STF1_RAT
ID STF1_RAT Reviewed; 462 AA.
AC P50569;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Steroidogenic factor 1;
DE Short=SF-1;
DE Short=STF-1;
DE AltName: Full=Adrenal 4-binding protein;
DE AltName: Full=Fushi tarazu factor homolog 1;
DE AltName: Full=Nuclear receptor subfamily 5 group A member 1;
DE AltName: Full=Steroid hormone receptor Ad4BP;
GN Name=Nr5a1; Synonyms=Ftzf1;
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 [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=7706291; DOI=10.1074/jbc.270.13.7453;
RA Nomura M.M.N., Smith J.;
RT "An E box element is required for the expression of the ad4bp gene, a
RT mammalian homologue of ftz-f1 gene, which is essential for adrenal and
RT gonadal development.";
RL J. Biol. Chem. 270:7453-7461(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-293.
RX PubMed=8395654; DOI=10.1210/mend.7.6.8395654;
RA Lynch J.P., Lala D.S., Peluso J.J., Luo W., Parker K.L., White B.A.;
RT "Steroidogenic factor 1, an orphan nuclear receptor, regulates the
RT expression of the rat aromatase gene in gonadal tissues.";
RL Mol. Endocrinol. 7:776-786(1993).
CC -!- FUNCTION: Transcriptional activator. Seems to be essential for sexual
CC differentiation and formation of the primary steroidogenic tissues.
CC Binds to the Ad4 site found in the promoter region of steroidogenic
CC P450 genes such as CYP11A, CYP11B and CYP21B. Also regulates the
CC AMH/Muellerian inhibiting substance gene as well as the AHCH and STAR
CC genes. 5'-YCAAGGYC-3' and 5'-RRAGGTCA-3' are the consensus sequences
CC for the recognition by NR5A1. The SFPQ-NONO-NR5A1 complex binds to the
CC CYP17 promoter and regulates basal and cAMP-dependent transcriptional
CC activity. Binds phosphatidylcholine and phospholipids with a
CC phosphatidylinositol (PI) headgroup, in particular PI(3,4)P2 and
CC PI(3,4,5)P3. Activated by the phosphorylation of NR5A1 by HIPK3 leading
CC to increased steroidogenic gene expression upon cAMP signaling pathway
CC stimulation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds DNA as a monomer (By similarity). Part of a complex
CC consisting of SFPQ, NONO and NR5A1. Interacts with NR0B2, NCOA2 and
CC PPARGC1A. Interacts with DGKQ and CDK7. Binds to and activated by HIPK3
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Acetylation stimulates the transcriptional activity.
CC {ECO:0000250}.
CC -!- PTM: Sumoylation reduces CDK7-mediated phosphorylation on Ser-203.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on Ser-203 by CDK7. This phosphorylation promotes
CC transcriptional activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR5
CC subfamily. {ECO:0000305}.
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DR EMBL; D42156; BAA07722.1; -; Genomic_DNA.
DR PIR; A56120; A56120.
DR RefSeq; NP_001178028.1; NM_001191099.1.
DR AlphaFoldDB; P50569; -.
DR SMR; P50569; -.
DR STRING; 10116.ENSRNOP00000017651; -.
DR PhosphoSitePlus; P50569; -.
DR PaxDb; P50569; -.
DR PRIDE; P50569; -.
DR Ensembl; ENSRNOT00000017651; ENSRNOP00000017651; ENSRNOG00000012682.
DR GeneID; 83826; -.
DR KEGG; rno:83826; -.
DR UCSC; RGD:68350; rat.
DR CTD; 2516; -.
DR RGD; 68350; Nr5a1.
DR eggNOG; KOG4218; Eukaryota.
DR GeneTree; ENSGT00940000153391; -.
DR HOGENOM; CLU_011437_0_0_1; -.
DR InParanoid; P50569; -.
DR OMA; LDYCITA; -.
DR OrthoDB; 619653at2759; -.
DR PhylomeDB; P50569; -.
DR TreeFam; TF350737; -.
DR Reactome; R-RNO-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-RNO-4090294; SUMOylation of intracellular receptors.
