ID   XRCC2_MOUSE             Reviewed;         278 AA.
AC   Q9CX47; O88730; Q9D5T1;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=DNA repair protein XRCC2;
DE   AltName: Full=X-ray repair cross-complementing protein 2;
GN   Name=Xrcc2;
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].
RC   STRAIN=L929; TISSUE=Testis;
RX   PubMed=9628903; DOI=10.1093/nar/26.13.3084;
RA   Cartwright R., Tambini C.E., Simpson P.J., Thacker J.;
RT   "The XRCC2 DNA repair gene from human and mouse encodes a novel member of
RT   the recA/RAD51 family.";
RL   Nucleic Acids Res. 26:3084-3089(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic 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 MRNA].
RC   TISSUE=Retina;
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   [4]
RP   MUTAGENESIS OF LEU-14.
RX   PubMed=30042186; DOI=10.1136/jmedgenet-2017-105145;
RA   Yang Y., Guo J., Dai L., Zhu Y., Hu H., Tan L., Chen W., Liang D., He J.,
RA   Tu M., Wang K., Wu L.;
RT   "XRCC2 mutation causes meiotic arrest, azoospermia and infertility.";
RL   J. Med. Genet. 55:628-636(2018).
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 RAD51 paralog protein complex
CC       BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA
CC       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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RAD51D. Part of the BCDX2 complex consisting of
CC       RAD51B, RAD51C, RAD51D and XRCC2; the complex has a ring-like structure
CC       arranged into a flat disk around a central channel. In the absence of
CC       DNA, the BCDX2 subcomplex XRCC2:RAD51D formed a multimeric ring
CC       structure; in the presence of single-stranded DNA it formed a
CC       filamentous structure with the ssDNA (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed at low level in somatic tissues and at
CC       high level in testis.
CC   -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily. {ECO:0000305}.
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DR   EMBL; Y17040; CAA76599.1; -; mRNA.
DR   EMBL; AK020192; BAB32023.1; -; mRNA.
DR   EMBL; AK014963; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC033417; AAH33417.1; -; mRNA.
DR   CCDS; CCDS19135.1; -.
DR   RefSeq; NP_065595.2; NM_020570.2.
DR   AlphaFoldDB; Q9CX47; -.
DR   SMR; Q9CX47; -.
DR   BioGRID; 208291; 7.
DR   STRING; 10090.ENSMUSP00000030773; -.
DR   PhosphoSitePlus; Q9CX47; -.
DR   EPD; Q9CX47; -.
DR   PaxDb; 10090-ENSMUSP00000030773; -.
DR   ProteomicsDB; 299723; -.
DR   Antibodypedia; 18833; 409 antibodies from 36 providers.
DR   DNASU; 57434; -.
DR   Ensembl; ENSMUST00000030773.12; ENSMUSP00000030773.8; ENSMUSG00000028933.12.
DR   GeneID; 57434; -.
DR   KEGG; mmu:57434; -.
DR   UCSC; uc008wta.1; mouse.
DR   AGR; MGI:1927345; -.
DR   CTD; 7516; -.
DR   MGI; MGI:1927345; Xrcc2.
DR   VEuPathDB; HostDB:ENSMUSG00000028933; -.
DR   eggNOG; KOG2859; Eukaryota.
DR   GeneTree; ENSGT00390000020445; -.
DR   HOGENOM; CLU_059815_1_0_1; -.
DR   InParanoid; Q9CX47; -.
DR   OMA; KHCLGRL; -.
DR   OrthoDB; 318445at2759; -.
DR   PhylomeDB; Q9CX47; -.
DR   TreeFam; TF101202; -.
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; 57434; 31 hits in 115 CRISPR screens.
DR   ChiTaRS; Xrcc2; mouse.
DR   PRO; PR:Q9CX47; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q9CX47; Protein.
DR   Bgee; ENSMUSG00000028933; Expressed in spermatocyte and 192 other cell types or tissues.
DR   ExpressionAtlas; Q9CX47; baseline and differential.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:InterPro.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0000400; F:four-way junction DNA binding; IEA:Ensembl.
DR   GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR   GO; GO:0006974; P:DNA damage response; IMP:MGI.
DR   GO; GO:0006281; P:DNA repair; ISO:MGI.
DR   GO; GO:0042148; P:DNA strand invasion; ISS:UniProtKB.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0035264; P:multicellular organism growth; IGI:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:MGI.
DR   GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR   GO; GO:0050769; P:positive regulation of neurogenesis; IMP:MGI.
DR   GO; GO:2000269; P:regulation of fibroblast apoptotic process; IGI:MGI.
DR   GO; GO:0010332; P:response to gamma radiation; IMP:MGI.
DR   GO; GO:0010165; P:response to X-ray; IMP:MGI.
DR   GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR   CDD; cd19490; XRCC2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   InterPro; IPR030547; XRCC2.
DR   PANTHER; PTHR46644; DNA REPAIR PROTEIN XRCC2; 1.
DR   PANTHER; PTHR46644:SF2; DNA REPAIR PROTEIN XRCC2; 1.
DR   Pfam; PF08423; Rad51; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50162; RECA_2; 1.
DR   Genevisible; Q9CX47; MM.
PE   1: Evidence at protein level;
KW   DNA damage; DNA recombination; DNA repair; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..278
FT                   /note="DNA repair protein XRCC2"
FT                   /id="PRO_0000122949"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43543"
FT   MUTAGEN         14
FT                   /note="L->P: Mutant male mice exhibit meiotic arrest,
FT                   azoospermia and infertility. Females exhibit infertility or
FT                   low reproductive capacity."
FT                   /evidence="ECO:0000269|PubMed:30042186"
SQ   SEQUENCE   278 AA;  31391 MW;  8E65467596E604FD CRC64;
     MCSDFRRAES GTELLARLEG RSSLKELEPN LFADEDSPVH GDIFEFHGPE GTGKTEMLYH
     LTARCILPKS EGGLQIEVLF IDTDYHFDML RLVTVLEHRL SQSSEEAMKL CLARLFLAYC
     SSSMQLLLTL HSLEALLCSR PSLCLLIVDS LSSFYWIDRV SGGESVALQE STLQKCSQLL
     ERLVTEYRLL LFATTQSLMQ KGSDSADGPS SSKHPCDGDM GYRAYLCKAW QRVVKHRVIF
     SRDDEAKSSR FSLVSRHLKS NSLKKHSFMV RESGVEFC
//