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ZBT32_PANPA
ID   ZBT32_PANPA             Reviewed;         487 AA.
AC   A1YGK1;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   02-JUN-2021, entry version 58.
DE   RecName: Full=Zinc finger and BTB domain-containing protein 32;
GN   Name=ZBTB32;
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597;
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; DQ977292; ABM54426.1; -; Genomic_DNA.
DR   BMRB; A1YGK1; -.
DR   STRING; 9597.XP_003816184.1; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   Proteomes; UP000240080; 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; 2.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
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_0000285478"
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          111..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        111..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;  52975 MW;  B237D5982C31636E CRC64;
     MSLPPIRLPS PYGXDRLVQL AARLRPALCD TXITVGSQEF PAHSLVLAGV SQQLGRRGQW
     XXGEGISPST FAQLLNFVYG ESVELQPGEL RPLQEAARAL GVQSLEEACW RARGDRAKKP
     DPGLKKHQEE PEKPSRNPER ELGDPGEKQK PEQVSRTGGR EQEMLHKHSP PRGSPEMAGA
     TQEAQQEQTR SKEKHLQAPV GQRGADGKHG VLMWLRENPG GSEESLRKLP GPLPPAGSLQ
     TSVTPRPSWA EAPWLVGGQP ALWSILLMPP RYGIPFYHST PTTGAWQEVW REHRIPLSLN
     APKGLWSQNQ LASSSPTPGS LPQGPAQLSP GEMEESDQGH TGALATCAGH EDKAGCPPRP
     HPPPAPPARS RPYACSVCGK RFSLKHQMET HYRVHTGEKP FSCSLCPQRS RDFSAMTKHL
     RTHGAAPYRC SLCGAGCPSL ASMQAHMRGH SPSQLPPGWT IRSTFLYSSS RPSRPSTSPC
     CPSSSTT
 
 
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