ID G1SFN0_RABIT Unreviewed; 751 AA.
AC G1SFN0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=BRCA1 associated RING domain 1 {ECO:0000313|Ensembl:ENSOCUP00000001334.3};
GN Name=BARD1 {ECO:0000313|Ensembl:ENSOCUP00000001334.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000001334.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000001334.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000001334.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000001334.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000001334.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AAGW02042602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02042603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008257340.2; XM_008259118.2.
DR AlphaFoldDB; G1SFN0; -.
DR SMR; G1SFN0; -.
DR STRING; 9986.ENSOCUP00000001334; -.
DR PaxDb; 9986-ENSOCUP00000001334; -.
DR Ensembl; ENSOCUT00000001552.4; ENSOCUP00000001334.3; ENSOCUG00000001552.4.
DR GeneID; 100340914; -.
DR KEGG; ocu:100340914; -.
DR CTD; 580; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4362; Eukaryota.
DR GeneTree; ENSGT00940000156532; -.
DR HOGENOM; CLU_021642_0_0_1; -.
DR InParanoid; G1SFN0; -.
DR OMA; KKSIKMW; -.
DR OrthoDB; 2478587at2759; -.
DR TreeFam; TF326440; -.
DR Proteomes; UP000001811; Chromosome 7.
DR Bgee; ENSOCUG00000001552; Expressed in embryo and 14 other cell types or tissues.
DR GO; GO:0070531; C:BRCA1-A complex; IEA:Ensembl.
DR GO; GO:0070532; C:BRCA1-B complex; IEA:Ensembl.
DR GO; GO:0031436; C:BRCA1-BARD1 complex; IEA:Ensembl.
DR GO; GO:0070533; C:BRCA1-C complex; IEA:Ensembl.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:Ensembl.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:Ensembl.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0046826; P:negative regulation of protein export from nucleus; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0085020; P:protein K6-linked ubiquitination; IEA:Ensembl.
DR GO; GO:0042325; P:regulation of phosphorylation; IEA:Ensembl.
DR CDD; cd17734; BRCT_Bard1_rpt1; 1.
DR CDD; cd17720; BRCT_Bard1_rpt2; 1.
DR CDD; cd16496; RING-HC_BARD1; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR039503; BARD1_Znf-RING.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR24171; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 39-RELATED; 1.
DR PANTHER; PTHR24171:SF8; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 39-RELATED; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF14835; zf-RING_6; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00292; BRCT; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52113; BRCT domain; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50172; BRCT; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 25..62
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REPEAT 400..432
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 433..465
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 466..498
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 543..626
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 640..751
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 161..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 751 AA; 83472 MW; A4A83F71666F09B0 CRC64;
MDPAGGGAWA HSRAALGRLE NLLRCSRCGN ILREPVCLGG CEHIFCSNCV SDCIGTRCPV
CHTPAWIQDV KINRQLGSMI QLCSKLRNLL HDNKLPDLKE DTSRTRLFND AESKKNSIKM
WFSPRSKKVR YIVSKVSVQT QPQKMKDENT QQTSMYEFVS ATPPTDVPKK AKKNSTTSGK
KQKKKTLAEI NQEWNLEAGK ENSETDLKDE CKEKLVSFCS QPSVIASPPV NDEIDLLASG
SVIECEPLGN LTEATLPLAE QIESPDIETK SEVTLEEVCE NYPTSKRSLP LDGKGKRRLP
SPVSKKRRSS TPSTSRDFPK QTEISENVPL PNCSSPPSNK RKVGTTLSRK SSNVPEESLN
LSPGTPPSSL NSSTYRRMMS SPLVLKSSPG SLMAGKRNHR GETLLHVAAI KGDVPSVEYL
LQNGSDPNVK DNAGWTPLHE ACNHGHLRVV ELLLQHKALV NSTGYQNDSP LHDAAKNGHL
DIVKLLLSYG ASRNAVNIFG LRPVDYTDNE NMKSLLLLPE KNESSSTRHG LVLNTGHRRD
RPLILIGSGL SSEQQKMLDE LAAILKAKKC TEFDSTVTHV IVPGGTLQST LKCMLGILNG
CWILKFEWVK ACLQSKTCER EEKYEVPDGP QRSRLNREQL LPKLFDGCYF YFGGTFKHLP
KDNLIKLVTA AGGQVLSRRP KPDSDVTQTI NTVAYHAQPD SDQRFCTQYI IYEDFSPHYH
PERIRQGKVW MAPSSWFIGC VMAFELLPLD S
//
