ID   STF1_BOVIN              Reviewed;         461 AA.
AC   Q04752;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 184.
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=AD4BP, FTZF1;
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], AND PROTEIN SEQUENCE OF 120-180.
RC   TISSUE=Adrenal cortex;
RX   PubMed=8463279; DOI=10.1016/s0021-9258(18)53202-6;
RA   Honda S., Morohashi K., Nomura M., Takeya H., Kitajima M., Omura T.;
RT   "Ad4BP regulating steroidogenic P-450 gene is a member of steroid hormone
RT   receptor superfamily.";
RL   J. Biol. Chem. 268:7494-7502(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 13-81.
RX   PubMed=1406703; DOI=10.1210/mend.6.8.1406703;
RA   Lala D.S., Rice D.A., Parker K.L.;
RT   "Steroidogenic factor I, a key regulator of steroidogenic enzyme
RT   expression, is the mouse homolog of fushi tarazu-factor I.";
RL   Mol. Endocrinol. 6:1249-1258(1992).
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 phospholipids with a phosphatidylinositol (PI)
CC       headgroup, in particular PI(3,4)P2 and PI(3,4,5)P3. Activated by the
CC       phosphorylation of NR5A1 by HIPK3 leading to increased steroidogenic
CC       gene expression upon cAMP signaling pathway stimulation (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds DNA as a monomer. Part of a complex consisting of SFPQ,
CC       NONO and NR5A1. Interacts with NR0B2. Interacts with DGKQ and CDK7.
CC       Binds to and activated by HIPK3 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q04752; O60869-1: EDF1; Xeno; NbExp=4; IntAct=EBI-850837, EBI-781310;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Adrenal, ovary, testis, placenta, adipocyte, and
CC       brain.
CC   -!- PTM: May be regulated by phosphorylation and dephosphorylation.
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; D13569; BAA02764.1; -; mRNA.
DR   EMBL; S45997; AAB23574.2; -; mRNA.
DR   PIR; A46077; A46077.
DR   RefSeq; NP_776828.1; NM_174403.2.
DR   RefSeq; XP_010808627.1; XM_010810325.2.
DR   AlphaFoldDB; Q04752; -.
DR   SMR; Q04752; -.
DR   IntAct; Q04752; 1.
DR   STRING; 9913.ENSBTAP00000011869; -.
DR   iPTMnet; Q04752; -.
DR   PaxDb; 9913-ENSBTAP00000011869; -.
DR   Ensembl; ENSBTAT00000011869.4; ENSBTAP00000011869.3; ENSBTAG00000009017.4.
DR   GeneID; 281948; -.
DR   KEGG; bta:281948; -.
DR   CTD; 2516; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009017; -.
DR   VGNC; VGNC:32248; NR5A1.
DR   eggNOG; KOG4218; Eukaryota.
DR   GeneTree; ENSGT00940000153391; -.
DR   HOGENOM; CLU_011437_0_0_1; -.
DR   InParanoid; Q04752; -.
DR   OMA; EVTCNNL; -.
DR   OrthoDB; 2968690at2759; -.
DR   TreeFam; TF350737; -.
DR   Reactome; R-BTA-383280; Nuclear Receptor transcription pathway.
DR   Reactome; R-BTA-4090294; SUMOylation of intracellular receptors.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000009017; Expressed in theca cell and 30 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IMP:UniProtKB.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; ISS:HGNC-UCL.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0004879; F:nuclear receptor activity; IEA:Ensembl.
DR   GO; GO:0003707; F:nuclear steroid receptor activity; IDA:UniProtKB.
DR   GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
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; IMP:UniProtKB.
DR   GO; GO:0001222; F:transcription corepressor binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030325; P:adrenal gland development; IEA:Ensembl.
DR   GO; GO:0008585; P:female gonad development; ISS:UniProtKB.
DR   GO; GO:0042445; P:hormone metabolic process; IEA:Ensembl.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0033327; P:Leydig cell differentiation; IEA:Ensembl.
DR   GO; GO:0001553; P:luteinization; IEA:Ensembl.
DR   GO; GO:0051457; P:maintenance of protein location in nucleus; IEA:Ensembl.
DR   GO; GO:0008584; P:male gonad development; ISS:UniProtKB.
DR   GO; GO:0030238; P:male sex determination; IEA:Ensembl.
DR   GO; GO:2000195; P:negative regulation of female gonad development; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:2000020; P:positive regulation of male gonad development; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; IBA:GO_Central.
DR   CDD; cd07167; NR_DBD_Lrh-1_like; 1.
DR   CDD; cd07070; NR_LBD_SF-1; 1.
DR   Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR   Gene3D; 1.10.565.10; Retinoid X Receptor; 1.
DR   InterPro; IPR035500; NHR-like_dom_sf.
DR   InterPro; IPR016355; NR5-like.
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; NUCLEAR RECEPTOR SUBFAMILY 5 GROUP A; 1.
DR   PANTHER; PTHR24086:SF24; STEROIDOGENIC FACTOR 1; 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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1.
DR   PROSITE; PS51843; NR_LBD; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Direct protein sequencing; DNA-binding;
KW   Isopeptide bond; Lipid-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Receptor; Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..461
FT                   /note="Steroidogenic factor 1"
FT                   /id="PRO_0000053728"
FT   DOMAIN          222..459
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          116..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..461
FT                   /note="Important for dimerization"
FT   COMPBIAS        124..140
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         341
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phosphocholine"
FT                   /ligand_id="ChEBI:CHEBI:57643"
FT                   /evidence="ECO:0000250|UniProtKB:P33242"
FT   BINDING         436
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phosphocholine"
FT                   /ligand_id="ChEBI:CHEBI:57643"
FT                   /evidence="ECO:0000250|UniProtKB:P33242"
FT   BINDING         440
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        64..65
FT                   /note="Missing (in Ref. 2; AAB23574)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   461 AA;  51613 MW;  910747C467ABBD6E CRC64;
     MDYSYDEDLD ELCPVCGDKV SGYHYGLLTC ESCKGFFKRT VQNNKHYTCT ESQSCKIDKT
     QRKRCPFCRF QKCLTVGMRL EAVRADRMRG GRNKFGPMYK RDRALKQQKK AQIRANGFKL
     ETGPPVGVPP PPPPPPDYML PHGLHASEPK GLASGPPAGP LGDFGAPALP MAVPSAHGPL
     AGYLYPAFPG RAIKSEYPEP YASPPQPGPP YGYPEPFSGG PGVPELILQL LQLEPDEDQV
     RARIVGCLQE PAKGRPDQPA PFSLLCRMAD QTFISIVDWA RRCMVFKELE VADQMTLLQN
     CWSELLVFDH IYRQIQHGKE GSILLVTGQE VELTTVAAQA GSLLHSLVLR AQELVLQLHA
     LQLDRQEFVC LKFLILFSLD VKFLNNHSLV KEAQEKANAA LLDYTLCHYP HCGDKFQQLL
     LCLVEVRALS MQAKEYLYHK HLGNEMPRNN LLIEMLQAKQ T
//