ID ZN750_BOVIN Reviewed; 703 AA.
AC A2VDR9;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 28-JAN-2026, entry version 82.
DE RecName: Full=Zinc finger protein 750;
GN Name=ZNF750;
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 skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription factor involved in epidermis differentiation.
CC Required for terminal epidermal differentiation: acts downstream of
CC p63/TP63 and activates expression of late epidermal differentiation
CC genes. Specifically binds to the promoter of KLF4 and promotes its
CC expression (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; BC133373; AAI33374.1; -; mRNA.
DR RefSeq; NP_001075002.1; NM_001081533.1.
DR AlphaFoldDB; A2VDR9; -.
DR SMR; A2VDR9; -.
DR FunCoup; A2VDR9; 64.
DR STRING; 9913.ENSBTAP00000034629; -.
DR GlyGen; A2VDR9; 4 sites.
DR PaxDb; 9913-ENSBTAP00000034629; -.
DR Ensembl; ENSBTAT00000034744.5; ENSBTAP00000034629.2; ENSBTAG00000015406.7.
DR Ensembl; ENSBTAT00090076728; ENSBTAP00090042710; ENSBTAG00090036000.
DR GeneID; 535628; -.
DR KEGG; bta:535628; -.
DR CTD; 79755; -.
DR VEuPathDB; HostDB:ENSBTAG00000015406; -.
DR VGNC; VGNC:37340; ZNF750.
DR eggNOG; ENOG502QU7X; Eukaryota.
DR GeneTree; ENSGT00530000063870; -.
DR HOGENOM; CLU_023455_0_0_1; -.
DR InParanoid; A2VDR9; -.
DR OMA; PSAYDHY; -.
DR OrthoDB; 8933073at2759; -.
DR Reactome; R-BTA-212436; Generic Transcription Pathway.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000015406; Expressed in esophagus and 68 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0008544; P:epidermis development; ISS:UniProtKB.
DR GO; GO:0061436; P:establishment of skin barrier; IEA:Ensembl.
DR GO; GO:0044091; P:membrane biogenesis; IEA:Ensembl.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:2000304; P:positive regulation of ceramide biosynthetic process; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR InterPro; IPR039363; ZNF750.
DR InterPro; IPR039064; ZNF750_Znf.
DR PANTHER; PTHR14678; PROLINE-RICH PROTEIN 35-RELATED; 1.
DR PANTHER; PTHR14678:SF1; ZINC FINGER PROTEIN 750; 1.
DR Pfam; PF15269; zf-C2H2_7; 1.
PE 2: Evidence at transcript level;
KW Activator; Differentiation; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..703
FT /note="Zinc finger protein 750"
FT /id="PRO_0000284952"
FT ZN_FING 25..51
FT /note="CCHC-type"
FT /evidence="ECO:0000250|UniProtKB:Q32MQ0"
FT REGION 60..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..592
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q32MQ0"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q32MQ0"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q32MQ0"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q32MQ0"
SQ SEQUENCE 703 AA; 75167 MW; 621465798EB98152 CRC64;
MSLLKERKPK KPHYIPRPPG KPFKYKCFQC PFTCNEKSHL FNHMKYGLCK NSITLVSEQD
RVPKCSKPNS SDPKQTNQPD PVVKPTSSKP VPSGLSHLDA KLQHSLAKDD IKENLDLHAR
GPHRCLGQKP TPHKEAAPPS PAPEAAVGTQ PVLEGAVRPS AFVPVGEHRL KGQELTETPE
ALALTHAPAK ASSFHTKSAF HAPGYPWRAG SPFLTPEFPH KIPSTKGFGA TSPYVHPSIT
EYPPHFYTEH GLATIYSPYL LAGNSPECDS PLLSVYGAQD QRHFLPHPGP IPKHLNPAPS
TYDHYRFFQQ YHSSLPIPYG FYRPESAFSS YGLRLPPVAG ISRDQSSHLL EEAALGYQAL
SPSKLNSSNS HKKHTELEKQ SPTPEAKEPS KDGQRDTEGT KMSPRAGSAA TGSPGRPSPT
NFTQTSQPCA GLCGLSDAPA SSAPGRIPPP EQGLAAFKPI KKNTEHPHSQ APENRAVSPK
SLEALSTDAP TQLGSLEAAP SSPEDGSRAA PLNLSTKPEA EPAATCSPAH GGFVEPQDAP
LNLSVKDPCN ALTSRPSVCS PPRGAEPAAA PTPSPTQQRE PASSGDGPDP SSVEAPVPSP
TGKAQDIRAA DSDEQKQTAA VALCQLAAYS PGNVEPAAQE PTCRPDAPTP RAPESQEAQC
DLRPKGQKRT SPREVGKGQQ GSKKAKPSDT ARVFTLRKRT RVS
//
