STF1_MOUSE
ID STF1_MOUSE Reviewed; 462 AA.
AC P33242; Q812G5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Steroidogenic factor 1;
DE Short=SF-1;
DE Short=STF-1;
DE AltName: Full=Adrenal 4-binding protein;
DE AltName: Full=Embryonal LTR-binding protein;
DE Short=ELP;
DE AltName: Full=Embryonal long terminal repeat-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;
DE AltName: Full=Steroid hydroxylase positive regulator;
GN Name=Nr5a1; Synonyms=Ftzf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=DBA/2J;
RX PubMed=1545809; DOI=10.1128/mcb.12.3.1286-1291.1992;
RA Tsukiyama T., Ueda H., Hirose S., Niwa O.;
RT "Embryonal long terminal repeat-binding protein is a murine homolog of FTZ-
RT F1, a member of the steroid receptor superfamily.";
RL Mol. Cell. Biol. 12:1286-1291(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8413309; DOI=10.1210/mend.7.7.8413309;
RA Ikeda Y., Lala D.S., Luo X., Kim E., Moisan M.P., Parker K.L.;
RT "Characterization of the mouse FTZ-F1 gene, which encodes a key regulator
RT of steroid hydroxylase gene expression.";
RL Mol. Endocrinol. 7:852-860(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-172.
RC STRAIN=C57L/JxA/HeJF1;
RX PubMed=12239114; DOI=10.1210/en.2002-220349;
RA Frigeri C., Tsao J., Cordova M., Schimmer B.P.;
RT "A polymorphic form of steroidogenic factor-1 is associated with
RT adrenocorticotropin resistance in y1 mouse adrenocortical tumor cell
RT mutants.";
RL Endocrinology 143:4031-4037(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP SUBUNIT.
RX PubMed=8395013; DOI=10.1128/mcb.13.9.5794-5804.1993;
RA Wilson T.E., Fahrner T.J., Milbrandt J.;
RT "The orphan receptors NGFI-B and steroidogenic factor 1 establish monomer
RT binding as a third paradigm of nuclear receptor-DNA interaction.";
RL Mol. Cell. Biol. 13:5794-5804(1993).
RN [8]
RP FUNCTION, AND INTERACTION WITH HIPK3.
RX PubMed=17210646; DOI=10.1128/mcb.02253-06;
RA Lan H.-C., Li H.-J., Lin G., Lai P.-Y., Chung B.-C.;
RT "Cyclic AMP stimulates SF-1-dependent CYP11A1 expression through
RT homeodomain-interacting protein kinase 3-mediated Jun N-terminal kinase and
RT c-Jun phosphorylation.";
RL Mol. Cell. Biol. 27:2027-2036(2007).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 219-462 IN COMPLEX WITH NR0B2 AND
RP PHOSPHOLIPID, AND MUTAGENESIS OF ALA-270 AND ARG-314.
RX PubMed=15707893; DOI=10.1016/j.cell.2005.01.024;
RA Krylova I.N., Sablin E.P., Moore J., Xu R.X., Waitt G.M., MacKay J.A.,
RA Juzumiene D., Bynum J.M., Madauss K., Montana V., Lebedeva L., Suzawa M.,
RA Williams J.D., Williams S.P., Guy R.K., Thornton J.W., Fletterick R.J.,
RA Willson T.M., Ingraham H.A.;
RT "Structural analyses reveal phosphatidyl inositols as ligands for the NR5
RT orphan receptors SF-1 and LRH-1.";
RL Cell 120:343-355(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 223-461 IN COMPLEX WITH NR0B2 AND
RP PHOSPHOLIPID, AND MUTAGENESIS OF LEU-345; LEU-348; VAL-349; ALA-352;
RP ALA-434 AND LYS-441.
RX PubMed=15721253; DOI=10.1016/j.molcel.2005.02.002;
RA Li Y., Choi M., Cavey G., Daugherty J., Suino K., Kovach A., Bingham N.C.,
RA Kliewer S.A., Xu H.E.;
RT "Crystallographic identification and functional characterization of
RT phospholipids as ligands for the orphan nuclear receptor steroidogenic
RT factor-1.";
RL Mol. Cell 17:491-502(2005).
