ID   ZN397_BOVIN             Reviewed;         534 AA.
AC   Q1LZ87;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Zinc finger protein 397;
GN   Name=ZNF397;
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=Hippocampus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent transcriptional repressor. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; BC116143; AAI16144.1; -; mRNA.
DR   RefSeq; NP_001068730.1; NM_001075262.1.
DR   RefSeq; XP_005224020.1; XM_005223963.3.
DR   AlphaFoldDB; Q1LZ87; -.
DR   SMR; Q1LZ87; -.
DR   PaxDb; Q1LZ87; -.
DR   PRIDE; Q1LZ87; -.
DR   GeneID; 506448; -.
DR   KEGG; bta:506448; -.
DR   CTD; 84307; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_002678_57_1_1; -.
DR   InParanoid; Q1LZ87; -.
DR   OrthoDB; 1318335at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; cd07936; SCAN; 1.
DR   Gene3D; 1.10.4020.10; -; 1.
DR   InterPro; IPR003309; SCAN_dom.
DR   InterPro; IPR038269; SCAN_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF02023; SCAN; 1.
DR   Pfam; PF00096; zf-C2H2; 9.
DR   SMART; SM00431; SCAN; 1.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   SUPFAM; SSF57667; SSF57667; 5.
DR   PROSITE; PS50804; SCAN_BOX; 1.
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; Phosphoprotein;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..534
FT                   /note="Zinc finger protein 397"
FT                   /id="PRO_0000269561"
FT   DOMAIN          50..132
FT                   /note="SCAN box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT   ZN_FING         285..307
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         313..335
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         341..363
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         369..391
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         397..419
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         425..447
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         453..475
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         481..503
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         509..531
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          197..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         31
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NF99"
FT   CROSSLNK        55
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NF99"
FT   CROSSLNK        171
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NF99"
FT   CROSSLNK        202
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NF99"
FT   CROSSLNK        252
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NF99"
SQ   SEQUENCE   534 AA;  61277 MW;  119647F1529CB8C8 CRC64;
     MAVESRAVST PVPQNSQEQE LILVKVEESR SWGQKLKQSG SARSCQELFR QQFRKFCYQE
     TPGPREALGR LQELCYQWLR PELHTKEQIL ELLVLEQFLS ILPEELQIWV QQHSPKNGEE
     AVTLLEDLER EFDDPGQQVP ATPQGPPMPW KDLTCLGAAQ EFTHIQRQPL KKQLKPWEPC
     LPPKSGCENN ESAIKKDISG EKSQRLSQEP SFGGFSEHKS SLEWQQGSAP GETLRRSPSQ
     RASFSPVIFT HKLLANRDHP EPQRNLILST NSVTYQKVPT EERPYRCDIC GHSFKQHSSL
     TQHQRIHTGE KPYKCNQCGK AFSLRSYLII HQRIHSGEKA YECSECGKAF NQSSALIRHR
     KIHTGEKACK CNECGKAFSQ SSYLIIHQRI HTGEKPYECN ECGKTFSQSS KLIRHQRIHT
     GERPYECNEC GKAFRQSSEL ITHQRIHSGE KPYECNECGK AFSLSSNLIR HQRIHSGEEP
     YQCNECGKTF KRSSALVQHQ RIHSGEEAYI CSECGKAFRH RSVLTRHQRV HTVK