ID BRC2A_ARATH Reviewed; 1151 AA.
AC Q7Y1C5; O81303; Q9M164;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 27-NOV-2024, entry version 136.
DE RecName: Full=Protein BREAST CANCER SUSCEPTIBILITY 2 homolog A {ECO:0000303|PubMed:16415210};
DE Short=AtBRCA2A {ECO:0000303|PubMed:16415210};
GN Name=BRCA2A {ECO:0000303|PubMed:16415210};
GN Synonyms=BRCA5(IV) {ECO:0000303|PubMed:15014444};
GN OrderedLocusNames=At4g00020/At4g00010 {ECO:0000312|Araport:AT4G00020};
GN ORFNames=F6N15.14/F6N15.15 {ECO:0000312|EMBL:CAB80759.1,
GN ECO:0000312|EMBL:CAB80760.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RAD51 AND DMC1, AND
RP TISSUE SPECIFICITY.
RX PubMed=15014444; DOI=10.1038/sj.emboj.7600146;
RA Siaud N., Dray E., Gy I., Gerard E., Takvorian N., Doutriaux M.P.;
RT "Brca2 is involved in meiosis in Arabidopsis thaliana as suggested by its
RT interaction with Dmc1.";
RL EMBO J. 23:1392-1401(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP INTERACTION WITH RAD51; DMC1 AND DSS1(I).
RX PubMed=16415210; DOI=10.1104/pp.105.075838;
RA Dray E., Siaud N., Dubois E., Doutriaux M.P.;
RT "Interaction between Arabidopsis Brca2 and its partners Rad51, Dmc1, and
RT Dss1.";
RL Plant Physiol. 140:1059-1069(2006).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22039535; DOI=10.1371/journal.pone.0026696;
RA Dumont M., Massot S., Doutriaux M.P., Gratias A.;
RT "Characterization of Brca2-deficient plants excludes the role of NHEJ and
RT SSA in the meiotic chromosomal defect phenotype.";
RL PLoS ONE 6:E26696-E26696(2011).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22077663; DOI=10.1111/j.1469-8137.2011.03947.x;
RA Seeliger K., Dukowic-Schulze S., Wurz-Wildersinn R., Pacher M., Puchta H.;
RT "BRCA2 is a mediator of RAD51- and DMC1-facilitated homologous
RT recombination in Arabidopsis thaliana.";
RL New Phytol. 193:364-375(2012).
CC -!- FUNCTION: Involved in double-strand break repair and/or homologous
CC recombination by mediating RAD51- and DMC1-facilitated DNA repair.
CC Plays an essential role in both somatic and meiotic homologous
CC recombination. Is crucial for the formation of RAD51 and DMC1 foci
CC during male meiotic homologous recombination in prophase I.
CC {ECO:0000269|PubMed:15014444, ECO:0000269|PubMed:22039535,
CC ECO:0000269|PubMed:22077663}.
CC -!- SUBUNIT: Interacts with RAD51 and DMC1 (PubMed:15014444,
CC PubMed:16415210). Interacts with DSS1(I) (PubMed:16415210).
CC {ECO:0000269|PubMed:15014444, ECO:0000269|PubMed:16415210}.
CC -!- INTERACTION:
CC Q7Y1C5; Q39009: DMC1; NbExp=4; IntAct=EBI-307680, EBI-307715;
CC Q7Y1C5; Q9XIR8: DSS1(I); NbExp=2; IntAct=EBI-307680, EBI-931045;
CC Q7Y1C5; P94102: RAD51; NbExp=5; IntAct=EBI-307680, EBI-307687;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Name=1;
CC IsoId=Q7Y1C5-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in flower buds.
CC {ECO:0000269|PubMed:15014444}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutants brca2a and brca2b are sterile due to
CC aberrant chromosome aggregates, chromosomal fragmentation and
CC missegregation during meiosis. {ECO:0000269|PubMed:22039535,
CC ECO:0000269|PubMed:22077663}.
CC -!- MISCELLANEOUS: [Isoform 1]: A number of isoforms are produced.
CC According to EST sequences.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC19315.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g00010 and At4g00020.; Evidence={ECO:0000305};
CC Sequence=CAB80759.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80760.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g00010 and At4g00020.; Evidence={ECO:0000305};
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DR EMBL; AF069299; AAC19315.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161471; CAB80759.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161471; CAB80760.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81813.1; -; Genomic_DNA.
DR EMBL; AJ488304; CAD32571.1; -; mRNA.
DR PIR; A85001; A85001.
DR PIR; T01330; T01330.
DR RefSeq; NP_191913.3; NM_116219.5. [Q7Y1C5-1]
DR AlphaFoldDB; Q7Y1C5; -.
DR SMR; Q7Y1C5; -.
DR BioGRID; 13519; 5.
DR DIP; DIP-59496N; -.
DR IntAct; Q7Y1C5; 5.
DR STRING; 3702.Q7Y1C5; -.
DR iPTMnet; Q7Y1C5; -.
DR PaxDb; 3702-AT4G00020.2; -.
DR ProteomicsDB; 240412; -. [Q7Y1C5-1]
DR EnsemblPlants; AT4G00020.1; AT4G00020.1; AT4G00020. [Q7Y1C5-1]
DR GeneID; 828230; -.
DR Gramene; AT4G00020.1; AT4G00020.1; AT4G00020. [Q7Y1C5-1]
DR KEGG; ath:AT4G00020; -.
DR Araport; AT4G00020; -.
DR TAIR; AT4G00020; BRCA2(IV).
DR eggNOG; KOG4751; Eukaryota.
