ID   ZN436_PONAB             Reviewed;         470 AA.
AC   Q5R5Y7;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Zinc finger protein 436;
GN   Name=ZNF436;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-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}.
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DR   EMBL; CR860714; CAH92829.1; -; mRNA.
DR   RefSeq; NP_001126653.1; NM_001133181.1.
DR   AlphaFoldDB; Q5R5Y7; -.
DR   SMR; Q5R5Y7; -.
DR   STRING; 9601.ENSPPYP00000002018; -.
DR   GeneID; 100173652; -.
DR   KEGG; pon:100173652; -.
DR   CTD; 80818; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; Q5R5Y7; -.
DR   OrthoDB; 1318335at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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; 12.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 12.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 6.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
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..470
FT                   /note="Zinc finger protein 436"
FT                   /id="PRO_0000047586"
FT   DOMAIN          14..86
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         138..160
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         166..188
FT                   /note="C2H2-type 2; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         194..216
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         222..244
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         250..272
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         278..300
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         306..328
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         334..356
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         362..384
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         390..412
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         418..440
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         446..468
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          62..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        66
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C0F3"
SQ   SEQUENCE   470 AA;  54334 MW;  A00A80EE26431323 CRC64;
     MAATLLMAGS QAPVTFEDMA MYLTREEWRP LDAAQRDLYR DVMQENYGNV VSLDFEIRSE
     NEVNPKQEIS EDVQFGTTSE RPAENAEENP ESEEGFESGD RSERQWGDLT AEEWVSYPLQ
     QVTDLLVHKE VHTGIRYHIC SHCGKAFSQI SDLNRHQKTH TGDRPYKCYE CGKGFSRSSH
     LIQHQRTYTG ERPYDCNECG KSFGRSSHLI QHQTIHTGEK PHKCNECGKS FCRLSHLIQH
     QRTHSGEKPY ECEECGKSFS RSSHLAQHQR THTGEKPYEC NECGRGFSER SDLIKHYRVH
     TGERPYKCDE CGKNFSQNSD LVRHRRAHTG EKPYHCNECG ENFSRISHLV QHQRTHTGEK
     PYECNACGKS FSRSSHLITH QKIHTGEKPY ECNECWRSFG ERSDLIKHQR THTGEKPYEC
     VQCGKGFTQS SNLITHQRVH TGEKPYECTE CEKSFSRSSA LIKHKRVHTD