STF1_NOTEU
ID STF1_NOTEU Reviewed; 463 AA.
AC Q95L87;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 98.
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 Notamacropus eugenii (Tammar wallaby) (Macropus eugenii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Diprotodontia; Macropodidae; Notamacropus.
OX NCBI_TaxID=9315;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11602358; DOI=10.1016/s0378-1119(01)00677-1;
RA Whitworth D.J., Pask A.J., Shaw G., Marshall Graves J.A., Behringer R.R.,
RA Renfree M.B.;
RT "Characterization of steroidogenic factor 1 during sexual differentiation
RT in a marsupial.";
RL Gene 277:209-219(2001).
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 -!- TISSUE SPECIFICITY: Expressed in the pre-granulosa and Sertoli cells of
CC the ovary and testis, respectively. In the testis it is also present in
CC the interstitial cells. In the adult ovary it is expressed in the
CC interstitial gland, and in the granulosa cells and theca interna of
CC small to medium-sized antral follicles, but is not expressed in large
CC antral follicles. {ECO:0000269|PubMed:11602358}.
CC -!- DEVELOPMENTAL STAGE: Expressed by both ovaries and testes on the day of
CC birth, just prior to the onset of testicular differentiation, until at
CC least 8 days after birth by which time the ovary also has begun to
CC sexually differentiate. {ECO:0000269|PubMed:11602358}.
CC -!- PTM: Acetylation stimulates the transcriptional activity.
CC {ECO:0000250}.
CC -!- PTM: Sumoylation reduces CDK7-mediated phosphorylation on Ser-202.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on Ser-202 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; AF401742; AAK94918.1; -; mRNA.
DR AlphaFoldDB; Q95L87; -.
DR SMR; Q95L87; -.
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; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..463
FT /note="Steroidogenic factor 1"
FT /id="PRO_0000053731"
FT DOMAIN 224..461
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..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..216
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 343
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphocholine"
FT /ligand_id="ChEBI:CHEBI:57643"
FT /evidence="ECO:0000250|UniProtKB:P33242"
FT BINDING 438
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphocholine"
FT /ligand_id="ChEBI:CHEBI:57643"
FT /evidence="ECO:0000250|UniProtKB:P33242"
FT BINDING 442
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 202
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 193
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 463 AA; 51869 MW; 5311B624C76B7E56 CRC64;
MDYSYDEDLD ELCPVCGDKV SGYHYGLLTC ESCKGFFKRT VQNNKHYTCT ESQNCKIDKT
QRKRCPYCRF QKCLTVGMRL EAVRADRMRG GRNKFGPMYK RDRALKQQKK ALIRANGFKL
ETGPSMGPPP QTDYPLAPAL HPGAKGLAPA PPAGPPGDYE RGPYGPPGVP MAVPTHGPLA
GYLYPAFPGR AIKSEYPEPY ASPHEPAPPY GYPEPYPSGP GLPGVPELIL KLLQLEPDEG
QLKARILACL QEPSKGRPDR PTPFGLMCKM ADQTLFSIVE WARSCVVFKE LEVADQMKLL
QNCWSELLVF DHIYRQIQHG KEGSILLVTG QEVDLSTVAA QAGSLLHSLV LRAQDLVQQL
HSLQVDRQEF VCLKFLILFS LDVKFLENHG LAKDAQEKAN SALLEYTMCH YPHCGDKFRQ
LLLRLAEVRS LSMQAEEYLY HKHLGGEVPC NNLLIEMLHA KRT
