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ZN181_PONAB
ID   ZN181_PONAB             Reviewed;         615 AA.
AC   Q5REF1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Zinc finger protein 181;
GN   Name=ZNF181;
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.
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; CR857578; CAH89856.1; -; mRNA.
DR   RefSeq; NP_001124863.1; NM_001131391.1.
DR   AlphaFoldDB; Q5REF1; -.
DR   SMR; Q5REF1; -.
DR   STRING; 9601.ENSPPYP00000011020; -.
DR   GeneID; 100171725; -.
DR   KEGG; pon:100171725; -.
DR   CTD; 339318; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; Q5REF1; -.
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; 10.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 11.
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; 11.
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..615
FT                   /note="Zinc finger protein 181"
FT                   /id="PRO_0000230667"
FT   DOMAIN          48..120
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         281..303
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         309..331
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         337..359
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         365..387
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         393..415
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         421..443
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         449..471
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         477..499
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         505..527
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         533..555
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         561..583
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   CROSSLNK        153
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M3W8"
FT   CROSSLNK        170
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M3W8"
SQ   SEQUENCE   615 AA;  70556 MW;  7B45CBDD3ABCC6D3 CRC64;
     MPQLQYPECY LAPNRCLVSN CGVNKMSNEE LVGQNHGMEG EACTGEDVTF SDVAIDFSHE
     EWGWLNSAQR DLYKDVMVQN YENLVSVAGL SVTKPHVITL LEDGKEPWMM EKKLSKGLIP
     DWESRWENKE LSTKKDIYDE DSPQTVIIEK VVKQSYEFSN SKMNLEYTEK LEGKHGSQVD
     HFRPAILTSR ESPIADSVYK YNIFRSTFHS KSTLSEPQKI SAEGNSYKYD ILKKNLPKKS
     VIKNEKVNGG KKLLNSNKSG AAFSQGKSLA LPQTCNREKI YTCSECGKAF GKQSILNRHW
     RIHTGEKPYE CRECGKTFSH GSSLTRHLIS HSGEKPYKCI ECGKAFSHVS SLTNHQSTHT
     GEKPYECMNC GKSFSRVSHL IEHLRIHTQE KLYECRICGK AFIHRSSLIH HQKIHTGEKP
     YECRECGKAF CCSSHLTRHQ RIHTMEKQYE CNKCLKVFSS LSFLVQHQSI HTEEKPFECQ
     KCRKSFNQLE SLNMHLRNHI RLKPYECSIC GKAFSHRSSL LQHHRIHTGE KPYECIKCGK
     TFSCSSNLTV HQRIHTGEKP YKCNECGKAF SKGSNLTAHQ RVHNGEKPNS VVSVEKPLDH
     MNHYTCEKSY RRETI
 
 
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