ID   M3Z6C5_MUSPF            Unreviewed;       980 AA.
AC   M3Z6C5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Zinc finger BED domain-containing protein 6 {ECO:0000313|RefSeq:XP_012913617.1};
DE   SubName: Full=Zinc finger BED-type containing 6 {ECO:0000313|Ensembl:ENSMPUP00000019138.1};
GN   Name=ZBED6 {ECO:0000313|Ensembl:ENSMPUP00000019138.1,
GN   ECO:0000313|RefSeq:XP_012913617.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000019138.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000019138.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_012913617.1}
RP   IDENTIFICATION.
RC   TISSUE=Brain {ECO:0000313|RefSeq:XP_012913617.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; AEYP01041210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012913617.1; XM_013058163.2.
DR   STRING; 9669.ENSMPUP00000019138; -.
DR   Ensembl; ENSMPUT00000019414.1; ENSMPUP00000019138.1; ENSMPUG00000019262.1.
DR   GeneID; 101691688; -.
DR   KEGG; mpuf:101691688; -.
DR   CTD; 100381270; -.
DR   eggNOG; KOG1121; Eukaryota.
DR   GeneTree; ENSGT00940000163411; -.
DR   HOGENOM; CLU_303823_0_0_1; -.
DR   OMA; YTWRAIC; -.
DR   OrthoDB; 3084694at2759; -.
DR   Proteomes; UP000000715; Unplaced.
DR   GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:Ensembl.
DR   GO; GO:0001835; P:blastocyst hatching; IEA:Ensembl.
DR   GO; GO:0051148; P:negative regulation of muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR   InterPro; IPR008906; HATC_C_dom.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR003656; Znf_BED.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   PANTHER; PTHR47241; FINGER PROTEIN, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR47241:SF2; ZINC FINGER BED DOMAIN-CONTAINING PROTEIN 6; 1.
DR   Pfam; PF05699; Dimer_Tnp_hAT; 1.
DR   Pfam; PF02892; zf-BED; 2.
DR   SMART; SM00614; ZnF_BED; 2.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR   SUPFAM; SSF140996; Hermes dimerisation domain; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50808; ZF_BED; 2.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00027}.
FT   DOMAIN          130..187
FT                   /note="BED-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50808"
FT   DOMAIN          265..322
FT                   /note="BED-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50808"
FT   REGION          208..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          328..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..238
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..363
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   980 AA;  109920 MW;  6454155B684F1FAD CRC64;
     MSVCTLSVPV SSLSSGRRCS TFSGAGILGC VPINSNTDEE DVLEGKMVAE GMDKEAKLPA
     KKKRKKGLRI KGKRRRKKLL LAKKFSKDLG SGRPVADAPA LLTSSAHEQD EESLFENNIE
     KQIYLPSTRA KTSIVWHFFH VDPQYTWRAI CNLCEKSVSR GKPGSHLGTS TLQRHLQARH
     SPHWTRANKY GVTSGEEDFT LDVPLSPSSA GSNGSFEYMS TDPLDENRMG KKRDKSVSDA
     LRAERGRFLI KSNIVKHALI PGTRAKTSAV WNFFYTDPQH ISRAVCNICK RSVSRGRPGS
     HLGTSTLQRH LQATHPIHWA VANKDSGAVG NGLDEGETER NDLLRDPLHG EKSTGSHDLT
     AEDLSDSDSD EPPVLEVENS RRCESPIPVA EQDTLTHAQE RETTYSENSV SSQISQAIIQ
     MIVEDMHPYN YFSTPAFQRF MQIVAPDYRL PSETYFFTKA VPQLYDWVRE KIFLTLENVQ
     SQKIHLTVDI WTHDPSTDYF IVTVHWVSLE TAPSSNGRIP NFRKWAVLCV TGLAKDCLIT
     NILQELNDQI GLWLSPNFLI PSFIVSDNSS NVVHAIKDGG FTHVPCFLHC LNIVIQDFFC
     EHKSIENMLV AARKTCHHFS HSVKARQILQ EFQNDHQLPW KNLKQDETGH WISTFYMLKW
     LLEHCYSVHH SLGRASGVVL TSLQWTLMTY VCDILKPFEE ATQKVSVKTT GLNQVLPLIH
     HLLLSLQKLR EDFQIRGITQ ALNLVDSLSL KLETDTLLSA MLKSKPCILA ALLDPCFKNS
     LEDFFPQGAD LETYKQILAE EVCNYMESSE VCHIATSDAS GPPAIVGADS FTSSIREGTS
     SSGSFDSSAV DNVAIGSKSF MFPSAIAVVD EYFKEKYSDI SGGGDPLIYW QRKVSIWPAL
     TQVAIQYLSC PMCSWQSECI FTANSQFHPK QIVSLDFDNI EQLMFLKMNL KNVNYDYSTL
     VLSWDPGNEV IQSNEKEILP
//