ID   ZN566_PANTR             Reviewed;         418 AA.
AC   Q6J6I6;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Zinc finger protein 566;
GN   Name=ZNF566;
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 [MRNA].
RA   Zhong C., Zhou G., Yu L.;
RT   "Cloning of a novel chimpanzee ZNF566 gene.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY589491; AAT41869.1; -; mRNA.
DR   RefSeq; NP_001009089.1; NM_001009089.1.
DR   RefSeq; XP_009433640.1; XM_009435365.2.
DR   AlphaFoldDB; Q6J6I6; -.
DR   SMR; Q6J6I6; -.
DR   STRING; 9598.ENSPTRP00000018667; -.
DR   PaxDb; Q6J6I6; -.
DR   GeneID; 455988; -.
DR   KEGG; ptr:455988; -.
DR   CTD; 84924; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; Q6J6I6; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF00096; zf-C2H2; 4.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 7.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 5.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE   2: Evidence at transcript level;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..418
FT                   /note="Zinc finger protein 566"
FT                   /id="PRO_0000047657"
FT   DOMAIN          6..77
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         169..193
FT                   /note="C2H2-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         199..221
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         227..249
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         255..277
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         283..305
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         311..333
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         339..361
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         367..389
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   CROSSLNK        314
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q969W8"
FT   CROSSLNK        328
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q969W8"
SQ   SEQUENCE   418 AA;  49216 MW;  F94A54491AB7BF7F CRC64;
     MAQESVMFSD VSVDFSQEEW ECLNDDQRDL YRDVMLENYS NLVSMGHSIS KPNVISYLEQ
     GKEPWLVDRE LTRGQWPVLE SRCETKKLFL KKEIYEIEST QWEIMEKLTR HDFQCSSFRD
     DWECNRQFKK ELGSQGGHFN QLVFTHEDLP TLSHHPSFTL QQIINSKKKF CASKEYRKTF
     RHGSQFATHE IIHTTEKPYE CKECGKSFRH PSRLTHHQKI HTGKKPFECK ECGKTFICGS
     DLTRHHRIHT GEKPYECKEC GKAFSSGSNF TRHQRIHTGE KPYECKECGK AFSSGSNFTQ
     HQRIHTGEKP YECKECGNAF SQSSQLIKHQ RIHTGEKPYE CKECEKAFRS GSDLTRHQRI
     HTGEKPYECK ICGKAYSQSS QLISHHRIHT SEKPYEYREC GKNFNYDPQL IQHQNLYW