BARD1_ARATH
ID BARD1_ARATH Reviewed; 714 AA.
AC F4I443; B5A7D6; B5A7D7; Q9ZWC2;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=BRCA1-associated RING domain protein 1 {ECO:0000303|PubMed:18591352};
DE Short=AtBARD1 {ECO:0000303|PubMed:18591352};
DE AltName: Full=Protein REPRESSOR OF WUSCHEL 1 {ECO:0000303|PubMed:19704708};
GN Name=BARD1 {ECO:0000303|PubMed:18591352};
GN Synonyms=ROW1 {ECO:0000303|PubMed:19704708};
GN OrderedLocusNames=At1g04020 {ECO:0000312|Araport:AT1G04020};
GN ORFNames=F21M11.4 {ECO:0000312|EMBL:AAD10669.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 47-714 (ISOFORM 1), FUNCTION, DISRUPTION
RP PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP SUBUNIT, AND INTERACTION WITH SYD.
RX PubMed=18591352; DOI=10.1105/tpc.108.058867;
RA Han P., Li Q., Zhu Y.-X.;
RT "Mutation of Arabidopsis BARD1 causes meristem defects by failing to
RT confine WUSCHEL expression to the organizing center.";
RL Plant Cell 20:1482-1493(2008).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH BRCA1, TISSUE SPECIFICITY,
RP 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 [5]
RP REVIEW.
RX PubMed=19704708; DOI=10.4161/psb.4.1.7312;
RA Han P., Zhu Y.-X.;
RT "BARD1 may be renamed ROW1 because it functions mainly as a REPRESSOR OF
RT WUSCHEL1.";
RL Plant Signal. Behav. 4:52-54(2009).
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).
RN [7]
RP INDUCTION BY ERF114.
RX PubMed=23616605; DOI=10.1104/pp.113.214049;
RA Mehrnia M., Balazadeh S., Zanor M.I., Mueller-Roeber B.;
RT "EBE, an AP2/ERF transcription factor highly expressed in proliferating
RT cells, affects shoot architecture in Arabidopsis.";
RL Plant Physiol. 162:842-857(2013).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=25631790; DOI=10.1038/ncomms7003;
RA Zhang Y., Jiao Y., Liu Z., Zhu Y.-X.;
RT "ROW1 maintains quiescent centre identity by confining WOX5 expression to
RT specific cells.";
RL Nat. Commun. 6:6003-6003(2015).
CC -!- FUNCTION: Binds specifically to H3K4me3 regions of target genes (e.g.
CC WUS and WOX5) promoters to repress their transcription via chromatin
CC remodeling. Required for the shoot apical meristem (SAM) organization
CC and maintenance, by confining WUS expression to the organizing center,
CC and for the quiescent center (QC) development in the root apical
CC meristem (RAM), by repressing WOX5 expression in the root proximal
CC meristem (PubMed:18591352, PubMed:25631790). Plays a role in DNA repair
CC and in cell-cycle control. Required for the repair of DNA double-strand
CC breaks (DSBs), both natural and induced by genotoxic stress, by
CC homologous recombination (HR) (PubMed:16957774).
CC {ECO:0000269|PubMed:16957774, ECO:0000269|PubMed:18591352,
CC ECO:0000269|PubMed:25631790}.
CC -!- SUBUNIT: Component of a DNA-protein complex on WUS and WOX5 promoters
CC (PubMed:25631790, PubMed:18591352). Interacts with SYD
CC (PubMed:18591352). Forms heterodimer with BRCA1 (PubMed:16957774).
CC {ECO:0000269|PubMed:16957774, ECO:0000269|PubMed:18591352,
CC ECO:0000269|PubMed:25631790}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16957774,
CC ECO:0000305|PubMed:18591352}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=Additional isoforms seem to exist. {ECO:0000305};
CC Name=1;
CC IsoId=F4I443-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in the shoot apical meristem (SAM),
CC roots, flowers, embryos and seedlings (PubMed:18591352). Mostly
CC expressed in flowers and siliques, and, to a lower extent, in roots,
CC rosette leaves, inflorescence and young cauline leaves
CC (PubMed:16957774). {ECO:0000269|PubMed:16957774,
CC ECO:0000269|PubMed:18591352}.
CC -!- DEVELOPMENTAL STAGE: Expressed specifically in the apical domains of
CC the shoot apical meristem (SAM), inflorescences, ovules, anthers and
CC embryos. In young seedlings, localized mainly in the outermost three to
CC four cell layers of the main shoot apex and in developing leaf
CC primordia and young leaves. Also present in the meristem zone of
CC primary roots and in the initiation site of lateral roots.
