ID   ZN181_BOVIN             Reviewed;         570 AA.
AC   Q2KI58;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Zinc finger protein 181;
GN   Name=ZNF181;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Rumen;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) 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}.
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; BC112761; AAI12762.1; -; mRNA.
DR   RefSeq; NP_001070017.1; NM_001076549.1.
DR   AlphaFoldDB; Q2KI58; -.
DR   SMR; Q2KI58; -.
DR   STRING; 9913.ENSBTAP00000054562; -.
DR   PaxDb; Q2KI58; -.
DR   PRIDE; Q2KI58; -.
DR   Ensembl; ENSBTAT00000013039; ENSBTAP00000013039; ENSBTAG00000009889.
DR   GeneID; 767826; -.
DR   KEGG; bta:767826; -.
DR   CTD; 339318; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009889; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000161431; -.
DR   HOGENOM; CLU_002678_44_0_1; -.
DR   InParanoid; Q2KI58; -.
DR   OrthoDB; 1318335at2759; -.
DR   Reactome; R-BTA-212436; Generic Transcription Pathway.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000009889; Expressed in oocyte and 107 other tissues.
DR   ExpressionAtlas; Q2KI58; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; 11.
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..570
FT                   /note="Zinc finger protein 181"
FT                   /id="PRO_0000230665"
FT   DOMAIN          4..75
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         236..258
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         264..286
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         292..314
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         320..342
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         348..370
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         376..398
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         404..426
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         432..454
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         460..482
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         488..510
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         516..538
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   CROSSLNK        125
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M3W8"
SQ   SEQUENCE   570 AA;  65934 MW;  30C864C5F3DBC62F CRC64;
     MFQVTFSDVA IDFSHEEWRW LNSTQRNLYK DVMVQNYENL VSLGLSIPKP YVIALLEDGK
     EPCMVEEKLS KDTFPDCKTR WENKELSMKE DIYDEDLPQM VLKEKTIQQN HEFSNFNKDL
     YYIKKFKGKY ENQVEHFRPV TLTFRESPIG ESVYKCNAFK SIFHLKSVFS EPQRISAEGK
     SHKCDILKKS LPTNSVIKNE NINDGKKLLN SNESVAAFSQ SKSLTLHQTL NKEKIYTCNE
     CGKAFGKQSI LNRHWRIHTG EKPYECHECG KTFSHGSSLT RHQISHSGEK PYKCIECGKA
     FSHVSSLTNH QSTHTGEKPY ECMNCGKAFS RVSHLIEHLR IHTQEKLYEC RICGKAFIHR
     SSLIHHQKIH TGEKPYECRE CGKAFCCSSH LTRHQRIHAI EKQFECNKCL KVFSSLSFLI
     QHQSIHTEEK PFECQKCGKS FNQPESLNMH LRNHTRLKPY ECSICGKAFS HRSSLFQHHR
     IHTGEKPYEC IKCGKTFSCS SNLTVHQRIH TGEKPYKCNE CGKAFSKGSN LTAHQRVHNG
     EKPSSTISVE KSLGHMSHCV YERSHNRETA