ID   HINFP_BOVIN             Reviewed;         516 AA.
AC   Q2TBP2;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Histone H4 transcription factor;
DE   AltName: Full=Histone nuclear factor P;
DE            Short=HiNF-P;
DE   AltName: Full=MBD2-interacting zinc finger protein;
DE   AltName: Full=Methyl-CpG-binding protein 2-interacting zinc finger protein;
GN   Name=HINFP; Synonyms=MIZF;
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=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcriptional repressor that binds to the consensus
CC       sequence 5'-CGGACGTT-3' and to the RB1 promoter. Transcriptional
CC       activator that promotes histone H4 gene transcription at the G1/S phase
CC       transition in conjunction with NPAT. Also activates transcription of
CC       the ATM and PRKDC genes. Autoregulates its expression by associating
CC       with its own promoter (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds MBD2 and a histone deacetylase complex. Interacts with
CC       NPAT (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Associated with
CC       discrete nuclear foci. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated. Ubiquitination may lead to proteasome-mediated
CC       degradation (By similarity). {ECO:0000250}.
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DR   EMBL; BC109865; AAI09866.1; -; mRNA.
DR   RefSeq; NP_001033620.1; NM_001038531.2.
DR   AlphaFoldDB; Q2TBP2; -.
DR   STRING; 9913.ENSBTAP00000019990; -.
DR   PaxDb; Q2TBP2; -.
DR   PRIDE; Q2TBP2; -.
DR   GeneID; 511965; -.
DR   KEGG; bta:511965; -.
DR   CTD; 25988; -.
DR   eggNOG; KOG3608; Eukaryota.
DR   InParanoid; Q2TBP2; -.
DR   OrthoDB; 1318335at2759; -.
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; 2.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   SUPFAM; SSF57667; SSF57667; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..516
FT                   /note="Histone H4 transcription factor"
FT                   /id="PRO_0000281105"
FT   ZN_FING         15..39
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         127..151
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         167..191
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         197..219
FT                   /note="C2H2-type 4; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         227..249
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         253..276
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         282..304
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         310..335
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         343..366
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          371..516
FT                   /note="Interaction with NPAT"
FT                   /evidence="ECO:0000250"
FT   REGION          372..405
FT                   /note="Required for activation of histone H4 transcription
FT                   and contributes to DNA-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          429..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   516 AA;  59256 MW;  19AEA2148217DDC5 CRC64;
     MPPPGKVPRK ENLGLQCEWG SCSFVCSAME EFCEHVTQHL QQHLQGSGEE EEEEEDLLEE
     EFSCLWRECG FCSPDNSADL IRHVYFHCYH TKLKQWGLQA LQSQADLSPC ILDFQSRNLI
     PDIPDHFLCL WEHCENSFDN PEWFYRHVEA HSQCCEYQVV GKDNNVVLCG WKGCTCTFKD
     RFKLREHLRS HTQEKVVACP TCGGMFANNT KFLDHIRRQS SLDQQHFQCS HCSKRFATER
     LLRDHMRNHV NHYKCPLCDM TCPLPSSLRN HMRFRHSEAR PFKCDCCDYS CKNLIDLRKH
     LDTHSKEPAY SCDFENCTFS ARSLYSIKSH YRKVHEGDSE PRYRCHVCDK CFTRGNNLTV
     HLRKKHQFKW PSGHPRFRYK EHEDGYMRLQ LVRYESVELT QQLLRQPQEG SGLGASLNES
     SLQDIILETV PGEPGPQEEA EEEGGGGEGI ALPASQGTSS PIIHVVNQTN AQGEREVVYY
     VLFEAPGEPP PASEPPSGGV MGELQGAAEE PEVQMV