CC {ECO:0000269|PubMed:18591352}.
CC -!- INDUCTION: Up-regulated by the transcription factor ERF114.
CC {ECO:0000269|PubMed:23616605}.
CC -!- DISRUPTION PHENOTYPE: Enhanced sensitivity to genotoxic stresses (e.g.
CC bleomycin and mitomycin C (MMC)) due to reduced intrachromosomal
CC homologous recombination (HR) (PubMed:16957774). Meristem defects
CC associated with ectopic WUSCHEL expression at high levels (e.g. 238
CC fold higher than controls) mainly in the outermost cell layers instead
CC of the organizing center (PubMed:18591352). Abnormal quiescent center
CC (QC) in the root apical meristem (RAM) and defects in cell
CC differentiation leading to short roots and loss of gravitropic
CC response, probably due to defect in columella cell differentiation.
CC Ectopic expression of WOX5 in RAM cells that normally express ROW1
CC (PubMed:25631790). {ECO:0000269|PubMed:16957774,
CC ECO:0000269|PubMed:18591352, ECO:0000269|PubMed:25631790}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD10669.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC003027; AAD10669.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; EU817406; ACF35259.1; -; mRNA.
DR EMBL; EU817407; ACF35260.1; -; mRNA.
DR PIR; D86171; D86171.
DR AlphaFoldDB; F4I443; -.
DR SMR; F4I443; -.
DR STRING; 3702.AT1G04020.1; -.
DR PaxDb; F4I443; -.
DR ProteomicsDB; 240812; -. [F4I443-1]
DR Araport; AT1G04020; -.
DR TAIR; locus:2024244; AT1G04020.
DR eggNOG; KOG4362; Eukaryota.
DR InParanoid; F4I443; -.
DR PRO; PR:F4I443; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I443; baseline and differential.
DR Genevisible; F4I443; 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:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
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:0080182; P:histone H3-K4 trimethylation; IDA:UniProtKB.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0010078; P:maintenance of root meristem identity; IMP:UniProtKB.
DR GO; GO:0010492; P:maintenance of shoot apical meristem identity; 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:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
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:0065004; P:protein-DNA complex assembly; IDA:UniProtKB.
DR GO; GO:0009934; P:regulation of meristem structural organization; IMP: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; IPR001965; Znf_PHD.
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 SMART; SM00292; BRCT; 2.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 2.
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 Alternative splicing; Developmental protein; DNA damage; DNA repair;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..714
FT /note="BRCA1-associated RING domain protein 1"
FT /id="PRO_0000432982"
FT DOMAIN 482..577
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 598..713
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT ZN_FING 25..63
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 331..382
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 402..451
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 106..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 714 AA; 79690 MW; 9CE32995288E50CE CRC64;
MAEFTNMLMN PWVLHLQKLE LELKCPLCLK LLNRPVLLPC DHVFCDSCVH KSSQVESGCP
VCKSKHPKKA RRDLRFMESV ISIYKSLNAA VSVHLPQLQI PNDCNYKNDA LNNSNSPKHG
ESEDSEMTDK DVSKRSGGTD SSSRDGSPLP TSEESDPRPK HQDWTEKQLS DHLLLYEFES
EYDAANHTPE SYTEQAAKNV RDITASEQPS NAARKRICGD SFIQESSPNP KTQDPTLLRL
MESLRSDDPT DYVKAQNHQQ LPKSHTEQDS KRKRDITASD AMENHLKVPK RENNLMQKSA
DIDCNGKCSA NSDDQLSEKI SKALEQTSSN ITICGFCQSA RVSEATGEML HYSRGRPVDG
DDIFRSNVIH VHSACIEWAP QVYYEGDTVK NLKAELARGM KIKCTKCSLK GAALGCFVKS
CRRSYHVPCA REISRCRWDY EDFLLLCPAH SSVKFPNEKS GHRVSRAEPL PKINPAELCS
LEQTPAFTKE LVLCGSALSK SDKKLMESLA VRFNATISRY WNPSVTHVIA STDEKGACTR
TLKVLMGILN GKWIINAAWM KASLKASQPV DEEPFEIQID TQGCQDGPKT ARLRAETNKP
KLFEGLKFYF FGDFYKGYKE DLQNLVKVAG GTILNTEDEL GAESSNNVND QRSSSIVVYN
IDPPHGCALG EEVTIIWQRA NDAEALASQT GSRLVGHTWV LESIAGYKLH PVIG
