STF1_PIG
ID STF1_PIG Reviewed; 461 AA.
AC P79387; A2BD07;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 3.
DT 03-AUG-2022, entry version 153.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9724033; DOI=10.1210/endo.139.9.6193;
RA Pilon N., Behdjani R., Daneau I., Lussier J.G., Silversides D.W.;
RT "Porcine steroidogenic factor-1 gene (pSF-1) expression and analysis of
RT embryonic pig gonads during sexual differentiation.";
RL Endocrinology 139:3803-3812(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Large white X Landrace X Duroc;
RX PubMed=17416745; DOI=10.1101/gr.6085507;
RA Mikawa S., Morozumi T., Shimanuki S., Hayashi T., Uenishi H., Domukai M.,
RA Okumura N., Awata T.;
RT "Fine mapping of a swine quantitative trait locus for number of vertebrae
RT and analysis of an orphan nuclear receptor, germ cell nuclear factor
RT (NR6A1).";
RL Genome Res. 17:586-593(2007).
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 {ECO:0000255|PROSITE-ProRule:PRU00407}.
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; U84399; AAC64209.1; -; mRNA.
DR EMBL; AP009124; BAF45331.1; -; Genomic_DNA.
DR RefSeq; NP_999344.1; NM_214179.1.
DR RefSeq; XP_013849311.1; XM_013993857.1.
DR AlphaFoldDB; P79387; -.
DR SMR; P79387; -.
DR STRING; 9823.ENSSSCP00000005989; -.
DR PaxDb; P79387; -.
DR PRIDE; P79387; -.
DR Ensembl; ENSSSCT00000034748; ENSSSCP00000047808; ENSSSCG00000005588.
DR Ensembl; ENSSSCT00015050376; ENSSSCP00015020094; ENSSSCG00015037779.
DR Ensembl; ENSSSCT00025044265; ENSSSCP00025018842; ENSSSCG00025032540.
DR Ensembl; ENSSSCT00030064379; ENSSSCP00030029440; ENSSSCG00030046093.
DR Ensembl; ENSSSCT00035103682; ENSSSCP00035044375; ENSSSCG00035076132.
DR Ensembl; ENSSSCT00040004107; ENSSSCP00040001286; ENSSSCG00040003271.
DR Ensembl; ENSSSCT00045057600; ENSSSCP00045040288; ENSSSCG00045033632.
DR Ensembl; ENSSSCT00055055738; ENSSSCP00055044488; ENSSSCG00055028135.
DR Ensembl; ENSSSCT00060106495; ENSSSCP00060047033; ENSSSCG00060077360.
DR Ensembl; ENSSSCT00065028781; ENSSSCP00065011774; ENSSSCG00065021631.
DR Ensembl; ENSSSCT00070033299; ENSSSCP00070027811; ENSSSCG00070016898.
DR Ensembl; ENSSSCT00070033310; ENSSSCP00070027821; ENSSSCG00070016898.
DR GeneID; 397368; -.
DR KEGG; ssc:397368; -.
DR CTD; 2516; -.
DR VGNC; VGNC:90886; NR5A1.
DR eggNOG; KOG4218; Eukaryota.
DR GeneTree; ENSGT00940000153391; -.
DR InParanoid; P79387; -.
DR OMA; HALAHHI; -.
DR OrthoDB; 619653at2759; -.
DR Proteomes; UP000008227; Chromosome 1.
DR Proteomes; UP000314985; Chromosome 1.
DR Bgee; ENSSSCG00000005588; Expressed in granulosa cell and 6 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:HGNC-UCL.
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: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:0001221; F:transcription coregulator binding; IEA:Ensembl.
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 2: Evidence at transcript level;
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..461
FT /note="Steroidogenic factor 1"
FT /id="PRO_0000053733"
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 119..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..461
FT /note="Important for dimerization"
FT COMPBIAS 125..143
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 4
FT /note="S -> W (in Ref. 1; AAC64209)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="S -> T (in Ref. 1; AAC64209)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="R -> G (in Ref. 1; AAC64209)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="L -> H (in Ref. 1; AAC64209)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 51575 MW; 0F5051A722FF64B2 CRC64;
MDYSYDEDLD ELCPVCGDKV SGYHYGLLTC ESCKGFFKRT VQNNKHYTCT ESQSCKIDKT
QRKRCPFCRF QKCLTVGMRL EAVRADRMRG GRNKFGPMYK RDRALKQQKK AQIRANGFKL
ETGPPMGVAP PPPPPPDYML PPGLHAPEPK GLAAGPPTGP LGDFGAPTLP MAVPSAHGPL
AGYLYPAFPG RAIKSEYPEP YASPPQPGPP YGYPEPFSGG PGVPELIVQL LQLEPDEDQV
RARIVGCLQE PAKGRPDQPA PFSLLCRMAD QTFISIVDWA RRCMVFKELE VADQMTLLQN
CWSELLVFDH IYRQIQHGKE GSILLVTGQE VELTTVAAQA GSLLHGLVLR AQELVLQLHA
LQLDRQEFVC LKFLILFSLD VKFLNNHSLV KDAQEKANAA LLDYTLCHYP HCGDKFQQLL
LCLVEVRALS MQAKEYLYHK HLGNEMPRNN LLIEMLQAKQ T
