BRCA2_DROME
ID BRCA2_DROME Reviewed; 971 AA.
AC Q9W157; B2CPK7; B2CPK8; Q494G5; Q8MRU0;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Breast cancer type 2 susceptibility protein homolog {ECO:0000303|PubMed:17822964};
DE Short=dmbrca2 {ECO:0000303|PubMed:17822964};
GN Name=Brca2 {ECO:0000312|FlyBase:FBgn0050169}; ORFNames=CG30169;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:AAF47220.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF47220.3}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAZ66318.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAZ66318.1}; TISSUE=Larva, and Pupae;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:ACB30271.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 234-278, AND VARIANT LYS-242.
RC STRAIN=Oregon-R {ECO:0000312|EMBL:ACB30270.1}, and
RC Zimbabwe30 {ECO:0000312|EMBL:ACB30271.1};
RA Barnwell C.V., Kommaraju K.R., Noor M.A.;
RT "Disruption of Drosophila melanogaster dmbrca2 (CG30169) affects rates of
RT female meiotic crossing over.";
RL Dros. Info. Service 91:1-4(2008).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAM51132.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 276-971.
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SPN-A, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17822964; DOI=10.1016/j.dnarep.2007.07.013;
RA Brough R., Wei D., Leulier S., Lord C.J., Rong Y.S., Ashworth A.;
RT "Functional analysis of Drosophila melanogaster BRCA2 in DNA repair.";
RL DNA Repair 7:10-19(2008).
RN [7] {ECO:0000305}
RP FUNCTION, INTERACTION WITH RAD9, AND DISRUPTION PHENOTYPE.
RX PubMed=18266476; DOI=10.1371/journal.pgen.0040031;
RA Klovstad M., Abdu U., Schupbach T.;
RT "Drosophila brca2 is required for mitotic and meiotic DNA repair and
RT efficient activation of the meiotic recombination checkpoint.";
RL PLoS Genet. 4:E31-E31(2008).
RN [8]
RP INTERACTION WITH CYCG.
RX PubMed=22976300; DOI=10.1242/jcs.113902;
RA Nagel A.C., Fischer P., Szawinski J., La Rosa M.K., Preiss A.;
RT "Cyclin G is involved in meiotic recombination repair in Drosophila
RT melanogaster.";
RL J. Cell Sci. 125:5555-5563(2012).
CC -!- FUNCTION: Involved in and required for double-strand break repair by
CC meiotic and mitotic homologous recombination. During meiosis, has a
CC dual role in the repair of meiotic double-stranded breaks and the
CC efficient activation of the meiotic recombination checkpoint.
CC {ECO:0000269|PubMed:17822964, ECO:0000269|PubMed:18266476}.
CC -!- SUBUNIT: Interacts with Rad9 (PubMed:18266476). Interacts with spn-
CC A/Rad51 (PubMed:17822964). Interacts with cyclin CycG
CC (PubMed:22976300). {ECO:0000269|PubMed:17822964,
CC ECO:0000269|PubMed:18266476, ECO:0000269|PubMed:22976300}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17822964}. Note=Brca2
CC and spn-A/Rad51 become recruited to nuclear foci after DNA damage.
CC {ECO:0000269|PubMed:17822964}.
CC -!- DISRUPTION PHENOTYPE: Induced sensitivity to DNA damage induced by
CC irradiation or treatment with hydroxyurea/ Repair by homologous
CC recombination is dramatically decreased. Instead, large flanking
CC deletions are formed, and repair by the non-conservative single-strand
CC annealing pathway predominates. {ECO:0000269|PubMed:17822964,
CC ECO:0000269|PubMed:18266476}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM51132.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE013599; AAF47220.3; -; Genomic_DNA.
DR EMBL; BT023811; AAZ66318.1; -; mRNA.
DR EMBL; EU541213; ACB30270.1; -; Genomic_DNA.
DR EMBL; EU541214; ACB30271.1; -; Genomic_DNA.
DR EMBL; AY119272; AAM51132.1; ALT_INIT; mRNA.
DR RefSeq; NP_611925.2; NM_138081.4.
DR AlphaFoldDB; Q9W157; -.
DR BioGRID; 63488; 25.
DR IntAct; Q9W157; 8.
DR MINT; Q9W157; -.
DR STRING; 7227.FBpp0072209; -.
DR PaxDb; Q9W157; -.
DR DNASU; 37916; -.
DR EnsemblMetazoa; FBtr0072302; FBpp0072209; FBgn0050169.
DR GeneID; 37916; -.
DR KEGG; dme:Dmel_CG30169; -.
DR UCSC; CG30169-RA; d. melanogaster.
DR CTD; 675; -.
DR FlyBase; FBgn0050169; Brca2.
