Swiss-Prot entry

ID   STF1_MOUSE     STANDARD;      PRT;   462 AA.
AC   P33242;
DT   01-FEB-1994 (Rel. 28, Created)
DT   01-OCT-1996 (Rel. 34, Last sequence update)
DT   01-MAY-2005 (Rel. 47, Last annotation update)
DE   Steroidogenic factor 1 (STF-1) (SF-1) (Adrenal 4 binding protein)
DE   (Steroid hormone receptor Ad4BP) (Fushi tarazu factor homolog 1)
DE   (Embryonal LTR binding protein) (ELP) (Embryonal long terminal repeat-
DE   binding protein) (Steroid hydroxylase positive regulator).
GN   Name=Nr5a1; Synonyms=Ftzf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; 
OC   Muridae; Murinae; Mus. 
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 2).
RX   MEDLINE=92186861; PubMed=1545809 [NCBI, ExPASy, EBI, Israel, Japan];
RA   Tsukiyama T., Ueda H., Hirose S., Niwa O.;
RT   "Embryonal long terminal repeat-binding protein is a murine homolog of
RT   FTZ-F1, a member of the steroid receptor superfamily.";
RL   Mol. Cell. Biol. 12:1286-1291(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Embryonic carcinoma;
RX   MEDLINE=94019394; PubMed=8413309 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1210/me.7.7.852;
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
RT   regulator of steroid hydroxylase gene expression.";
RL   Mol. Endocrinol. 7:852-860(1993).
RN   [3]
RP   SUBUNITS.
RX   MEDLINE=93361012; PubMed=8395013 [NCBI, ExPASy, EBI, Israel, Japan];
RA   Wilson T.E., Fahrner T.J., Milbrandt J.;
RT   "The orphan receptors NGFI-B and steroidogenic factor 1 establish
RT   monomer binding as a third paradigm of nuclear receptor-DNA
RT   interaction.";
RL   Mol. Cell. Biol. 13:5794-5804(1993).
CC   -!- FUNCTION: Seems to be essential for sexual differentiation and
CC       formation of the primary steroidogenic tissues. Binds to the Ad4
CC       site found in the promoter region of steroidogenic P-450 genes
CC       such as CYP11A, CYP11B and CYP21B. Also regulates the Muellerian
CC       inhibiting substance (AMH) gene as well as the AHCH and STAR
CC       genes. Transcription repressor of the Moloney leukemia virus long
CC       terminal repeat in undifferentiated murine embryonal carcinoma
CC       cells. It binds the sequence element 5'-TCAAGGTCA-3'.
CC   -!- SUBUNIT: Binds DNA as a monomer.
CC   -!- SUBCELLULAR LOCATION: Nuclear.
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   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR5
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; D10584; BAA01441.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; S65878; AAB28338.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; S65875; AAB28338.1; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; S65919; AAB28338.1; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; S65876; AAB28338.1; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; S65877; AAB28338.1; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; S65876; AAB28339.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; S65875; AAB28339.1; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; S65919; AAB28339.1; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   PIR; A40716; A40716.
DR   HSSP; P03372; 1HCQ. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   TRANSFAC; T00251; -.
DR   TRANSFAC; T01147; -.
DR   Ensembl; ENSMUSG00000026751; Mus_musculus
DR   MGD; MGI:1346833; Nr5a1.
DR   GeneLynx; Nr5a1..
DR   SOURCE; Nr5a1..
DR   GO; GO:0005634; C:nucleus; IDA.
DR   GO; GO:0003677; F:DNA binding; IDA.
DR   GO; GO:0005515; F:protein binding; IPI.
DR   GO; GO:0016563; F:transcriptional activator activity; IDA.
DR   GO; GO:0001553; P:luteinization; IMP.
DR   GO; GO:0008584; P:male gonad development; IMP.
DR   GO; GO:0045944; P:positive regulation of transcription from P...; IDA.
DR   InterPro; IPR000536; Hrmon_recept_lig.
DR   InterPro; IPR001723; Stdhrmn_receptor.
DR   InterPro; IPR008946; Str_ncl_receptor.
DR   InterPro; IPR000324; VitD_receptor.
DR   InterPro; IPR001628; Znf_C4steroid.
DR   InterPro; Graphical view of domain structure.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   Pfam; Graphical view of domain structure.
DR   PRINTS; PR00398; STRDHORMONER.
DR   PRINTS; PR00047; STROIDFINGER.
DR   PRINTS; PR00350; VITAMINDR.
DR   ProDom; PD000035; Znf_C4steroid; 1.
DR   ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR   SMART; SM00430; HOLI; 1.
DR   SMART; SM00399; ZnF_C4; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR   CMR; P33242.
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; P33242.
DR   ProtoNet; P33242.
DR   ProtoMap; P33242.
DR   PRESAGE; P33242.
DR   DIP; P33242.
DR   ModBase; P33242.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   Alternative splicing; DNA-binding; Nuclear protein; Receptor;
KW   Repressor; Transcription; Transcription regulation; Zinc-finger.
FT   DNA_BIND     10     85       Nuclear receptor-type.
FT   ZN_FING      13     33       C4-type.
FT   ZN_FING      49     73       C4-type.
FT   DOMAIN      267    309       Ligand-binding (Potential).
FT   VARSPLIC    333    462       ELSTVAVQAGSLLHSLVLRAQELVLQLHALQLDRQEFVCLK
FT                                FLILFSLDVKFLNNHSLVKDAQEKANAALLDYTLCHYPHCG
FT                                DKFQQLLLCLVEVRALSMQAKEYLYHKHLGNEMPRNNLLIE
FT                                MLQAKQT -> TELVKPLVLHNPRPLRADSGHPKFQIQGHA
FT                                LARLLCVLGPFEEPQCGMVSGSSYRR (in isoform
FT                                2).
FT                                /FTId=VSP_003715.
FT   CONFLICT    164    164       I -> F (in Ref. 2).
FT   CONFLICT    172    172       S -> A (in Ref. 2).
FT   CONFLICT    256    256       G -> R (in Ref. 2).
FT   CONFLICT    328    328       S -> T (in Ref. 2).
SQ   SEQUENCE   462 AA;  51946 MW;  CA27CA6CABC0213A CRC64;
     MDYSYDEDLD ELCPVCGDKV SGYHYGLLTC ESCKGFFKRT VQNNKHYTCT ESQSCKIDKT
     QRKRCPFCRF QKCLTVGMRL EAVRADRMRG GRNKFGPMYK RDRALKQQKK AQIRANGFKL
     ETGPPMGVPP PPPPPPDYML PPSLHAPEPK ALVSGPPSGP LGDIGAPSLP MSVPGPHGPL
     AGYLYPAFSN RTIKSEYPEP YASPPQQPGP PYSYPEPFSG GPNVPELILQ LLQLEPEEDQ
     VRARIVGCLQ EPAKSGSDQP APFSLLCRMA DQTFISIVDW ARRCMVFKEL EVADQMTLLQ
     NCWSELLVLD HIYRQVQYGK EDSILLVSGQ EVELSTVAVQ AGSLLHSLVL RAQELVLQLH
     ALQLDRQEFV CLKFLILFSL DVKFLNNHSL VKDAQEKANA ALLDYTLCHY PHCGDKFQQL
     LLCLVEVRAL SMQAKEYLYH KHLGNEMPRN NLLIEMLQAK QT
//