BRCA1_ARATH
ID BRCA1_ARATH Reviewed; 941 AA.
AC Q8RXD4; Q9SUA7;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein BREAST CANCER SUSCEPTIBILITY 1 homolog {ECO:0000303|PubMed:12582233};
DE Short=AtBRCA1 {ECO:0000303|PubMed:12582233};
GN Name=BRCA1 {ECO:0000303|PubMed:12582233};
GN OrderedLocusNames=At4g21070 {ECO:0000312|Araport:AT4G21070};
GN ORFNames=T13K14.230 {ECO:0000312|EMBL:CAB45902.1};
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], INDUCTION BY GAMMA RAYS, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=12582233; DOI=10.1093/nar/gkg202;
RA Lafarge S., Montane M.-H.;
RT "Characterization of Arabidopsis thaliana ortholog of the human breast
RT cancer susceptibility gene 1: AtBRCA1, strongly induced by gamma rays.";
RL Nucleic Acids Res. 31:1148-1155(2003).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH BARD1/ROW1, INDUCTION BY
RP GAMMA RAYS, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16957774; DOI=10.1038/sj.emboj.7601313;
RA Reidt W., Wurz R., Wanieck K., Chu H.H., Puchta H.;
RT "A homologue of the breast cancer-associated gene BARD1 is involved in DNA
RT repair in plants.";
RL EMBO J. 25:4326-4337(2006).
RN [6]
RP REVIEW, AND GENE FAMILY.
RX PubMed=22629260; DOI=10.3389/fpls.2011.00019;
RA Trapp O., Seeliger K., Puchta H.;
RT "Homologs of breast cancer genes in plants.";
RL Front. Plant Sci. 2:19-19(2011).
CC -!- FUNCTION: Plays a role in DNA repair and in cell-cycle control.
CC Required for the repair of DNA double-strand breaks (DSBs), both
CC natural and induced by genotoxic stress, by homologous recombination
CC (HR). {ECO:0000269|PubMed:16957774}.
CC -!- SUBUNIT: Forms heterodimer with BARD1/ROW1.
CC {ECO:0000269|PubMed:16957774}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:16957774}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously with highest levels in
CC flower buds (PubMed:12582233). Mostly expressed in flowers and
CC siliques, and, to a lower extent, in roots, rosette leaves,
CC inflorescence and young cauline leaves (PubMed:16957774).
CC {ECO:0000269|PubMed:12582233, ECO:0000269|PubMed:16957774}.
CC -!- INDUCTION: By gamma rays treatment. {ECO:0000269|PubMed:12582233,
CC ECO:0000269|PubMed:16957774}.
CC -!- DISRUPTION PHENOTYPE: Enhanced sensitivity to mitomycin C.
CC {ECO:0000269|PubMed:16957774}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB45902.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At4g21065 and At4g21070.; Evidence={ECO:0000305};
CC Sequence=CAB79107.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At4g21065 and At4g21070.; Evidence={ECO:0000305};
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DR EMBL; AY081328; AAL91217.1; -; mRNA.
DR EMBL; AL080282; CAB45902.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161554; CAB79107.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84396.1; -; Genomic_DNA.
DR EMBL; AF515728; AAO39850.1; -; mRNA.
DR EMBL; BT010547; AAQ65170.1; -; mRNA.
DR RefSeq; NP_193839.4; NM_118225.5.
DR AlphaFoldDB; Q8RXD4; -.
DR SMR; Q8RXD4; -.
DR BioGRID; 13145; 1.
DR STRING; 3702.AT4G21070.1; -.
DR PaxDb; Q8RXD4; -.
DR PRIDE; Q8RXD4; -.
DR ProteomicsDB; 240501; -.
DR EnsemblPlants; AT4G21070.1; AT4G21070.1; AT4G21070.
DR GeneID; 827854; -.
DR Gramene; AT4G21070.1; AT4G21070.1; AT4G21070.
DR KEGG; ath:AT4G21070; -.
DR Araport; AT4G21070; -.
DR TAIR; locus:2133109; AT4G21070.