RN [11] {ECO:0007744|PDB:3F7D}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 219-462 IN COMPLEX WITH A
RP PHOSPHATIDYLCHOLINE AND PPARGC1A, INTERACTION WITH NCOA2 AND PPARGC1A,
RP FUNCTION, MUTAGENESIS OF ALA-270 AND LEU-345, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18988706; DOI=10.1210/me.2007-0508;
RA Sablin E.P., Blind R.D., Krylova I.N., Ingraham J.G., Cai F.,
RA Williams J.D., Fletterick R.J., Ingraham H.A.;
RT "Structure of SF-1 bound by different phospholipids: evidence for
RT regulatory ligands.";
RL Mol. Endocrinol. 23:25-34(2009).
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 (By similarity). Transcription repressor of the Moloney
CC leukemia virus long terminal repeat in undifferentiated murine
CC embryonal carcinoma cells. Binds phosphatidylcholine and phospholipids
CC with a phosphatidylinositol (PI) headgroup, in particular
CC phosphatidyl(3,4)bisphosphate, phosphatidyl(3,5)bisphosphate and
CC phosphatidyl(3,4,5)triphosphate. Activated by the phosphorylation of
CC NR5A1 by HIPK3 leading to increased steroidogenic gene expression upon
CC cAMP signaling pathway stimulation. {ECO:0000250,
CC ECO:0000269|PubMed:17210646, ECO:0000269|PubMed:18988706}.
CC -!- SUBUNIT: Binds DNA as a monomer (By similarity). Part of a complex
CC consisting of SFPQ, NONO and NR5A1. Interacts with DGKQ and CDK7 (By
CC similarity). Interacts with NR0B2, NCOA2 and PPARGC1A. Binds to and
CC activated by HIPK3. {ECO:0000250, ECO:0000269|PubMed:15707893,
CC ECO:0000269|PubMed:15721253, ECO:0000269|PubMed:17210646,
CC ECO:0000269|PubMed:18988706, ECO:0000269|PubMed:8395013}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P33242-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P33242-2; Sequence=VSP_003715;
CC -!- DEVELOPMENTAL STAGE: Expressed during early embryonic development.
CC Expressed only in undifferentiated embryonal carcinoma cells.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA01441.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D10584; BAA01441.1; ALT_INIT; mRNA.
DR EMBL; S65878; AAB28338.1; -; Genomic_DNA.
DR EMBL; S65875; AAB28338.1; JOINED; Genomic_DNA.
DR EMBL; S65919; AAB28338.1; JOINED; Genomic_DNA.
DR EMBL; S65876; AAB28338.1; JOINED; Genomic_DNA.
DR EMBL; S65877; AAB28338.1; JOINED; Genomic_DNA.
DR EMBL; S65876; AAB28339.1; -; Genomic_DNA.
DR EMBL; S65875; AAB28339.1; JOINED; Genomic_DNA.
DR EMBL; S65919; AAB28339.1; JOINED; Genomic_DNA.
DR EMBL; AF511594; AAM43952.1; -; mRNA.
DR EMBL; AK134378; BAE22121.1; -; mRNA.
DR EMBL; AK144376; BAE25855.1; -; mRNA.
DR EMBL; AL844842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC110476; AAI10477.1; -; mRNA.
DR EMBL; BC110477; AAI10478.1; -; mRNA.
DR CCDS; CCDS16011.1; -. [P33242-1]
DR PIR; A40716; A40716.
DR PIR; A42128; A42128.
DR RefSeq; NP_001303616.1; NM_001316687.1. [P33242-1]
DR RefSeq; NP_620639.1; NM_139051.3. [P33242-1]
DR PDB; 1YMT; X-ray; 1.20 A; A=219-462.
DR PDB; 1YP0; X-ray; 1.50 A; A=223-461.
DR PDB; 2FF0; NMR; -; A=10-111.
DR PDB; 3F7D; X-ray; 2.20 A; A=219-462.
DR PDBsum; 1YMT; -.
DR PDBsum; 1YP0; -.
DR PDBsum; 2FF0; -.
DR PDBsum; 3F7D; -.
DR AlphaFoldDB; P33242; -.
DR SMR; P33242; -.
DR BioGRID; 204975; 16.
DR ELM; P33242; -.
DR IntAct; P33242; 1.
DR STRING; 10090.ENSMUSP00000108504; -.
DR ChEMBL; CHEMBL1764943; -.
DR SwissLipids; SLP:000001543; -.
DR iPTMnet; P33242; -.
DR PhosphoSitePlus; P33242; -.
DR PaxDb; P33242; -.
DR PRIDE; P33242; -.
