RA51C_CRIGR
ID RA51C_CRIGR Reviewed; 366 AA.
AC Q8R2J9; Q8VDE9;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 90.
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 Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=11912211; DOI=10.1074/jbc.m201402200;
RA French C.A., Masson J.Y., Griffin C.S., O'Regan P., West S.C., Thacker J.;
RT "Role of mammalian RAD51L2 (RAD51C) in recombination and genetic
RT stability.";
RL J. Biol. Chem. 277:19322-19330(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-349 (ISOFORM 1), IDENTIFICATION OF ISOFORM
RP 2, AND FUNCTION.
RC TISSUE=Lung;
RX PubMed=12000837; DOI=10.1093/nar/30.10.2172;
RA Godthelp B.C., Wiegant W.W., van Duijn-Goedhart A., Scharer O.D.,
RA van Buul P.P.W., Kanaar R., Zdzienicka M.Z.;
RT "Mammalian Rad51C contributes to DNA cross-link resistance, sister
RT chromatid cohesion and genomic stability.";
RL Nucleic Acids Res. 30:2172-2182(2002).
RN [3]
RP FUNCTION.
RX PubMed=17268176; DOI=10.1159/000097416;
RA Renglin Lindh A., Schultz N., Saleh-Gohari N., Helleday T.;
RT "RAD51C (RAD51L2) is involved in maintaining centrosome number in
RT mitosis.";
RL Cytogenet. Genome Res. 116:38-45(2007).
RN [4]
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).
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:11912211, ECO:0000269|PubMed:12000837,
CC ECO:0000269|PubMed:17268176, 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. The BCDX2 complex consits of RAD51B, RAD51C, RAD51D
CC and XRCC2; the CX3 complex consists of RAD51C and XRCC3. The BCDX2
CC subcomplex RAD51B:RAD51C interacts with RAD51. Interacts with SWSAP1;
CC involved in homologous recombination repair. Interacts directly with
CC PALB2 which may serve as a scaffold for a HR complex containing PALB2,
CC BRCA2, RAD51C, RAD51 and XRCC3. Interacts with HELQ.
CC {ECO:0000250|UniProtKB:O43502}.
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=Q8R2J9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R2J9-2; Sequence=VSP_040285;
CC -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily. {ECO:0000305}.
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DR EMBL; AJ413202; CAC88355.1; -; mRNA.
DR EMBL; AJ428572; CAD21699.1; -; mRNA.
DR RefSeq; NP_001231005.1; NM_001244076.1. [Q8R2J9-1]
DR RefSeq; XP_007642544.1; XM_007644354.2. [Q8R2J9-1]
DR RefSeq; XP_007642545.1; XM_007644355.2. [Q8R2J9-1]
DR RefSeq; XP_007642546.1; XM_007644356.2. [Q8R2J9-1]
DR AlphaFoldDB; Q8R2J9; -.
DR SMR; Q8R2J9; -.
DR STRING; 10029.NP_001231005.1; -.
DR Ensembl; ENSCGRT00001010694; ENSCGRP00001006776; ENSCGRG00001009215. [Q8R2J9-1]
DR GeneID; 100689078; -.
DR KEGG; cge:100689078; -.
DR CTD; 5889; -.
DR eggNOG; KOG1434; Eukaryota.
DR GeneTree; ENSGT00940000156805; -.
DR OMA; RLILYWN; -.
DR GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0048476; C:Holliday junction resolvase complex; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:0000400; F:four-way junction DNA binding; IEA:Ensembl.
DR GO; GO:0006310; P:DNA recombination; ISS:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:0007141; P:male meiosis I; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0007062; P:sister chromatid cohesion; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0000722; P:telomere maintenance via recombination; IEA:Ensembl.
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 Alternative splicing; ATP-binding; Cytoplasm; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein.
FT CHAIN 1..366
FT /note="DNA repair protein RAD51 homolog 3"
FT /id="PRO_0000402422"
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 338..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 COMPBIAS 338..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 227..270
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040285"
SQ SEQUENCE 366 AA; 40381 MW; 150835C21F8619FA CRC64;
MQRELVSFPL SPTVRVKLVA AGFQTAEDVL GVKPSELSKE VGISKEEALE TLQIVRRESL
TDKPRCAGAS VAGKKYTALE LLEQEHTQGF IITFCSALDN ILGGGIPLMK TTEVCGVPGV
GKTQLCMQLA VDVQIPECFG GVAGEAVFID TEGSFMVDRV VTLANACIQH LHLIAGTHKD
EEHQKALEGF TLENILSHIY YFRCHDYTEL LAQVYLLPDF LSNHSKVQLV IIDGIALPFR
HDLDDLSLRT RLLNGLAQQM ISLANNHRLA VILTNQMTTK IDKNQALLVP ALGESWGHAA
TIRLIFHWEQ KQRFATLYKS PSQKESTIPF QITPQGFRDA AVTASSSQTE GSSNLRKRSR
EPEEGC
