ID   ZN148_BOVIN             Reviewed;         794 AA.
AC   Q3Y4E1;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Zinc finger protein 148;
DE   AltName: Full=Transcription factor ZBP-89;
DE   AltName: Full=Zinc finger DNA-binding protein 89;
GN   Name=ZNF148; Synonyms=ZBP89;
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 [MRNA].
RC   TISSUE=Liver;
RA   Jiang H., Xu Q., Springer L.;
RT   "Cloning and characterization of the bovine ZBP-89 mRNA.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in transcriptional regulation. Represses the
CC       transcription of a number of genes including gastrin, stromelysin and
CC       enolase. Binds to the G-rich box in the enhancer region of these genes
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with HNRNPDL. Interacts with the 5FMC complex; the
CC       interaction requires association with CHTOP. Interacts with CAVIN1.
CC       {ECO:0000250|UniProtKB:Q61624, ECO:0000250|UniProtKB:Q9UQR1}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- PTM: Sumoylated with SUMO2. Desumoylated by SENP3, resulting in the
CC       stimulation of transcription of its target genes (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; DQ162621; AAZ86076.1; -; mRNA.
DR   RefSeq; NP_001028293.1; NM_001033121.1.
DR   AlphaFoldDB; Q3Y4E1; -.
DR   SMR; Q3Y4E1; -.
DR   STRING; 9913.ENSBTAP00000000628; -.
DR   PaxDb; Q3Y4E1; -.
DR   GeneID; 613265; -.
DR   KEGG; bta:613265; -.
DR   CTD; 7707; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; Q3Y4E1; -.
DR   Proteomes; UP000009136; 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   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SUPFAM; SSF57667; SSF57667; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   2: Evidence at transcript level;
KW   Acetylation; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..794
FT                   /note="Zinc finger protein 148"
FT                   /id="PRO_0000247550"
FT   ZN_FING         171..193
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         199..221
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         227..249
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         255..278
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          298..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          775..794
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..338
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        776..794
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61624"
FT   MOD_RES         194
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT   MOD_RES         250
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT   MOD_RES         301
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61624"
FT   MOD_RES         306
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT   MOD_RES         412
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT   MOD_RES         607
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT   MOD_RES         665
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT   MOD_RES         784
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT   CROSSLNK        6
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT   CROSSLNK        88
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT   CROSSLNK        115
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT   CROSSLNK        132
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT   CROSSLNK        291
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT   CROSSLNK        308
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT   CROSSLNK        356
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT   CROSSLNK        356
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT   CROSSLNK        402
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT   CROSSLNK        421
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT   CROSSLNK        424
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQR1"
SQ   SEQUENCE   794 AA;  89003 MW;  7B5C54A7EB4477AE CRC64;
     MNIDDKLEGL FLKCGGIDEM QSSRAMVVMG GVSGQSTVSG ELQESVLQDR SMPHQEILAA
     DEVLQESEMR QQDMISHDEL MVHEETVKND EEQMETHERL PQGLQYALNV PISVKQEITF
     TDVSEQLMRD KKQIREPVDL QKKKKRKQRS PAKILTINED GSLGLKTPKS HVCEHCNAAF
     RTNYHLQRHV FIHTGEKPFQ CSQCDMRFIQ KYLLQRHEKI HTGEKPFRCD ECGMRFIQKY
     HMERHKRTHS GEKPYQCEYC LQYFSRTDRV LKHKRMCHEN HDKKLNRCAI KGGLLTSEED
     SGFSTSPKDN SLPKKKRQKT EKKSSGMDKE SSLDKSDLKK DKNDYLPLYS SSTKVKDEYM
     VAEYAVEMPH SSVGGSHLED ASGEIHPPKL VLKKINSKRS LKQPLEQNQT ISPLSTYEES
     KVSKYAFELV DKQALLDSEG NADIDQVDNL QEGPSKPVHS STNYDDAMQF LKKKRYLQAA
     SNNSREYALN VGTIASQPSV TQAAVASVID ESTTASILDS QALNVEIKSN HDKNVIPDEV
     LQTLLDHYSH KANGQHEISF SVADTEVTSS ISINSSEVPE VTQSENVGSS SQASSSDKAN
     MLQEYSKFLQ QALDRTSQND AYLNSPSLNF VTDNQTLPNQ PAFSSIDKQV YATMPINSFR
     SGMNSPLRTT PDKSHFGLIV GDSQHSFPFS GDETNHASAT STQDFLDQVT SQKKAEAQPV
     HQAYQMSSFE QPFRAPYHGS RAGIATQFST ANGQVNLRGP GTSAEFPEFP LVNVNDNRAG
     MTSSPDATTG QTFG