DR HOGENOM; CLU_004336_0_0_1; -.
DR InParanoid; Q7Y1C5; -.
DR OMA; MMELYNQ; -.
DR PhylomeDB; Q7Y1C5; -.
DR PRO; PR:Q7Y1C5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q7Y1C5; baseline and differential.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IGI:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR CDD; cd04493; BRCA2DBD_OB1; 1.
DR CDD; cd04494; BRCA2DBD_OB2; 1.
DR FunFam; 2.40.50.140:FF:000262; Protein BREAST CANCER SUSCEPTIBILITY 2 homolog B; 1.
DR FunFam; 2.40.50.140:FF:000267; Protein BREAST CANCER SUSCEPTIBILITY 2 homolog B; 1.
DR FunFam; 2.40.50.140:FF:000282; Protein BREAST CANCER SUSCEPTIBILITY 2 homolog B; 1.
DR FunFam; 2.40.50.140:FF:000297; Protein BREAST CANCER SUSCEPTIBILITY 2 homolog B; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 4.
DR InterPro; IPR015525; BRCA2.
DR InterPro; IPR015252; BRCA2_hlx.
DR InterPro; IPR036315; BRCA2_hlx_sf.
DR InterPro; IPR015187; BRCA2_OB_1.
DR InterPro; IPR048262; BRCA2_OB_2_dom.
DR InterPro; IPR002093; BRCA2_repeat.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR11289:SF0; BREAST CANCER TYPE 2 SUSCEPTIBILITY PROTEIN; 1.
DR PANTHER; PTHR11289; BREAST CANCER TYPE 2 SUSCEPTIBILITY PROTEIN BRCA2; 1.
DR Pfam; PF09169; BRCA-2_helical; 1.
DR Pfam; PF09103; BRCA-2_OB1; 1.
DR Pfam; PF00634; BRCA2; 4.
DR PIRSF; PIRSF002397; BRCA2; 1.
DR SUPFAM; SSF81872; BRCA2 helical domain; 1.
DR SUPFAM; SSF81878; BRCA2 tower domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
DR PROSITE; PS50138; BRCA2_REPEAT; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; DNA damage; DNA recombination;
KW DNA repair; DNA-binding; Meiosis; Reference proteome; Repeat.
FT CHAIN 1..1151
FT /note="Protein BREAST CANCER SUSCEPTIBILITY 2 homolog A"
FT /id="PRO_0000430159"
FT REPEAT 63..97
FT /note="BRCA2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00032"
FT REPEAT 116..150
FT /note="BRCA2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00032"
FT REPEAT 163..197
FT /note="BRCA2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00032"
FT REPEAT 257..291
FT /note="BRCA2 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00032"
FT REGION 408..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1151 AA; 126652 MW; 47E02E02623269AF CRC64;
MSTWQLFPDS SGDGFRWEVA GRILQSVSDS TPTKALESTA PLPSMADLLL QGCSKLIARE
EAMPGEIPMF RTGLGKSVVL KESSIAKAKS ILAEKVTYSD LRNTNCSIPQ MRQVDTAETL
PMFRTASGKS VPLKESSIAK AMSILGSDKI IDSDNVLPRE SGFGVSNSLF QTASNKKVNV
SSAGLARAKA LLGLEEDDLN GFNHVNQSSS SSQQHGWSGL KTHEEFDATV VKHHSGTPGQ
YEDYVSGKRS EVLNPSLKVP PTKFQTAGGK SLSVSAEALK RARNLLGDPE LGSFFDDVAG
GDQFFTPEKD ERLSDIAINN GSANRGYIAH EEKTSNKHTP NSFVSPLWSS SKQFSSVNLE
NLASGGNLIK KFDAAVDETD CALNATHGLS NNRSLASDMA VNNSKVNGFI PRGRQPGRPA
DQPLVDITNR RDTAYAYNKQ DSTQKKRLGK TVSVSPFKRP RISSFKTPSK KHALQASSGL
SVVSCDTLTS KKVLSTRYPE KSPRVYIKDF FGMHPTATTR MDYVPDHVRR IKSSNADKYV
FCDESSSNKV GAETFLQMLA ESGASLQHAS RKWVTNHYRW IVWKLACYDI YYPAKCRGNF
LTITNVLEEL KYRYEREVNH GHCSAIKRIL SGDAPASSMM VLCISAINPK TDNDSQEAHC
SDSCSNVKVE LTDGWYSMNA ALDVVLTKQL NAGKLFVGQK LRILGAGLSG WATPTSPLEA
VISSTICLLL NINGTYRAHW ADRLGFCKEI GVPLALNCIK CNGGPVPKTL AGIKRIYPIL
YKERLGEKKS IVRSERIESR IIQLHNQRRS ALVEGIMCEY QRGINGVHSQ NDTDSEEGAK
IFKLLETAAE PEFLMAEMSP EQLRSFTTYK AKFEAAQQMR KEKSVAETLE DAGLGERNVT
PFMRIRLVGL TSLSYEGEHN PKEGIVTIWD PTERQRTELT EGKIYMMKGL VPINSDSEIL
YLHARGSSSR WQPLSPKDSE NFQPFFNPRK PISLSNLGEI PLSSEFDIAA YVVYVGNAYT
DVLQKKQWVF VTDGSAQHSG EISNSLLAIS FSTSFMDDSS VSHISHNLVG SVVGFCNLIK
RAKDVTNEIW VAEAAENSVY FINAEAAYSS HLKTSSAHIQ TWAKLSSSKS VIHELRQRVL
SIIGACKSPS C
//