DR ProteomicsDB; 257089; -. [P33242-1]
DR ProteomicsDB; 257090; -. [P33242-2]
DR Antibodypedia; 16333; 439 antibodies from 35 providers.
DR DNASU; 26423; -.
DR Ensembl; ENSMUST00000028084; ENSMUSP00000028084; ENSMUSG00000026751. [P33242-1]
DR Ensembl; ENSMUST00000112883; ENSMUSP00000108504; ENSMUSG00000026751. [P33242-1]
DR GeneID; 26423; -.
DR KEGG; mmu:26423; -.
DR UCSC; uc008jnr.1; mouse. [P33242-1]
DR UCSC; uc008jnt.1; mouse. [P33242-2]
DR CTD; 2516; -.
DR MGI; MGI:1346833; Nr5a1.
DR VEuPathDB; HostDB:ENSMUSG00000026751; -.
DR eggNOG; KOG4218; Eukaryota.
DR GeneTree; ENSGT00940000153391; -.
DR HOGENOM; CLU_011437_0_0_1; -.
DR InParanoid; P33242; -.
DR OMA; LDYCITA; -.
DR OrthoDB; 619653at2759; -.
DR PhylomeDB; P33242; -.
DR TreeFam; TF350737; -.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-MMU-4090294; SUMOylation of intracellular receptors.
DR BioGRID-ORCS; 26423; 0 hits in 76 CRISPR screens.
DR EvolutionaryTrace; P33242; -.
DR PRO; PR:P33242; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P33242; protein.
DR Bgee; ENSMUSG00000026751; Expressed in Leydig cell region of testis and 68 other tissues.
DR Genevisible; P33242; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0004879; F:nuclear receptor activity; ISO:MGI.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030325; P:adrenal gland development; IMP:MGI.
DR GO; GO:0097720; P:calcineurin-mediated signaling; ISO:MGI.
DR GO; GO:0008585; P:female gonad development; ISS:UniProtKB.
DR GO; GO:0042445; P:hormone metabolic process; IMP:MGI.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; ISO:MGI.
DR GO; GO:0033327; P:Leydig cell differentiation; IGI:MGI.
DR GO; GO:0001553; P:luteinization; IMP:MGI.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IDA:MGI.
DR GO; GO:0008584; P:male gonad development; IMP:MGI.
DR GO; GO:0030238; P:male sex determination; ISO:MGI.
DR GO; GO:0010259; P:multicellular organism aging; IMP:MGI.
DR GO; GO:2000195; P:negative regulation of female gonad development; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:2000020; P:positive regulation of male gonad development; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0022414; P:reproductive process; IMP:MGI.
DR GO; GO:0097210; P:response to gonadotropin-releasing hormone; IEA:Ensembl.
DR GO; GO:0060008; P:Sertoli cell differentiation; IGI:MGI.
DR GO; GO:0007530; P:sex determination; ISS:UniProtKB.
DR GO; GO:0009888; P:tissue development; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR IDEAL; IID50074; -.
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 3D-structure; Acetylation; Activator; Alternative splicing; DNA-binding;
KW Isopeptide bond; Lipid-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Receptor; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..462
FT /note="Steroidogenic factor 1"
FT /id="PRO_0000053732"
FT DOMAIN 223..460
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 117..149
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 342
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphocholine"
FT /ligand_id="ChEBI:CHEBI:57643"
FT /evidence="ECO:0000269|PubMed:18988706"
FT BINDING 437
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphocholine"
FT /ligand_id="ChEBI:CHEBI:57643"
FT /evidence="ECO:0000269|PubMed:18988706"
FT BINDING 441
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphocholine"
FT /ligand_id="ChEBI:CHEBI:57643"
FT /evidence="ECO:0000269|PubMed:18988706"
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 VAR_SEQ 333..462
FT /note="ELSTVAVQAGSLLHSLVLRAQELVLQLHALQLDRQEFVCLKFLILFSLDVKF
FT LNNHSLVKDAQEKANAALLDYTLCHYPHCGDKFQQLLLCLVEVRALSMQAKEYLYHKHL
FT GNEMPRNNLLIEMLQAKQT -> TELVKPLVLHNPRPLRADSGHPKFQIQGHALARLLC
FT VLGPFEEPQCGMVSGSSYRR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1545809"
FT /id="VSP_003715"
FT VARIANT 172
FT /note="A -> S (in strain: C3H/HeJ and DBA/2J; does not
FT change transcriptional activity)"
FT /evidence="ECO:0000269|PubMed:12239114"
FT MUTAGEN 270
FT /note="A->W: Reduced lipid binding and transactivation.
