BRC2_CAEEL
ID BRC2_CAEEL Reviewed; 394 AA.
AC G5EG86;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=DNA repair protein brc-2 {ECO:0000305};
GN Name=brc-2 {ECO:0000312|WormBase:T07E3.5};
GN ORFNames=T07E3.5 {ECO:0000312|WormBase:T07E3.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000312|EMBL:AAR98640.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kohara Y., Shin-i T., Suzuki Y., Sugano S., Thierry-Mieg D.,
RA Thierry-Mieg J.;
RT "The Caenorhabditis elegans transcriptome project, a complementary view of
RT the genome.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH RAD-51, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 36-SER--ARG-42.
RX PubMed=15798199; DOI=10.1128/mcb.25.8.3127-3139.2005;
RA Martin J.S., Winkelmann N., Petalcorin M.I., McIlwraith M.J., Boulton S.J.;
RT "RAD-51-dependent and -independent roles of a Caenorhabditis elegans BRCA2-
RT related protein during DNA double-strand break repair.";
RL Mol. Cell. Biol. 25:3127-3139(2005).
RN [4] {ECO:0000305}
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF PHE-35 AND ILE-43.
RX PubMed=16843491; DOI=10.1016/j.jmb.2006.06.020;
RA Petalcorin M.I., Sandall J., Wigley D.B., Boulton S.J.;
RT "CeBRC-2 stimulates D-loop formation by RAD-51 and promotes DNA single-
RT strand annealing.";
RL J. Mol. Biol. 361:231-242(2006).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH RAD-51, AND DOMAIN.
RX PubMed=17483448; DOI=10.1073/pnas.0702805104;
RA Petalcorin M.I., Galkin V.E., Yu X., Egelman E.H., Boulton S.J.;
RT "Stabilization of RAD-51-DNA filaments via an interaction domain in
RT Caenorhabditis elegans BRCA2.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8299-8304(2007).
RN [6] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18779660;
RA Ko E., Lee J., Lee H.;
RT "Essential role of brc-2 in chromosome integrity of germ cells in C.
RT elegans.";
RL Mol. Cells 26:590-594(2008).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27761361; DOI=10.1002/2211-5463.12109;
RA Kwon M.S., Min J., Jeon H.Y., Hwang K., Kim C., Lee J., Joung J.G.,
RA Park W.Y., Lee H.;
RT "Paradoxical delay of senescence upon depletion of BRCA2 in telomerase-
RT deficient worms.";
RL FEBS Open Bio 6:1016-1024(2016).
CC -!- FUNCTION: Required for the homologous recombination repair of DNA
CC double strand breaks, thereby playing a role in chromosome integrity
CC (PubMed:15798199, PubMed:16843491). Acts by targeting rad-51 to sites
CC of DNA damage and stabilizing rad-51-DNA filaments by blocking ATP
CC hydrolysis catalyzed by rad-51 (PubMed:15798199, PubMed:16843491,
CC PubMed:17483448, PubMed:18779660). Promotes rad-51 mediated
CC displacement-loop (D-loop) formation during strand invasion between the
CC invading single-stranded DNA (ssDNA) and the homologous duplex DNA
CC (PubMed:16843491). Also functions independently of rad-51 in DNA
CC double-strand break (DSB) repair by promoting DNA single-strand
CC annealing (SSA) when the homologous recombination (HR) and non-
CC homologous end joining (NHEJ) pathways are compromised
CC (PubMed:15798199, PubMed:16843491). Binds selectively to single-
CC stranded (ssDNA) via its C-terminus (PubMed:15798199). Involved in
CC telomere maintenance and replicative senescence (PubMed:27761361).
CC {ECO:0000269|PubMed:15798199, ECO:0000269|PubMed:16843491,
CC ECO:0000269|PubMed:17483448, ECO:0000269|PubMed:18779660,
CC ECO:0000269|PubMed:27761361}.
CC -!- SUBUNIT: Interacts (via N-terminus) with rad-51; regulates rad-51
CC recruitment to sites of DNA double strand breaks (PubMed:15798199,
CC PubMed:17483448). {ECO:0000269|PubMed:15798199,
CC ECO:0000269|PubMed:17483448}.
CC -!- INTERACTION:
CC G5EG86; G5EGG8: rad-51; NbExp=3; IntAct=EBI-325989, EBI-2315986;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15798199}. Chromosome
CC {ECO:0000269|PubMed:15798199}. Note=Diffusely localized in the nucleus.
CC Recruited to sites of DNA damage upon induction of DNA double strand
CC breaks by ionizing radiation (IR) or in meiosis.
CC {ECO:0000269|PubMed:15798199}.
CC -!- TISSUE SPECIFICITY: Expressed in the germline, with highest expression
CC in cells undergoing oogenesis. {ECO:0000269|PubMed:15798199,
CC ECO:0000269|PubMed:18779660}.
CC -!- DOMAIN: The BRCA2 repeat-like region is required for rad-51 binding.
CC {ECO:0000269|PubMed:16843491, ECO:0000269|PubMed:17483448}.
