XRCC3_MOUSE
ID XRCC3_MOUSE Reviewed; 349 AA.
AC Q9CXE6;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=DNA repair protein XRCC3;
DE AltName: Full=X-ray repair cross-complementing protein 3;
GN Name=Xrcc3;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic liver;
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).
CC -!- FUNCTION: Involved in the homologous recombination repair (HRR) pathway
CC of double-stranded DNA, thought to repair chromosomal fragmentation,
CC translocations and deletions. Part of the RAD21 paralog protein complex
CC CX3 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA
CC damage, CX3 acts downstream of RAD51 recruitment; the complex binds
CC predominantly to the intersection of the four duplex arms of the
CC Holliday junction (HJ) and to junctions of replication forks. Involved
CC in HJ resolution and thus in processing HR intermediates late in the
CC DNA repair process; the function may be linked to the CX3 complex and
CC seems to involve GEN1 during mitotic cell cycle progression. Part of a
CC PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is
CC thought to play a role in DNA repair by HR. Plays a role in regulating
CC mitochondrial DNA copy number under conditions of oxidative stress in
CC the presence of RAD51 and RAD51C (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RAD51C and RAD51. Part of the CX3 complex
CC consisting of RAD51C and XRCC3; the complex has a ring-like structure
CC arranged into a flat disc around a central channel; CX3 can interact
CC with RAD51 in vitro. Forms a complex with FANCD2, BRCA2 and
CC phosphorylated FANCG. Interacts with SWSAP1 and ZSWIM7; involved in
CC homologous recombination repair. Interacts directly with PALB2 which
CC may serve as a scaffold for a HR complex containing PALB2, BRCA2,
CC RAD51C, RAD51 and XRCC3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cytoplasm, perinuclear region {ECO:0000250}. Mitochondrion matrix
CC {ECO:0000250}. Note=Accumulates in discrete nuclear foci prior to DNA
CC damage, and these foci persist throughout the time course of DNA
CC repair. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily. {ECO:0000305}.
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DR EMBL; AK014491; BAB29391.1; -; mRNA.
DR CCDS; CCDS26187.1; -.
DR RefSeq; NP_083151.1; NM_028875.3.
DR AlphaFoldDB; Q9CXE6; -.
DR SMR; Q9CXE6; -.
DR BioGRID; 216673; 5.
DR STRING; 10090.ENSMUSP00000021715; -.
DR iPTMnet; Q9CXE6; -.
DR PhosphoSitePlus; Q9CXE6; -.
DR EPD; Q9CXE6; -.
DR PaxDb; Q9CXE6; -.
DR PRIDE; Q9CXE6; -.
DR ProteomicsDB; 297655; -.
DR Antibodypedia; 14778; 605 antibodies from 35 providers.
DR DNASU; 74335; -.
DR Ensembl; ENSMUST00000021715; ENSMUSP00000021715; ENSMUSG00000021287.
DR GeneID; 74335; -.
DR KEGG; mmu:74335; -.
DR UCSC; uc007pdz.1; mouse.
DR CTD; 7517; -.
DR MGI; MGI:1921585; Xrcc3.
DR VEuPathDB; HostDB:ENSMUSG00000021287; -.
DR eggNOG; KOG1564; Eukaryota.
DR GeneTree; ENSGT00930000151053; -.
DR InParanoid; Q9CXE6; -.
DR OMA; PCLGLQW; -.
DR OrthoDB; 1341207at2759; -.
DR PhylomeDB; Q9CXE6; -.
DR TreeFam; TF101203; -.
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 BioGRID-ORCS; 74335; 30 hits in 109 CRISPR screens.
DR ChiTaRS; Xrcc3; mouse.
DR PRO; PR:Q9CXE6; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9CXE6; protein.
DR Bgee; ENSMUSG00000021287; Expressed in yolk sac and 205 other tissues.
DR ExpressionAtlas; Q9CXE6; baseline and differential.
DR Genevisible; Q9CXE6; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; 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; ISO:MGI.
DR GO; GO:0000400; F:four-way junction DNA binding; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; ISO:MGI.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IBA:GO_Central.
DR GO; GO:0036297; P:interstrand cross-link repair; ISO:MGI.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; ISS:UniProtKB.
DR GO; GO:0010824; P:regulation of centrosome duplication; ISS:UniProtKB.
DR GO; GO:0071140; P:resolution of mitotic recombination intermediates; ISS:UniProtKB.
DR GO; GO:0010033; P:response to organic substance; IEA:Ensembl.
DR GO; GO:0090656; P:t-circle formation; ISO:MGI.
DR GO; GO:0000722; P:telomere maintenance via recombination; ISO:MGI.
DR GO; GO:0090737; P:telomere maintenance via telomere trimming; ISO:MGI.
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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; DNA damage; DNA recombination;
KW DNA repair; DNA-binding; Mitochondrion; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..349
FT /note="DNA repair protein XRCC3"
FT /id="PRO_0000122952"
FT BINDING 107..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O43542"
SQ SEQUENCE 349 AA; 38446 MW; 15E5AFBBDEB9AAEB CRC64;
MDLDQLDLNP RITAAVKRGR LKSVKEILCY SGPDLQRLTG LPSHDVQCLL RAASLHLRGS
RVLSALHLFQ QKESFPEQHQ RLSLGCPVLD QFLGGGLPLE GITGLAGCSS AGKTQLALQL
CLAVQFPRQY GGLEAGAVYI CTEDAFPSKR LWQLIAQQRR LRTDAPEELI EKIRFSNHIF
IEHAADVDTL LECVSKKVPI LLSRGMARLV VVDSIAAPFR CEFHLQASAI RAKLLLSLGA
TLRRLSSTFR SPVLCINQVT DMVEDQQSVS RSLGASEERL SPALGITWAN QLLMRLMVDR
THEDDVTTGL PRSPVRTLRV LFAPHLPLSS CCYTVSGEGI RGMPGTQSY
