
RAD51 recruitment; CX3 seems to act downstream of RAD51
recruitment; both complexes bind predominantly to the intersection
of the four duplex arms of the Holliday junction (HJ) and to
junction of replication forks. The BCDX2 complex was originally
reported to bind single-stranded DNA, single-stranded gaps in
duplex DNA and specifically to nicks in duplex DNA. The BCDX2
subcomplex RAD51B:RAD51C exhibits single-stranded DNA-dependent
ATPase activity suggesting an involvement in early stages of the
HR pathway. Involved in RAD51 foci formation in response to DNA
damage suggesting an involvement in early stages of HR probably in
the invasion step. Has an early function in DNA repair in
facilitating phosphorylation of the checkpoint kinase CHEK2 and
thereby transduction of the damage signal, leading to cell cycle
arrest and HR activation. Participates in branch migration and HJ
resolution and thus is important for processing HR intermediates
late in the DNA repair process; the function may be linked to the
CX3 complex. Part of a PALB2-scaffolded HR complex containing
BRCA2 and which is thought to play a role in DNA repair by HR.
Protects RAD51 from ubiquitin-mediated degradation that is
enhanced following DNA damage. Plays a role in regulating
mitochondrial DNA copy number under conditions of oxidative stress
in the presence of RAD51 and XRCC3. Contributes to DNA cross-link
resistance, sister chromatid cohesion and genomic stability.
Involved in maintaining centrosome number in mitosis.
{ECO:0000269|PubMed:20471405}.
-!- SUBUNIT: Part of the Rad21 paralog protein complexes BCDX2 and
CX3; the complexes have a ring-like structure arranged into a flat
disc around a central channel. The BCDX2 complex consits of
RAD51B, RAD51C, RAD51D and XRCC2; the CX3 complex consists of
RAD51C and XRCC3. The BCDX2 subcomplex RAD51B:RAD51C interacts
with RAD51. Interacts with SWSAP1; involved in homologous
recombination repair. Interacts directly with PALB2 which may
serve as a scaffold for a HR complex containing PALB2, BRCA2,
RAD51C, RAD51 and XRCC3 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
{ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
Mitochondrion {ECO:0000250}. Note=DNA damage induces an increase
in nuclear levels. Accumulates in DNA damage induced nuclear foci
or RAD51C foci which is formed during the S or G2 phase of cell
cycle. Accumulation at DNA lesions requires the presence of
NBN/NBS1, ATM and RPA (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q924H5-1; Sequence=Displayed;
Name=2;
IsoId=Q924H5-2; Sequence=VSP_040206;
-!- TISSUE SPECIFICITY: Expressed in the heart, brain, spleen, lung,
liver, kidney and testis but not detected in skeletal muscle.
{ECO:0000269|PubMed:11410366}.
-!- DEVELOPMENTAL STAGE: Expressed in embryos at various developmental
stages. The expression is found to be higher between 11 and 15
days of gestation compared to day 7 or 17.
{ECO:0000269|PubMed:11410366}.
-!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF324883; AAK58420.1; -; Genomic_DNA.
EMBL; AK076551; BAC36388.1; -; mRNA.
EMBL; CU406989; CAQ51530.1; -; Genomic_DNA.
EMBL; CU406969; CAQ51530.1; JOINED; Genomic_DNA.
EMBL; CU406989; CAQ51531.1; -; Genomic_DNA.
EMBL; CU406969; CAQ51531.1; JOINED; Genomic_DNA.
EMBL; CU406969; CAQ52016.1; -; Genomic_DNA.
EMBL; CU406989; CAQ52016.1; JOINED; Genomic_DNA.
EMBL; CU406969; CAQ52015.1; -; Genomic_DNA.
EMBL; CU406989; CAQ52015.1; JOINED; Genomic_DNA.
EMBL; AL596130; CAI24486.1; -; Genomic_DNA.
EMBL; AL669902; CAI24486.1; JOINED; Genomic_DNA.
EMBL; AL596130; CAI24487.1; -; Genomic_DNA.
EMBL; AL669902; CAI24487.1; JOINED; Genomic_DNA.
EMBL; AL669902; CAI35963.1; -; Genomic_DNA.
EMBL; AL596130; CAI35963.1; JOINED; Genomic_DNA.
EMBL; AL669902; CAI35964.1; -; Genomic_DNA.
EMBL; AL596130; CAI35964.1; JOINED; Genomic_DNA.
EMBL; CH466556; EDL15814.1; -; Genomic_DNA.
EMBL; BC090648; AAH90648.1; -; mRNA.
EMBL; BC141034; AAI41035.1; -; mRNA.
