ID   ZN664_PONAB             Reviewed;         261 AA.
AC   Q5RAM9;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Zinc finger protein 664;
GN   Name=ZNF664;
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; CR858986; CAH91181.1; -; mRNA.
DR   RefSeq; NP_001125693.1; NM_001132221.1.
DR   AlphaFoldDB; Q5RAM9; -.
DR   SMR; Q5RAM9; -.
DR   STRING; 9601.ENSPPYP00000005888; -.
DR   GeneID; 100172615; -.
DR   KEGG; pon:100172615; -.
DR   CTD; 144348; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; Q5RAM9; -.
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   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 8.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   SUPFAM; SSF57667; SSF57667; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
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..261
FT                   /note="Zinc finger protein 664"
FT                   /id="PRO_0000296275"
FT   ZN_FING         3..25
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         31..53
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         59..81
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         87..109
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         115..137
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         143..165
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         171..193
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         199..221
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         227..249
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   CROSSLNK        257
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N3J9"
SQ   SEQUENCE   261 AA;  30300 MW;  696BA10383A70B79 CRC64;
     MIYKCPMCRE FFSERADLFM HQKIHTAEKP HKCDKCDKGF FHISELHIHW RDHTGEKVYK
     CDDCGKDFST TTKLNRHKKI HTVEKPYKCY ECGKAFNWSS HLQIHMRVHT GEKPYVCSEC
     GRGFSNSSNL CMHQRVHTGE KPFKCEECGK AFRHTSSLCM HQRVHTGEKL YKCYECGKAF
     SQSSSLCIHQ RVHTGEKPYR CCGCGKAFSQ SSSLCIHQRV HTGEKPFKCD ECGKAFSQST
     SLCIHQRVHT KERNHLKISV I