ID   ZN692_BOVIN             Reviewed;         510 AA.
AC   A0JNJ4;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Zinc finger protein 692 {ECO:0000250|UniProtKB:Q9BU19};
DE   AltName: Full=AICAR responsive element binding protein {ECO:0000250|UniProtKB:Q9BU19};
GN   Name=ZNF692 {ECO:0000250|UniProtKB:Q9BU19};
GN   Synonyms=AREBP {ECO:0000250|UniProtKB:Q9BU19},
GN   ZFP692 {ECO:0000250|UniProtKB:Q3U381};
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=Fetal muscle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May act as an transcriptional repressor for PCK1 gene
CC       expression, in turn may participate in the hepatic gluconeogenesis
CC       regulation through the activated AMPK signaling pathway.
CC       {ECO:0000250|UniProtKB:Q9BU19}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BU19}.
CC   -!- PTM: Phosphorylation at Ser-464 results in loss of DNA-binding
CC       activity. {ECO:0000250|UniProtKB:Q9BU19}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; BC126714; AAI26715.1; -; mRNA.
DR   RefSeq; NP_001019667.2; NM_001024496.2.
DR   RefSeq; XP_005209303.1; XM_005209246.3.
DR   AlphaFoldDB; A0JNJ4; -.
DR   SMR; A0JNJ4; -.
DR   STRING; 9913.ENSBTAP00000050696; -.
DR   PaxDb; A0JNJ4; -.
DR   PRIDE; A0JNJ4; -.
DR   GeneID; 507847; -.
DR   KEGG; bta:507847; -.
DR   CTD; 55657; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_045687_1_0_1; -.
DR   InParanoid; A0JNJ4; -.
DR   OrthoDB; 1318335at2759; -.
DR   TreeFam; TF332664; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; 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:0006111; P:regulation of gluconeogenesis; ISS:UniProtKB.
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; 3.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..510
FT                   /note="Zinc finger protein 692"
FT                   /id="PRO_0000278840"
FT   ZN_FING         322..347
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         353..377
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         383..405
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         411..433
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         442..465
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..202
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..301
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BU19"
FT   MOD_RES         225
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BU19"
FT   MOD_RES         464
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BU19"
SQ   SEQUENCE   510 AA;  55474 MW;  3E39A5719020DFD3 CRC64;
     MAASPADASR RRREKRRQLD ARRSKCRIRL GGHMEQWCLL KEQLGFSLHS QLAKFLLDRY
     TSSGCVLCAG PEPVAPKGLQ YLVLLSHAHS RECSLVPGLR GPGGQDGGLV WECSAGHTFS
     WGPSSGPKSP EEPNLTPLPS TDERSWCPEA KSGQEPAGLE SNCDERAQEA RMPRGAGPPP
     ETFPSLGEDG EEEEEDEEEM LSDASPWTYS SSPDDEPDVP KPPPSPVTHA LKDGEIAPAP
     AAVPAPLASP SSSASSLGSG APGPVEVRIQ PELRGTPQAD QQTEPLASPG SQAQSALASA
     WDEDTAQIGP KRIRKAAKRE LLPCDFPGCG RIFSNRQYLN HHKKYQHIHQ KSFSCPEPAC
     GKSFNFKKHL KEHVKLHSDT RDYICEFCAR SFRTSSNLVI HRRIHTGEKP LQCEICGFTC
     RQKASLNWHR RKHAETVAAL RFPCEFCGKR FEKPDSVAAH RSKSHPALLL APQELSGPVE
     SCSSILASAS LGASEGSRST LAPQAPILLP