ZBT7A_CHICK
ID ZBT7A_CHICK Reviewed; 546 AA.
AC O93567;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Zinc finger and BTB domain-containing protein 7A {ECO:0000305};
DE AltName: Full=Leukemia/lymphoma-related factor {ECO:0000303|PubMed:9927193};
DE Short=cLRF {ECO:0000303|PubMed:9927193};
GN Name=ZBTB7A {ECO:0000250|UniProtKB:O95365};
GN Synonyms=LRF {ECO:0000303|PubMed:9927193}, ZBTB7;
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 [MRNA].
RX PubMed=9927193; DOI=10.1038/sj.onc.1202332;
RA Davies J.M., Hawe N., Kabarowski J., Huang Q.-H., Zhu J., Brand N.J.,
RA Leprince D., Dhordain P., Cook M., Moriss-Kay G., Zelent A.;
RT "Novel BTB/POZ domain zinc-finger protein, LRF, is a potential target of
RT the LAZ-3/BCL-6 oncogene.";
RL Oncogene 18:365-375(1999).
CC -!- FUNCTION: Transcription factor that represses the transcription of a
CC wide range of genes involved in cell proliferation and differentiation.
CC Directly and specifically binds to the consensus sequence 5'-
CC [GA][CA]GACCCCCCCCC-3' and represses transcription both by regulating
CC the organization of chromatin and through the direct recruitment of
CC transcription factors to gene regulatory regions (By similarity). May
CC also play a role, independently of its transcriptional activity, in
CC double-strand break repair via classical non-homologous end
CC joining/cNHEJ and in alternative splicing (By similarity).
CC {ECO:0000250|UniProtKB:O88939, ECO:0000250|UniProtKB:O95365}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O88939}.
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DR EMBL; AF086831; AAC35368.1; -; mRNA.
DR RefSeq; NP_990011.1; NM_204680.1.
DR AlphaFoldDB; O93567; -.
DR SMR; O93567; -.
DR STRING; 9031.ENSGALP00000041866; -.
DR Ensembl; ENSGALT00000044229; ENSGALP00000041866; ENSGALG00000025907.
DR GeneID; 395411; -.
DR KEGG; gga:395411; -.
DR CTD; 51341; -.
DR VEuPathDB; HostDB:geneid_395411; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162053; -.
DR HOGENOM; CLU_025627_1_0_1; -.
DR InParanoid; O93567; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O93567; -.
DR PRO; PR:O93567; -.
DR Proteomes; UP000000539; Chromosome 28.
DR Bgee; ENSGALG00000025907; Expressed in ovary and 13 other tissues.
DR ExpressionAtlas; O93567; baseline and differential.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor 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:0001222; F:transcription corepressor binding; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; 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 GO; GO:2000677; P:regulation of transcription regulatory region DNA binding; ISS:UniProtKB.
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; 2.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..546
FT /note="Zinc finger and BTB domain-containing protein 7A"
FT /id="PRO_0000047718"
FT DOMAIN 34..101
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 359..381
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 387..409
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 415..437
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 443..467
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 189..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 546 AA; 59842 MW; 8E3DDC652E1876C7 CRC64;
MAGGVDGPIG IPFPDHSSDI LSSLNEQRNN GLLCDVVILV EGQEFPTHRS VLAACSQYFK
KLFTSGLVVD QQNVYEIDFV SADALSALLE FAYTATLTVS TSNVNDILNA AKLLEIPAVR
DVCTDLLDRK ILAKNDQMDL VDQIDQRNHL RAKEYLEFFQ SNPVNGHQGS FPWTNPELRD
LQRLNFRGQE DEEEPDCNGL DFYSQAPLNE RPKANDCDPD SNPAMWLDRE EEEAAAAPGS
LFSPSQNGHY SGRGLGTPGE EEGAPGAALD QQDAGDSPSF VPTGAEAEDD ARDVDGLAAS
VLQQVMGSVG RQQLGDDERK DDDGVVDYYL KYFGSSNESD VYPSWSQKVE KKIRAKAFQK
CPICAKVIQG AGKLPRHIRT HTGEKPYECN ICNVRFTRQD KLKVHMRKHT GEKPYLCQQC
GAAFAHNYDL KNHMRVHTGL RPYQCDSCFK TFVRSDHLHR HLKKDGCNGI PSRRGRRPRV
RDAGGLPTPT GNPEDGGFQG GGESQESEDT VQGNGREQHF EESSTAEAAG LNVAGGAAEG
SAPGPS