DR PRO; PR:P50569; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000012682; Expressed in ovary and 4 other tissues.
DR Genevisible; P50569; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0004879; F:nuclear receptor activity; ISO:RGD.
DR GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030325; P:adrenal gland development; ISO:RGD.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IMP:RGD.
DR GO; GO:0030154; P:cell differentiation; ISO:RGD.
DR GO; GO:0008585; P:female gonad development; IEP:RGD.
DR GO; GO:0042445; P:hormone metabolic process; ISO:RGD.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IDA:RGD.
DR GO; GO:0033327; P:Leydig cell differentiation; IEA:Ensembl.
DR GO; GO:0001553; P:luteinization; ISO:RGD.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; ISO:RGD.
DR GO; GO:0008584; P:male gonad development; ISS:UniProtKB.
DR GO; GO:0030238; P:male sex determination; ISO:RGD.
DR GO; GO:0010259; P:multicellular organism aging; ISO:RGD.
DR GO; GO:2000195; P:negative regulation of female gonad development; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:2000020; P:positive regulation of male gonad development; IMP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0022414; P:reproductive process; ISO:RGD.
DR GO; GO:0097210; P:response to gonadotropin-releasing hormone; IEP:RGD.
DR GO; GO:0060008; P:Sertoli cell differentiation; IEA:Ensembl.
DR GO; GO:0007530; P:sex determination; ISS:UniProtKB.
DR GO; GO:0009888; P:tissue development; ISO:RGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:RGD.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR016355; NR5_fam.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR24086; PTHR24086; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PIRSF; PIRSF002530; Nuc_orph_FTZ-F1; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 3: Inferred from homology;
KW Acetylation; Activator; DNA-binding; Isopeptide bond; Lipid-binding;
KW Metal-binding; Nucleus; Phosphoprotein; Receptor; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..462
FT /note="Steroidogenic factor 1"
FT /id="PRO_0000053734"
FT DOMAIN 223..460
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 10..85
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 13..33
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 49..73
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 117..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..143
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 342
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphocholine"
FT /ligand_id="ChEBI:CHEBI:57643"
FT /evidence="ECO:0000250|UniProtKB:P33242"
FT BINDING 437
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphocholine"
FT /ligand_id="ChEBI:CHEBI:57643"
FT /evidence="ECO:0000250|UniProtKB:P33242"
FT BINDING 441
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphocholine"
FT /ligand_id="ChEBI:CHEBI:57643"
FT /evidence="ECO:0000250|UniProtKB:P33242"
FT MOD_RES 34
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13285"
FT MOD_RES 38
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13285"
FT MOD_RES 72
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13285"
FT MOD_RES 203
FT /note="Phosphoserine; by CDK7"
FT /evidence="ECO:0000250|UniProtKB:Q13285"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 194
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CONFLICT 150
FT /note="K -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 52087 MW; 89963798A66FFE04 CRC64;
MDYSYDEDLD ELCPVCGDKV SGYHYGLLTC ESCKGFFKRT VQNNKHYTCT ESQSCKIDKT
QRKRCPFCRF QKCLTVGMRL EAVRADRMRG GRNKFGPMYK RDRALKQQKK AQIRANGFKL
ETGPPMGVPP PPPPPPDYML PPSLHAPEPK ALVSGPPSGP LGDFGAPSLP MAVPGPHGPL
AGYLYPAFSN RTIKSEYPEP YASPPQQPGP PYSYPEPFSG GPNVPELILQ LLQLEPEEDQ
VRARIVGCLQ EPAKSRPDQP APFSLLCRMA DQTFISIVDW ARRCMVFKEL EVADQMTLLQ
NCWSELLVLD HIYRQVQYGK EDSILLVTGQ EVELSTVAVQ AGSLLHSLVL RAQELVLQLH
ALQLDRQEFV CLKFLILFSL DVKFLNNHSL VKDAQEKANA ALLDYTLCHY PHCGDKFQQL
LLCLVEVRAL SMQAKEYLYH KHLGNEMPRN NLLIEMLQAK QT