CC -!- DISRUPTION PHENOTYPE: Mutant animals are egg-laying defective and
CC exhibit a reduced brood size and high embryonic lethality
CC (PubMed:15798199, PubMed:18779660). Impaired formation of rad-51 foci
CC and accumulation of rpa-1 foci in the meiotic region of the germline in
CC mutants either untreated or treated with ionizing radiation (IR),
CC indicating impaired DNA double strand break repair by homologous
CC recombination (PubMed:15798199, PubMed:18779660). Decompaction of
CC chromatin, chromosome aggregation and aberrant number of bivalent
CC chromosomes during meiosis (PubMed:15798199, PubMed:18779660). In a
CC telomerase trt-1 mutant background, RNAi-mediated knockdown leads to
CC telomere shortening in early generations, to telomere elongation in
CC late generations and to a delay in generational replicative senescence
CC (PubMed:27761361). {ECO:0000269|PubMed:15798199,
CC ECO:0000269|PubMed:18779660, ECO:0000269|PubMed:27761361}.
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DR EMBL; BX284603; CCD72025.1; -; Genomic_DNA.
DR EMBL; AY523518; AAR98640.1; -; mRNA.
DR PIR; A88492; A88492.
DR RefSeq; NP_498502.3; NM_066101.5.
DR AlphaFoldDB; G5EG86; -.
DR IntAct; G5EG86; 5.
DR STRING; 6239.T07E3.5; -.
DR EPD; G5EG86; -.
DR PaxDb; G5EG86; -.
DR PeptideAtlas; G5EG86; -.
DR EnsemblMetazoa; T07E3.5.1; T07E3.5.1; WBGene00020316.
DR GeneID; 175962; -.
DR KEGG; cel:CELE_T07E3.5; -.
DR CTD; 175962; -.
DR WormBase; T07E3.5; CE32718; WBGene00020316; brc-2.
DR eggNOG; ENOG502T7RB; Eukaryota.
DR HOGENOM; CLU_685589_0_0_1; -.
DR InParanoid; G5EG86; -.
DR OMA; ISMEPVF; -.
DR OrthoDB; 1722217at2759; -.
DR PRO; PR:G5EG86; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00020316; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:WormBase.
DR GO; GO:0006302; P:double-strand break repair; IMP:WormBase.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:WormBase.
DR GO; GO:0045002; P:double-strand break repair via single-strand annealing; IDA:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0000707; P:meiotic DNA recombinase assembly; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0032880; P:regulation of protein localization; IMP:WormBase.
DR GO; GO:0042148; P:strand invasion; IDA:WormBase.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Chromosome; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Meiosis; Nucleus; Reference proteome.
FT CHAIN 1..394
FT /note="DNA repair protein brc-2"
FT /id="PRO_0000441095"
FT REGION 1..60
FT /note="Interaction with rad-51"
FT /evidence="ECO:0000269|PubMed:17483448"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 28..62
FT /note="BRCA2 repeat-like region"
FT /evidence="ECO:0000305"
FT REGION 56..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..89
FT /note="Interaction with rad-51-DNA complexes"
FT /evidence="ECO:0000269|PubMed:17483448"
FT REGION 371..389
FT /note="Required for ssDNA binding"
FT /evidence="ECO:0000269|PubMed:15798199"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..135
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 35
FT /note="F->A: Abolishes interaction with rad-51, but binding
FT to ssDNA is retained. Loss of D-loop formation in the
FT presence of rad-51. Loss of inhibition of ATP hydrolysis by
FT rad-51."
FT /evidence="ECO:0000269|PubMed:16843491"
FT MUTAGEN 36..42
FT /note="Missing: Abolishes interaction with rad-51."
FT /evidence="ECO:0000269|PubMed:15798199"
FT MUTAGEN 43
FT /note="I->A: Abolishes interaction with rad-51, but binding
FT to ssDNA is retained. Loss of D-loop formation in the
FT presence of rad-51. Loss of inhibition of ATP hydrolysis by
FT rad-51."
FT /evidence="ECO:0000269|PubMed:16843491"
SQ SEQUENCE 394 AA; 44762 MW; E1B80474F2FE0451 CRC64;
MGDSSKKVKD SFDTISEPDS FDEPKGVPIS MEPVFSTAAG IRIDVKQESI DKSKKMLNSD
LKSKSSSKGG FSSPLVRKNN GSSAFVSPFR REGTSSTTTK RPASGGFEDF EAPPAKKSTS
SSSKKSKKHS KKEKKKEFKE IHADVLRVSR IYEKDKFRII LQESSSTPLI LATCSYNRGS
DIKFGDRIHV DAEVCKKSSS GDVTEIYIDR VLKNKENGAK SGIRRHSIAK KPFCIKPRFI
HELSDTKIKK TVVQVNLLDL NLDFYAGCSK CKHSLPEAAN QCEFCKDSQG KSELSMYSRV
RVMDFSGQMF INVTTKNMKK LLDLLGYEGF DNWFRFKDPQ ERQNYVFRPV MVEIEKSNDE
WECTDVAEVD WKDFGSYLKH KEDKKKRRSK KKHP
