ZBT14_CHICK
ID ZBT14_CHICK Reviewed; 448 AA.
AC Q92010;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Zinc finger and BTB domain-containing protein 14;
DE AltName: Full=Zinc finger protein 161 homolog;
DE Short=Zfp-161;
DE AltName: Full=Zinc finger protein 5;
DE Short=ZF5;
GN Name=ZBTB14; Synonyms=ZFP161;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Muscle;
RX PubMed=8764828; DOI=10.1016/0167-4781(96)00094-2;
RA Bhathal H.S., Stumph W.E.;
RT "Genomic and cDNA structures of the gene encoding the chicken ZF5 DNA
RT binding protein.";
RL Biochim. Biophys. Acta 1308:114-118(1996).
CC -!- FUNCTION: Transcriptional activator of the dopamine transporter (DAT),
CC binding it's promoter at the consensus sequence 5'-CCTGCACAGTTCACGGA-
CC 3'. Binds to 5'-d(GCC)(n)-3' trinucleotide repeats in promoter regions
CC and acts as a repressor of the FMR1 gene. Transcriptional repressor of
CC MYC and thymidine kinase promoters (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ZBTB21. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The BTB/POZ domain seems to direct the protein to discrete
CC regions in the nucleus. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; U51641; AAB38388.1; -; mRNA.
DR EMBL; U51640; AAB38387.1; -; Genomic_DNA.
DR PIR; S71427; S71427.
DR RefSeq; NP_990492.1; NM_205161.1.
DR AlphaFoldDB; Q92010; -.
DR SMR; Q92010; -.
DR STRING; 9031.ENSGALP00000023787; -.
DR PaxDb; Q92010; -.
DR GeneID; 396070; -.
DR KEGG; gga:396070; -.
DR CTD; 7541; -.
DR VEuPathDB; HostDB:geneid_396070; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q92010; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q92010; -.
DR PRO; PR:Q92010; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..448
FT /note="Zinc finger and BTB domain-containing protein 14"
FT /id="PRO_0000047319"
FT DOMAIN 36..102
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 275..302
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 303..330
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 331..358
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 359..386
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 387..415
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 130..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 50..66
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 176..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 448 AA; 51050 MW; 8DF0FA3D8580412A CRC64;
MEFFISMSET IKYNDDDHKT VFLKTLNEQR LEGEFCDIAI VVEDVKFRAH RCVLAACSTY
FKKLFKKLEV DSSSVIEIDF LRSDIFEEVL NYMYTAKISV KKEDVNLMMS SGQILGIRFL
DKLCSQKRDV SSPEENTQSK SKYCLKINRP IGEPNDTQDD EVEEIGDHDD SPSDVTVEGT
PPSQEDGKSP TTTLRVQEAI LKELGSEEVR KVNCYGQEVE SMETTESKDL GSQTPQALTF
NDGISEVKDE QTPGWTTAAG DMKFEYLLYG HREHIVCQAC GKTFSDEARL RKHEKLHTAD
RPFVCEMCTK GFTTQAHLKE HLKIHTGYKP YSCEVCGKSF IRAPDLKKHE RVHSNERPFA
CHMCDKAFKH KSHLKDHERR HRGEKPFVCG SCTKAFAKAS DLKRHENNMH SERKQVTTAN
SIQSETEQLQ AAAMAREAEQ QLETIACS
