ID   ZBT32_PANTR             Reviewed;         487 AA.
AC   A2T7E6;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   02-JUN-2021, entry version 76.
DE   RecName: Full=Zinc finger and BTB domain-containing protein 32;
GN   Name=ZBTB32;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Nickel G.C., Tefft D.L., Trevarthen K., Funt J., Adams M.D.;
RT   "Positive selection in transcription factor genes on the human lineage.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-binding protein that binds to the to a 5'-TGTACAGTGT-3'
CC       core sequence. May function as a transcriptional transactivator and
CC       transcriptional repressor. Probably exerts its repressor effect by
CC       preventing GATA3 from binding to DNA. May play a role in regulating the
CC       differentiation and activation of helper T-cells (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer (via PTB domain). Interacts with the N-terminal of
CC       FANCC. Interacts with ZBTB16. Interacts with GATA3 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Located in nuclear
CC       speckles. {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal zinc finger domain functions as a
CC       transcriptional transactivator. {ECO:0000250}.
CC   -!- DOMAIN: The BTB (POZ) domain possesses repressor activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; DQ977432; ABM92101.1; -; Genomic_DNA.
DR   BMRB; A2T7E6; -.
DR   STRING; 9598.ENSPTRP00000018588; -.
DR   PaxDb; A2T7E6; -.
DR   PRIDE; A2T7E6; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; A2T7E6; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion 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; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 3.
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; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..487
FT                   /note="Zinc finger and BTB domain-containing protein 32"
FT                   /id="PRO_0000285479"
FT   DOMAIN          29..87
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   ZN_FING         373..395
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         401..423
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         428..450
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          113..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          468..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   487 AA;  52970 MW;  12F890D5B770443F CRC64;
     MSLPPIRLPS PYGSDRLVQL AARLRPALCD TLITVGGQEF PAHSLVLAGV SQQLGRRGQW
     ALGEGISPST FAQLLNFVYG ESVELQPREL RPLQEAARAL GVQSLEEACW RARGDRAKKP
     DPGLKKHQEE PEKPSRNAER ELGDPGEKQK PEQVSRTGGR EQEMLHKHSP PRGSPEMAGA
     TQEAQQEQTR SKEKHLQAPV GQRGADGKHG VLMWLRENPG GSEESLHKLP GPLPPAGSLQ
     TSVTPRPSWA EAPWLVGGQP ALWSILLMPP RYGIPFYHST PTTGAWQEVW REHRIPLSLN
     APKGLWSQNQ LASSSPTPGS LPQGPAQLSP GEMEESDQGH TGALATCAGH EDKAGCPPRP
     HPPPAPPARS RPYACSVCGK RFSLKHQMET HYRVHTGEKP FSCSLCPQRS RDFSAMTKHL
     RTHGAAPYRX XLCGAGCPSL ASMQAHMRGH SPSQLPPGWT IRSTFLYSSS RPSRPSTSPC
     CPSSSTT