ID   ZNF76_RAT               Reviewed;         568 AA.
AC   B4F7E9;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Zinc finger protein 76;
DE   AltName: Full=Zinc finger protein 523;
GN   Name=Znf76; Synonyms=Zfp523;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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; BC168249; AAI68249.1; -; mRNA.
DR   RefSeq; NP_001128227.1; NM_001134755.1.
DR   AlphaFoldDB; B4F7E9; -.
DR   SMR; B4F7E9; -.
DR   STRING; 10116.ENSRNOP00000000595; -.
DR   PaxDb; B4F7E9; -.
DR   PeptideAtlas; B4F7E9; -.
DR   GeneID; 361809; -.
DR   KEGG; rno:361809; -.
DR   UCSC; RGD:1306239; rat.
DR   CTD; 224656; -.
DR   RGD; 1306239; Zfp523.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; B4F7E9; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; B4F7E9; -.
DR   PRO; PR:B4F7E9; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
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:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 4.
DR   SMART; SM00355; ZnF_C2H2; 7.
DR   SUPFAM; SSF57667; SSF57667; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
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..568
FT                   /note="Zinc finger protein 76"
FT                   /id="PRO_0000353097"
FT   REPEAT          34..45
FT                   /note="1"
FT   REPEAT          62..73
FT                   /note="2"
FT   REPEAT          88..99
FT                   /note="3"
FT   ZN_FING         165..189
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         195..219
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         225..249
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         255..279
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         285..309
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         315..339
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         345..368
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          34..99
FT                   /note="3 X 12 AA approximate repeats"
FT   REGION          365..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        24
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P36508"
SQ   SEQUENCE   568 AA;  61647 MW;  C451DFF75302EE8B CRC64;
     MESLGLQTVT LSDGTTAYVQ QAIKGEKLLE GQVIQLEDGT TAYIHQVTIQ KESFSFEDGQ
     PVQLEDGSMA YIHHTPKEGY DPSALEAVQL EDGSTAYIHH PVSVPPDSTI LAVQTEVGLE
     DLAAEEEEGF GADTVVALEQ YASKVLHDSP ASHNGKGQQV GDRAFRCGYK GCGRLYTTAH
     HLKVHERAHT GDRSYRCDFP SCGKAFATGY GLKSHVRTHT GEKPYKCPEE LCSKAFKTSG
     DLQKHVRTHT GERPFRCPFE GCGRSFTTSN IRKVHVRTHT GERPYTCPEP HCGRGFTSAT
     NYKNHVRIHT GEKPYVCTVP GCGKRFTEYS SLYKHHVVHT HCKPYTCSSC GKTYRQTSTL
     AMHKRSAHGE LEATEESEQA LYEQQQLEAA SAAEESPSPK PTHIAYLSEV KEESSDIPTQ
     VAMVTEEDGA PQVALITQDG TQQVSLSPED LQALGSAISV VTQHRSTTLT IPGHQEELAT
     SGTHTVTMVS ADGTQTQPVT IITSGALVTE DSSVASLHHQ QVALLATANG THIAVQLEDQ
     QTLEEVISVA TSAMQQGAVT LETTESGC