FT Abolishes ligand binding and reduces transactivation; when
FT associated with F-345."
FT /evidence="ECO:0000269|PubMed:15707893,
FT ECO:0000269|PubMed:18988706"
FT MUTAGEN 314
FT /note="R->M: Strongly reduced transactivation."
FT /evidence="ECO:0000269|PubMed:15707893"
FT MUTAGEN 345
FT /note="L->F: Abolishes ligand binding and reduces
FT transactivation; when associated with W-270."
FT /evidence="ECO:0000269|PubMed:15721253,
FT ECO:0000269|PubMed:18988706"
FT MUTAGEN 345
FT /note="L->W: Strongly reduced transactivation."
FT /evidence="ECO:0000269|PubMed:15721253,
FT ECO:0000269|PubMed:18988706"
FT MUTAGEN 348
FT /note="L->W: Strongly reduced transactivation."
FT /evidence="ECO:0000269|PubMed:15721253"
FT MUTAGEN 349
FT /note="V->W: Strongly reduced transactivation."
FT /evidence="ECO:0000269|PubMed:15721253"
FT MUTAGEN 352
FT /note="A->W: Strongly reduced transactivation."
FT /evidence="ECO:0000269|PubMed:15721253"
FT MUTAGEN 434
FT /note="A->W: Strongly reduced transactivation."
FT /evidence="ECO:0000269|PubMed:15721253"
FT MUTAGEN 440
FT /note="H->D: Strongly reduced transactivation; when
FT associated with D-442."
FT MUTAGEN 441
FT /note="K->E: Strongly reduced transactivation."
FT /evidence="ECO:0000269|PubMed:15721253"
FT MUTAGEN 442
FT /note="H->D: Strongly reduced transactivation; when
FT associated with D-440."
FT CONFLICT 164
FT /note="F -> I (in Ref. 1; BAA01441)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="R -> G (in Ref. 1; BAA01441)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="T -> S (in Ref. 1; BAA01441)"
FT /evidence="ECO:0000305"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:2FF0"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2FF0"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:2FF0"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:2FF0"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:2FF0"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:2FF0"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:2FF0"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2FF0"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:2FF0"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:2FF0"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1YMT"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:1YMT"
FT HELIX 238..249
FT /evidence="ECO:0007829|PDB:1YMT"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:1YP0"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:1YP0"
FT HELIX 263..283
FT /evidence="ECO:0007829|PDB:1YMT"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:1YMT"
FT HELIX 292..318
FT /evidence="ECO:0007829|PDB:1YMT"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:1YMT"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:1YMT"
FT HELIX 334..340
FT /evidence="ECO:0007829|PDB:1YMT"
FT HELIX 343..361
FT /evidence="ECO:0007829|PDB:1YMT"
FT HELIX 366..377
FT /evidence="ECO:0007829|PDB:1YMT"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:1YMT"
FT HELIX 388..409
FT /evidence="ECO:0007829|PDB:1YMT"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:3F7D"
FT HELIX 416..443
FT /evidence="ECO:0007829|PDB:1YMT"
FT HELIX 452..458
FT /evidence="ECO:0007829|PDB:1YMT"
SQ SEQUENCE 462 AA; 52077 MW; 67045B563403CF5A CRC64;
MDYSYDEDLD ELCPVCGDKV SGYHYGLLTC ESCKGFFKRT VQNNKHYTCT ESQSCKIDKT
QRKRCPFCRF QKCLTVGMRL EAVRADRMRG GRNKFGPMYK RDRALKQQKK AQIRANGFKL
ETGPPMGVPP PPPPPPDYML PPSLHAPEPK ALVSGPPSGP LGDFGAPSLP MAVPGPHGPL
AGYLYPAFSN RTIKSEYPEP YASPPQQPGP PYSYPEPFSG GPNVPELILQ LLQLEPEEDQ
VRARIVGCLQ EPAKSRSDQP APFSLLCRMA DQTFISIVDW ARRCMVFKEL EVADQMTLLQ
NCWSELLVLD HIYRQVQYGK EDSILLVTGQ EVELSTVAVQ AGSLLHSLVL RAQELVLQLH
ALQLDRQEFV CLKFLILFSL DVKFLNNHSL VKDAQEKANA ALLDYTLCHY PHCGDKFQQL
LLCLVEVRAL SMQAKEYLYH KHLGNEMPRN NLLIEMLQAK QT
