STF1_BOVIN
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 03-AUG-2022, entry version 176.
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; Q04752; -.
DR PRIDE; Q04752; -.
DR Ensembl; ENSBTAT00000011869; ENSBTAP00000011869; ENSBTAG00000009017.
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; LDYCITA; -.
DR OrthoDB; 619653at2759; -.
DR TreeFam; TF350737; -.
DR Reactome; R-BTA-383280; Nuclear Receptor transcription pathway.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000009017; Expressed in theca cell and 30 other 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:0010259; P:multicellular organism aging; 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 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 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