DR eggNOG; KOG4362; Eukaryota.
DR HOGENOM; CLU_004218_0_0_1; -.
DR InParanoid; Q8RXD4; -.
DR OMA; MKSGSNC; -.
DR OrthoDB; 854133at2759; -.
DR PhylomeDB; Q8RXD4; -.
DR PRO; PR:Q8RXD4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8RXD4; baseline and differential.
DR Genevisible; Q8RXD4; AT.
DR GO; GO:0070531; C:BRCA1-A complex; IBA:GO_Central.
DR GO; GO:0031436; C:BRCA1-BARD1 complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0071480; P:cellular response to gamma radiation; IEP:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; IMP:TAIR.
DR GO; GO:0006281; P:DNA repair; IMP:TAIR.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0035067; P:negative regulation of histone acetylation; IBA:GO_Central.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010332; P:response to gamma radiation; IEP:TAIR.
DR Gene3D; 3.30.40.10; -; 2.
DR Gene3D; 3.40.50.10190; -; 2.
DR InterPro; IPR031099; BRCA1-associated.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR13763; PTHR13763; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF16589; BRCT_2; 1.
DR PIRSF; PIRSF001734; BRCA1; 1.
DR SMART; SM00292; BRCT; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52113; SSF52113; 2.
DR PROSITE; PS50172; BRCT; 2.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Zinc; Zinc-finger.
FT CHAIN 1..941
FT /note="Protein BREAST CANCER SUSCEPTIBILITY 1 homolog"
FT /id="PRO_0000363413"
FT DOMAIN 724..819
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 840..941
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT ZN_FING 16..54
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 561..612
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 632..681
FT /note="PHD-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 87..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 298..305
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 444..451
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 97..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 941 AA; 103922 MW; 4EF2D20BA443C9AA CRC64;
MADTSHLERM GRELKCPICL SLYNSAVSLS CNHVFCNACI VKSMKMDATC PVCKIPYHRR
EIRGAPHMDS LVSIYKNMED ASGIKLFVSQ NNPSPSDKEK QVRDASVEKA SDKNRQGSRK
GRASKRNEYG KTKEIDVDAP GPIVMKPSSQ TKKRVQLLQN LSAESLTKPT ESVETAEKPK
DYTENTVIRL DEHPSLNKEG NLSPFFWLRD EDDGENSSQR TESDQLLGTT PVNVPSFSDL
MDSDHESPSK EDEQQKPNPG DMFDSEMFEW TQRPCSPEIL PSPVKAKVLG RDEIDLTQKK
LPKVKVASSK CKNRKAGSAR NTVARRSIGV SQEDNMESSA AATISEQQDS RGTSGTIIRN
DVNTDENVKA KRATRSKAQS TRVQSDLNVS NEADGKQGTK RKRSSIKSSP AHPIAGPNEL
SLGTEIVGKG DQDQAHGPSD THPEKRSPTE KPSLKKRGRK SNASSSLKDL SGKTQKKTSE
KKLKLDSHMI SSKATQPHGN GILTAGLNQG GDKQDSRNNR KSTVGKDDHT MQVIEKCSTI
NKSSSGGSAH LRRCNGSLTK KFTCAFCQCS EDTEASGEMT HYYRGEPVSA DFNGGSKVIH
VHKNCAEWAP NVYFNDLTIV NLDVELTRSR RISCSCCGLK GAALGCYNKS CKNSFHVTCA
KLIPECRWDN VKFVMLCPLD ASIKLPCEEA NSKDRKCKRT PKEPLHSQPK QVSGKANIRE
LHIKQFHGFS KKLVLSCSGL TVEEKTVIAE FAELSGVTIS KNWDSTVTHV IASINENGAC
KRTLKFMMAI LEGKWILTID WIKACMKNTK YVSEEPYEIT MDVHGIREGP YLGRQRALKK
KPKLFTGLKF YIMGDFELAY KGYLQDLIVA AGGTILRRRP VSSDDNEAST IVVFSVEPSK
KKTLTQRRSD AEALAKSARA RAASSSWVLD SIAGCQILVL I
