ID   ZN136_PONAB             Reviewed;         540 AA.
AC   Q5REK1;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Zinc finger protein 136;
GN   Name=ZNF136;
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=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in transcriptional regulation as a weak
CC       repressor when alone, or a potent one when fused with a heterologous
CC       protein containing a KRAB B-domain. {ECO:0000250}.
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; CR857524; CAH89806.1; -; mRNA.
DR   RefSeq; NP_001124834.1; NM_001131362.2.
DR   AlphaFoldDB; Q5REK1; -.
DR   SMR; Q5REK1; -.
DR   STRING; 9601.ENSPPYP00000010755; -.
DR   GeneID; 100171692; -.
DR   KEGG; pon:100171692; -.
DR   CTD; 7695; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; Q5REK1; -.
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; 7.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 14.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 7.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Repressor; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..540
FT                   /note="Zinc finger protein 136"
FT                   /id="PRO_0000269720"
FT   DOMAIN          4..90
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         140..162
FT                   /note="C2H2-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         168..190
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         196..218
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         224..246
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         252..274
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         280..302
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         308..330
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         336..358
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         364..386
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         392..414
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         420..442
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         448..470
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         476..498
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         504..526
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   MOD_RES         191
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52737"
SQ   SEQUENCE   540 AA;  62785 MW;  467FDDDF374B2176 CRC64;
     MDSVAFEDVD VNFTQEEWAL LDPSQKNLYR DVMWETMRNL ASVGKKWKDQ NIKDHYKHRG
     RNLRSHMLER LYQTKDSSQR GGIFSQFANQ NLSKKIPGVK LCESIVYGEV SMGQSSLNRH
     IKDHSGHEPK KYQEYGEKPD TRNQCWKPFS SHHSFRTHEI IHTGEKLYDC KECGKTFFSL
     KRIRRHIITH SGYTPYKCKV CGKAFDYPSR FRTHERSHTG EKPYECKECG KAFTCITSVR
     RHMIKHTGDG PYKCKVCGKP FHSLSSFQVH ERIHTGEKPF KCKQCGKAFS CSPTLRIHER
     THTGEKPYEC KQCGKAFSYL PSLRLHERIH TGEKPFVCKQ CGKAFRSAST FQIHERTHTG
     EKPYECKECG EAFSCIPSMR RHMIKHTGEG PYKCKVCGKP FHSLSPFRVH ERTHTGEKPY
     VCKHCGKAFV SSTSIRIHER THTGEKPYEC KQCGKAFSYL NSFRTHEMIH TGEKPFECKR
     CGKAFRSSSS FRLHERTHTG QKPYHCKECG KAYSCRASFQ RHMLTHAEDG PPYKCMWESL