CCDS; CCDS25212.1; -. [Q924H5-1]
CCDS; CCDS79013.1; -. [Q924H5-2]
RefSeq; NP_001278369.1; NM_001291440.1. [Q924H5-2]
RefSeq; NP_444499.1; NM_053269.3. [Q924H5-1]
UniGene; Mm.37376; -.
ProteinModelPortal; Q924H5; -.
SMR; Q924H5; -.
BioGrid; 227828; 1.
STRING; 10090.ENSMUSP00000064079; -.
PhosphoSitePlus; Q924H5; -.
EPD; Q924H5; -.
PaxDb; Q924H5; -.
PRIDE; Q924H5; -.
Ensembl; ENSMUST00000007790; ENSMUSP00000007790; ENSMUSG00000007646. [Q924H5-2]
Ensembl; ENSMUST00000067692; ENSMUSP00000064079; ENSMUSG00000007646. [Q924H5-1]
GeneID; 114714; -.
KEGG; mmu:114714; -.
UCSC; uc007ktp.2; mouse. [Q924H5-1]
UCSC; uc056ynv.1; mouse. [Q924H5-2]
CTD; 5889; -.
MGI; MGI:2150020; Rad51c.
eggNOG; KOG1434; Eukaryota.
eggNOG; COG0468; LUCA.
GeneTree; ENSGT00860000133731; -.
HOGENOM; HOG000227426; -.
HOVERGEN; HBG055764; -.
InParanoid; Q924H5; -.
KO; K10870; -.
OMA; HWDQKQR; -.
OrthoDB; EOG091G0Q7R; -.
PhylomeDB; Q924H5; -.
TreeFam; TF101220; -.
Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
Reactome; R-MMU-5693579; Homologous DNA Pairing and Strand Exchange.
Reactome; R-MMU-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
PRO; PR:Q924H5; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000007646; Expressed in 143 organ(s), highest expression level in secondary oocyte.
ExpressionAtlas; Q924H5; baseline and differential.
Genevisible; Q924H5; MM.
GO; GO:0030054; C:cell junction; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0048476; C:Holliday junction resolvase complex; IC:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0033063; C:Rad51B-Rad51C-Rad51D-XRCC2 complex; ISS:UniProtKB.
GO; GO:0033065; C:Rad51C-XRCC3 complex; ISS:UniProtKB.
GO; GO:0005657; C:replication fork; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IMP:MGI.
GO; GO:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central.
GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
GO; GO:0000400; F:four-way junction DNA binding; IBA:GO_Central.
GO; GO:0000150; F:recombinase activity; IBA:GO_Central.
GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
GO; GO:0006310; P:DNA recombination; ISO:MGI.
GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
GO; GO:0007066; P:female meiosis sister chromatid cohesion; IMP:MGI.
GO; GO:0007141; P:male meiosis I; IMP:MGI.
GO; GO:0000707; P:meiotic DNA recombinase assembly; IBA:GO_Central.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0007131; P:reciprocal meiotic recombination; IMP:MGI.
GO; GO:0010212; P:response to ionizing radiation; IBA:GO_Central.
GO; GO:0007283; P:spermatogenesis; IMP:MGI.
GO; GO:0042148; P:strand invasion; IBA:GO_Central.
GO; GO:0000722; P:telomere maintenance via recombination; IGI:BHF-UCL.
CDD; cd01123; Rad51_DMC1_radA; 1.
InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
InterPro; IPR016467; DNA_recomb/repair_RecA-like.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR033925; Rad51_DMC1_RadA.
InterPro; IPR020588; RecA_ATP-bd.
Pfam; PF08423; Rad51; 1.
PIRSF; PIRSF005856; Rad51; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50162; RECA_2; 1.
2: Evidence at transcript level;
Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
DNA damage; DNA recombination; DNA repair; DNA-binding; Mitochondrion;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 366 DNA repair protein RAD51 homolog 3.
/FTId=PRO_0000401939.
NP_BIND 116 123 ATP. {ECO:0000255}.
REGION 1 117 Required for Holliday junction resolution
activity.
REGION 70 127 Interaction with RAD51B, RAD51D and
XRCC3.
MOTIF 356 360 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000250|UniProtKB:O43502}.
VAR_SEQ 1 40 MQRELVGYPLSPAVRGKLVAAGFQTAEDVLEVKPSELSKE
-> MLYRVHLAWLPSPRLRPLFLFLCSLSGYIRNVTRTSET
RRQPYMKPVCGISSAAARPQ (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_040206.
CONFLICT 8 8 Y -> F (in Ref. 3; CAQ51530/CAQ52015 and
5; AAI41035). {ECO:0000305}.
CONFLICT 228 228 Q -> K (in Ref. 2; BAC36388).
{ECO:0000305}.
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


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