ID   ZBT8A_RAT               Reviewed;         441 AA.
AC   B1WBU4;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Zinc finger and BTB domain-containing protein 8A;
GN   Name=Zbtb8a;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR   EMBL; BC161892; AAI61892.1; -; mRNA.
DR   RefSeq; XP_006238993.1; XM_006238931.3.
DR   AlphaFoldDB; B1WBU4; -.
DR   STRING; 10116.ENSRNOP00000010983; -.
DR   iPTMnet; B1WBU4; -.
DR   PhosphoSitePlus; B1WBU4; -.
DR   PaxDb; B1WBU4; -.
DR   PRIDE; B1WBU4; -.
DR   GeneID; 313049; -.
DR   CTD; 653121; -.
DR   RGD; 1308756; Zbtb8a.
DR   VEuPathDB; HostDB:ENSRNOG00000008300; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_022356_1_1_1; -.
DR   InParanoid; B1WBU4; -.
DR   OMA; VPHYKSS; -.
DR   OrthoDB; 755439at2759; -.
DR   PhylomeDB; B1WBU4; -.
DR   PRO; PR:B1WBU4; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000008300; Expressed in pancreas and 18 other tissues.
DR   Genevisible; B1WBU4; RN.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR   GO; GO:0001223; F:transcription coactivator binding; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
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; 2.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   2: Evidence at transcript level;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..441
FT                   /note="Zinc finger and BTB domain-containing protein 8A"
FT                   /id="PRO_0000378510"
FT   DOMAIN          24..92
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   ZN_FING         282..304
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         310..333
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          135..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96BR9"
FT   MOD_RES         167
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96BR9"
FT   CROSSLNK        178
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96BR9"
FT   CROSSLNK        182
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96BR9"
FT   CROSSLNK        199
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96BR9"
FT   CROSSLNK        437
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96BR9"
SQ   SEQUENCE   441 AA;  49945 MW;  15655FAA7E99D15E CRC64;
     MEISSHQSHL LEQLNEQRRQ DVFCDCSILV EGKVFKAHRN VLFASSGYFK MLLSQNSKET
     SQPTTATFQT FSPDTFTVIL DFVYSGKLSL TGQNVIEVMS AASFLQMTDV ISVCKTFIKS
     SLDISEKEKD RYFSLSDKDT GSNGVERPSV YSSSWQEDGG SPRSHLSPDQ GPAIVSGKPW
     NKYSYHPASQ RSPQPPLAKH EQRKDPIKKT KHLRLPQPSE VVHFKSGKGD ARTSDSGHHV
     SQSEEQVQVD AEVDPVSAGY PYSQGPEVAS RSFPDNLPRL RFKCPYCTHV VKRKADLKRH
     LRCHTGERPY PCQACGKRFS RLDHLSSHFR TIHQACKLIC RKCKRHVTDL TGQVVQEGTR
     RYRLCNECLT EVGMDSLPAD LETEQHRVSP ADGDKDCRWH LSEEENRSYV EIVEDGSADL
     VIQQVDDSEE EEEKEIKPNI R