ID A0A3B1JVW6_ASTMX Unreviewed; 1579 AA.
AC A0A3B1JVW6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=RING-type E3 ubiquitin transferase BRCA1 {ECO:0000256|ARBA:ARBA00031556};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000045479.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000045479.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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DR STRING; 7994.ENSAMXP00000045479; -.
DR Ensembl; ENSAMXT00000047037.1; ENSAMXP00000045479.1; ENSAMXG00000036089.1.
DR GeneTree; ENSGT00440000034289; -.
DR InParanoid; A0A3B1JVW6; -.
DR OrthoDB; 5405431at2759; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000036089; Expressed in testis and 11 other cell types or tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd16498; RING-HC_BRCA1; 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; IPR011364; BRCA1.
DR InterPro; IPR031099; BRCA1-associated.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR13763:SF0; BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN; 1.
DR PANTHER; PTHR13763; BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN BRCA1; 1.
DR Pfam; PF00533; BRCT; 2.
DR Pfam; PF00097; zf-C3HC4; 1.
DR PIRSF; PIRSF001734; BRCA1; 3.
DR PRINTS; PR00493; BRSTCANCERI.
DR SMART; SM00292; BRCT; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52113; BRCT domain; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50172; BRCT; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 22..64
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1390..1461
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 1481..1579
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 108..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1219..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1579 AA; 172528 MW; 5BF7FF7BA00FCE3E CRC64;
MTAPKAEDIK RGIAVIWENL QCPICLDLMN APVSTRCDHQ FCKFCLMKLL ERSKKKETSC
PVCKMNVTKR SLKESPGFQR LVEGLQNLVQ SYEFDTCTSY FTGIPQSRKE TSVETESRDQ
QCSEENGSSG NDVTDKSASH FSSAAVKDAF AELMGLVDSC TVNSEQDCFD SGLGGPVNKA
DELQDVPSRI EDRQSNSPIP DSSGSDGKTD LHKRRSSRRP KRVGLEPDRI ADKRQKKSVE
KVAEWLLKIS PSSDTQTRDR SRDPSVPADS DSEKESVCSS SPTEAYPKDG DEDDVNPPKE
VRGRGLEEKV FGAVYKRERK GGKTKVNRPV SPEKETVTNP VPFNLVQEEE MMTRHGLKRK
RSCRLTPADF IKKSSSDGRE AEVKEPVDSV THNAVEENKQ VELNTEEQIE ILGECDKIAE
LSADAKCDNT VKNMEESPAI EVPLKRSGRR SKSKMQDIWQ NVDLDLKEKE NICDNRTSRK
RRSNRSSCEL TKDGHLDESK NAKCTKSLTL VDAAANNVDV MEQLKNKPKI VEAEINIESY
PSSADPRSPD ARKTRRSLRL QAFTTEIQGT LKQRRTTKPS SGPETHPLDN PSHFNCLDQP
NVDKVNANEE NVDADQGIGS TQQSRSGKTD LLIMKNGCVF NSSLGTIEAV QTNEETATSP
CVSEGQGPEQ NSVLSIIPDT VAQDGPSLPC SSVAASSAFP LQAVTLDSSL PEKSQTSPSA
GFVAPSVVQT LKDAHCERGG IEVEGETNDS ELDTELLMKS FKASKRKSFH LGSPKPSPKT
VQERLLTRTD EEQKLQYQIP TTCKDDELTS DLATICHNDL PPSSNASKLP LCEESSQRSQ
SSFGNAAVAS LIQANASVAT GDQKEAFLKN SGNSTCSGLS PNRVARSSQD SKLPTNSDSA
ASYQGFFPKV TSEESSICSS SEVQKNELQK SPKLGTCQPR IAEMSNKVEG SDVQTKHSSD
SNKSPNIAAA GSPNLGAHSN QFESSITPDG LIPKGPVPYE CQVTEPASNH SLNEENDAGS
QPCVPRKRRA QRLESSESEL SVEDDSLPTL AHIFKSHRLP SHSGQEPNQT SEISELDHQE
PDPGYQSPAD QEPDPGYQSP ADQEPDPGFQ SPADQANKSN EATPEAQSQN QECPENANAT
ADDDHLPQPS CREEWVTSSQ GSVDLFGTPE ESEAVGICGN VAVSRDSSQY SSEIITTQQK
EEMQQELCRL ERMMALVSEA LQKKEKDTSA KTQNKALNPT HSELQSAADP DQAEPCSPAL
PADRQSGLDS DGDHSGVSPG PAAPDGLCAP ESQPLLMTDQ AKTGRRVSRS RQKSQGRGRK
SSQKAEAGLS LRNHNTTSEG SVTELTKGNE AKEAQKQTRG ADMRRLGSSS TAGKMELVAS
GLSASELMLV KKFARKMHGH LSKEMTPGTT HVIIKTDEDL VCERTLKYFQ GIAGRKWVVS
FLWISECFNQ GQVLDEAQFE VRGDVVNGHN HNGPLKSRTT SDGLLMKGYE ICFQGSFTAM
TTDQMEAMVE MCGATVVKDP LMFSKHIESK CQLVVVQPGS DDSQTYYRAL QKKATVVSRS
WLLDTISTYS LQNPQDHKP
//
