STF1_HORSE
ID STF1_HORSE Reviewed; 461 AA.
AC Q9GKL2;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Steroidogenic factor 1;
DE Short=SF-1;
DE Short=STF-1;
DE AltName: Full=Nuclear receptor subfamily 5 group A member 1;
GN Name=NR5A1; Synonyms=SF1;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Corpus luteum, and Ovarian follicle;
RX PubMed=11108279; DOI=10.1210/endo.141.12.7808;
RA Boerboom D., Pilon N., Behdjani R., Silversides D.W., Sirois J.;
RT "Expression and regulation of transcripts encoding two members of the NR5A
RT nuclear receptor subfamily of orphan nuclear receptors, steroidogenic
RT factor-1 and NR5A2, in equine ovarian cells during the ovulatory process.";
RL Endocrinology 141:4647-4656(2000).
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 (By similarity). Part of a complex
CC consisting of SFPQ, NONO and NR5A1. Interacts with NR0B2. Interacts
CC with DGKQ and CDK7. Binds to and activated by HIPK3 (By similarity).
CC {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; AF203911; AAG35648.1; -; mRNA.
DR RefSeq; NP_001075320.1; NM_001081851.1.
DR AlphaFoldDB; Q9GKL2; -.
DR SMR; Q9GKL2; -.
DR STRING; 9796.ENSECAP00000011635; -.
DR PaxDb; Q9GKL2; -.
DR GeneID; 100033902; -.
DR KEGG; ecb:100033902; -.
DR CTD; 2516; -.
DR InParanoid; Q9GKL2; -.
DR OrthoDB; 619653at2759; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008585; P:female gonad development; ISS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0007530; P:sex determination; ISS:UniProtKB.
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 Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..461
FT /note="Steroidogenic factor 1"
FT /id="PRO_0000053730"
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..153
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 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"
SQ SEQUENCE 461 AA; 51644 MW; 85909263A89A1A9D CRC64;
MDYSYDEDLD ELCPVCGDKV SGYHYGLLTC ESCKGFFKRT VQNNKHYTCT ESQSCKIDKT
LRKRCPFCRF QKCLTVGMRL EAVRADRMRG GRNKFGPMYK RDRALKQQKK AQIRANGFKL
ETGPPMGVPP PPPPPPDYML PPGLHVPEPK GLASGPPAGP LGDFGAPALP MAVPSTNGPL
AGYLYPAFPG RAIKSEYPEP YASPPQPGPP YGYPEPFSGG PGVPELILQL LQLEPDEDQV
RARIIGCLQE PAKGRPDQPA SFNLLCRMAD QTFISIVDWA RRCMVFKELE VADQMTLLQN
CWSELLVFDH IYRQVQHGKE GSTLLVTGQE VELTTVAAQA GSLLHGLVLR AQELVLQMHA
LQLDRQEFVC LKFLILFSLD VKFLNNHSLV KDAQEKANTA LLDYTLCHYP HCGDKFQQLL
LCLVEVRALS MQAKEYLYHK HLGNEMPRNN LLIEMLQAKQ T
