ID   ZFP1_PONAB              Reviewed;         407 AA.
AC   Q5RC79;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Zinc finger protein 1 homolog;
DE            Short=Zfp-1;
GN   Name=ZFP1;
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:0000250|UniProtKB:P08042}.
CC       Note=Shows widespread expression throughout the nucleus, but appears to
CC       be excluded from nucleoli. {ECO:0000250|UniProtKB:P08042}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; CR858401; CAH90628.1; -; mRNA.
DR   RefSeq; NP_001125340.1; NM_001131868.1.
DR   AlphaFoldDB; Q5RC79; -.
DR   SMR; Q5RC79; -.
DR   STRING; 9601.ENSPPYP00000008529; -.
DR   PRIDE; Q5RC79; -.
DR   GeneID; 100172242; -.
DR   KEGG; pon:100172242; -.
DR   CTD; 162239; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; Q5RC79; -.
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; 6.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 5.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
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..407
FT                   /note="Zinc finger protein 1 homolog"
FT                   /id="PRO_0000047281"
FT   DOMAIN          8..83
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         184..206
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         212..234
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         240..262
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         268..290
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         296..318
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         324..346
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         352..374
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         380..402
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          2..167
FT                   /note="Required for correct nuclear localization and
FT                   exclusion from the nucleoli"
FT                   /evidence="ECO:0000250|UniProtKB:P08042"
FT   REGION          171..404
FT                   /note="Does not affect nuclear localization pattern"
FT                   /evidence="ECO:0000250|UniProtKB:P08042"
FT   CROSSLNK        74
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P2D0"
FT   CROSSLNK        114
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P2D0"
FT   CROSSLNK        145
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P2D0"
SQ   SEQUENCE   407 AA;  47484 MW;  35448BCA98246F25 CRC64;
     MNKSQGSVSF TDVTVDFTQE EWEQLDPSQR ILYMDVMLEN YSNLLSVEVW KADDQMERDH
     RNPDEQARQF LILKNQTPIE ERGDLFGRAL NLNTDFVSLR QVPYKYDLYE KTLKYNSDLL
     NSNRSYAGKQ TDECNEFGKA LLYLKQEKTH GGVEYSEYNK GGKALSHKAA IFKHQKIKNL
     VQPFICTYCD KAFSFKSLLI SHKRIHTGEK PYECNVCKKT FSHKANLIKH QRIHTGEKPF
     ECPECGKAFT HQSNLIVHQR AHMEKKPYEC SECGKTFAQK FELTTHQRIH TGERPYECNE
     CAKTFFKKSN LIIHQKIHTG EKRYECSECG KSFIQNSQLI IHMRTHTGEK PYECTECGKT
     FSQRSTLRLH LRIHTGEKPY ECSECGKAFS RKSRLSVHQR VHIGEKP