DR VEuPathDB; VectorBase:FBgn0050169; -.
DR eggNOG; KOG4751; Eukaryota.
DR HOGENOM; CLU_315529_0_0_1; -.
DR InParanoid; Q9W157; -.
DR OMA; ECFSEDM; -.
DR OrthoDB; 807034at2759; -.
DR PhylomeDB; Q9W157; -.
DR SignaLink; Q9W157; -.
DR BioGRID-ORCS; 37916; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37916; -.
DR PRO; PR:Q9W157; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0050169; Expressed in ovary and 23 other tissues.
DR Genevisible; Q9W157; DM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IDA:FlyBase.
DR GO; GO:0043150; P:DNA synthesis involved in double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:FlyBase.
DR GO; GO:0010778; P:meiotic DNA repair synthesis involved in reciprocal meiotic recombination; IMP:UniProtKB.
DR GO; GO:0051598; P:meiotic recombination checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:1901563; P:response to camptothecin; IMP:FlyBase.
DR InterPro; IPR015525; BRCA2.
DR InterPro; IPR002093; BRCA2_repeat.
DR PANTHER; PTHR11289; PTHR11289; 2.
DR PROSITE; PS50138; BRCA2_REPEAT; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; DNA damage; DNA repair; Meiosis; Mitosis;
KW Nucleus; Reference proteome; Repeat.
FT CHAIN 1..971
FT /note="Breast cancer type 2 susceptibility protein homolog"
FT /id="PRO_0000392916"
FT REPEAT 570..604
FT /note="BRCA2 1"
FT /evidence="ECO:0000255"
FT REPEAT 671..705
FT /note="BRCA2 2"
FT /evidence="ECO:0000255"
FT REPEAT 746..780
FT /note="BRCA2 3"
FT /evidence="ECO:0000255"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 242
FT /note="E -> K (in strain: Zimbabwe30)"
FT /evidence="ECO:0000269|Ref.4"
FT CONFLICT 502
FT /note="F -> S (in Ref. 5; AAM51132)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="D -> E (in Ref. 5; AAM51132)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="K -> Y (in Ref. 5; AAM51132)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="V -> D (in Ref. 5; AAM51132)"
FT /evidence="ECO:0000305"
FT CONFLICT 791
FT /note="T -> I (in Ref. 5; AAM51132)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 971 AA; 108649 MW; 9232DE2A667672CE CRC64;
MDQNGASGSH PNRLSQGRGA HARERGATVS AAANRSNIID EMAKICEADR QTFAIARRTR
GHERLAVDNS DFVAVEDLIL SYAEPTPEDQ VEMIMSDFCS SPTYAEDEDE PSHESEPWFR
FRNKRIRTYS RKRDPKSHKA VQNEKRRGSS GLSVQRDLNT SFTSMACDFD ASSQKIHEVL
LNLSQYFSAT ATASGPTPVP SQIDLPTEAR QDSGDECFNA ELENLRDDLL QSGFTFEASF
YENEHEQEGP GTMADTIYGD SMQSVPTTRL RLESGKRNVW SDADSTLKKA DVEIAENKKL
LMGQTQAKNV DIEENTNFIL EGIPLSEWLT PMELPEISKD VIKHIPDKKL KLEPSSQKEQ
KSSKDSNASK VRGASKQSCD INTKNEGTTI LDQPNAAEQE NLLNDGELLE EFLFNDWQPM
QCSNGPSTSK NAIQGPKENI NSINLDDKEQ PEKQTPNKSQ TISSHQLNGI RKKSFKFIEV
SEEMKIKGEE FVDKVVSGLY HFSHKCNLRT EEYSDNHSQV MESTQCAEFK SAPSKPIEIL
DGKETYNAIA KVDVGEINGK FSPLNNDTIA EPEFCGFRTA SNKAIPISEK MKIKTAEFMA
EFQSKETIQQ NDYLVHQPND KPTSVGLDTA LKRSIESSEE MRSKASKLVV VDTTMREPHQ
PTLDPVCRDL NESQFFGFRT ASNKAIEITE AMEKRGAMFL AQSKATDQLN GWQPSDFPDV
LPTSPNNEIH SINVENNKAV NTKTVSETEF FGFRTASNKG IVISENTKIK VAQFMSEFQA
ADASTDSNQP TVISEESRNI DAKFVDEAAA EDSANKPTFC NVQSLKNTSD IEHFKHDFFV
EHSAKEEHPL CSQPLVRTPR RSQEIHSSLS QLAGKSPLDQ ATKKSVIARR NLLSLKRKRK
IILSTETSTS CALPTMERFA PKPSSTSTPL ADRDLNRSKD CTKNRQDAED MSPICMQPKK
SRRLGLSRSR Y