FOXA3_RAT
ID FOXA3_RAT Reviewed; 354 AA.
AC P32183;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 155.
DE RecName: Full=Hepatocyte nuclear factor 3-gamma;
DE Short=HNF-3-gamma;
DE Short=HNF-3G;
DE AltName: Full=Forkhead box protein A3;
GN Name=Foxa3; Synonyms=Hnf3g, Tcf-3g, Tcf3g;
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 [MRNA].
RX PubMed=1672118; DOI=10.1101/gad.5.3.416;
RA Lai E., Prezioso V.R., Tao W.F., Chen W.S., Darnell J.E. Jr.;
RT "Hepatocyte nuclear factor 3 alpha belongs to a gene family in mammals that
RT is homologous to the Drosophila homeotic gene fork head.";
RL Genes Dev. 5:416-427(1991).
RN [2]
RP FUNCTION.
RX PubMed=9369482; DOI=10.1021/bi9703249;
RA Lin B., Morris D.W., Chou J.Y.;
RT "The role of HNF1alpha, HNF3gamma, and cyclic AMP in glucose-6-phosphatase
RT gene activation.";
RL Biochemistry 36:14096-14106(1997).
RN [3]
RP STRUCTURE BY NMR OF 107-223.
RX PubMed=8332212; DOI=10.1038/364412a0;
RA Clark K.L., Halay E.D., Lai E., Burley S.K.;
RT "Co-crystal structure of the HNF-3/fork head DNA-recognition motif
RT resembles histone H5.";
RL Nature 364:412-420(1993).
CC -!- FUNCTION: Transcription factor that is thought to act as a 'pioneer'
CC factor opening the compacted chromatin for other proteins through
CC interactions with nucleosomal core histones and thereby replacing
CC linker histones at target enhancer and/or promoter sites (By
CC similarity). Originally described as a transcription activator for a
CC number of liver genes such as AFP, albumin, tyrosine aminotransferase,
CC PEPCK, etc. Interacts with the cis-acting regulatory regions of these
CC genes. Involved in glucose homeostasis. Involved in regulation of
CC neuronal-specific transcription. May be involved in regulation of
CC spermatogenesis (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:9369482}.
CC -!- SUBUNIT: Interacts with FOXA2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Liver.
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DR EMBL; L09648; AAA41339.1; -; mRNA.
DR PIR; S35090; S35090.
DR RefSeq; NP_058773.1; NM_017077.2.
DR AlphaFoldDB; P32183; -.
DR SMR; P32183; -.
DR STRING; 10116.ENSRNOP00000019219; -.
DR PaxDb; P32183; -.
DR GeneID; 25100; -.
DR KEGG; rno:25100; -.
DR CTD; 3171; -.
DR RGD; 2809; Foxa3.
DR eggNOG; KOG3563; Eukaryota.
DR InParanoid; P32183; -.
DR OrthoDB; 1181467at2759; -.
DR PhylomeDB; P32183; -.
DR PRO; PR:P32183; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; IDA:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IEA:InterPro.
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:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0001678; P:cellular glucose homeostasis; ISO:RGD.
DR GO; GO:0009267; P:cellular response to starvation; ISO:RGD.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0070368; P:positive regulation of hepatocyte differentiation; IMP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR CDD; cd00059; FH; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR013638; Fork-head_N.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR018122; TF_fork_head_CS_1.
DR InterPro; IPR030456; TF_fork_head_CS_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00250; Forkhead; 1.
DR Pfam; PF08430; Forkhead_N; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00657; FORK_HEAD_1; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
PE 1: Evidence at protein level;
KW Activator; Chromatin regulator; Developmental protein; Differentiation;
KW DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..354
FT /note="Hepatocyte nuclear factor 3-gamma"
FT /id="PRO_0000091802"
FT DNA_BIND 118..209
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 52..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..75
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 354 AA; 37652 MW; 318B01ECCE7C365C CRC64;
MLGSVKMEAH DLAEWSYYPE AGEVYSPVNP VPTMAPLNSY MSLNPLSSPY PPGGLQASPL
PTGPLAPPAP TAPLGPTFPG LGAGSGTGGS ASGYGAPGPG LVHGKEMAKG YRRPLTHAKP
PYSYISLITM AIQQAPGKML TLSEIYQWIM DLFPYYRENQ QRWQNSIRHS LSFNDCFVKV
ARSPDKPGKG SYWALHPSSG NMFENGCYLR RQKRFKLEEK AKKGNSATSA TRNGTVGSAT
SATTTAATAV TSPAQPQPTP PSEPEAQSGE DVGGLDCASP PSSAPYFTGL ELPGELKLDA
PYNFNHPFSI NNLMSEQTST PSKLDVGFGG YGAESGEPGV YYQSLYSRSL LNAS
