ID   FTZF1_BOMMO             Reviewed;         534 AA.
AC   P49867; Q95V56;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   25-MAY-2022, entry version 128.
DE   RecName: Full=Nuclear hormone receptor FTZ-F1;
DE   AltName: Full=BmFTZ-F1;
DE   AltName: Full=Nuclear receptor subfamily 5 group A member 3;
GN   Name=FTZ-F1; Synonyms=NR5A3;
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=C108; TISSUE=Posterior silk gland;
RX   PubMed=8150206; DOI=10.1006/dbio.1994.1099;
RA   Sun G.-C., Hirose S., Ueda H.;
RT   "Intermittent expression of BmFTZ-F1, a member of the nuclear hormone
RT   receptor superfamily during development of the silkworm Bombyx mori.";
RL   Dev. Biol. 162:426-437(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Nistari;
RA   Uhlirova M., Asahina M., Riddiford L.M., Jindra M.;
RT   "Inducible gene expression in transgenic silkmoth.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play an important role in development.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC   -!- TISSUE SPECIFICITY: Present in all tissues examined.
CC   -!- DEVELOPMENTAL STAGE: Expression is intermittent being high during
CC       larval molting and both the larval-pupal and the pupal-adult
CC       transformations.
CC   -!- INDUCTION: By 20-hydroxyecdysone, but is not expressed until the
CC       ecdysteroid titer falls.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR5
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA01745.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; D10953; BAA01745.1; ALT_FRAME; mRNA.
DR   EMBL; AF426830; AAL30663.1; -; mRNA.
DR   RefSeq; NP_001037528.2; NM_001044063.2.
DR   AlphaFoldDB; P49867; -.
DR   SMR; P49867; -.
DR   STRING; 7091.BGIBMGA000716-TA; -.
DR   PRIDE; P49867; -.
DR   GeneID; 693070; -.
DR   KEGG; bmor:693070; -.
DR   CTD; 40045; -.
DR   eggNOG; KOG4218; Eukaryota.
DR   InParanoid; P49867; -.
DR   OrthoDB; 619653at2759; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   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   1: Evidence at protein level;
KW   Activator; Direct protein sequencing; DNA-binding; Metal-binding; Nucleus;
KW   Receptor; Reference proteome; Transcription; Transcription regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..534
FT                   /note="Nuclear hormone receptor FTZ-F1"
FT                   /id="PRO_0000053738"
FT   DOMAIN          299..531
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        86..161
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         89..109
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         125..149
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          227..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..259
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..296
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        244
FT                   /note="G -> R (in Ref. 1; BAA01745)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        477..482
FT                   /note="TLTCYP -> PYLLS (in Ref. 1; BAA01745)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   534 AA;  59616 MW;  2466F81E1425C683 CRC64;
     MHEDAPKMSI AQSLAASTSQ PKGDIVTEIP LEFAMSSMET KSIETTNVEL KITYVDPTTG
     TGGEPGAYLP TAGTVCDQTD TKDVIEELCP VCGDKVSGYH YGLLTCESCK GFFKRTVQNK
     KVYTCVAERA CHIDKTQRKR CPFCRFQKCL DVGMKLEAVR ADRMRGGRNK FGPMYKRDRA
     RKLQMMRQRQ IAVQTLRGSL GDGGLVLGFG SPYTAVSVKQ EIQIPQVSSL TSSPESSPGP
     ALLGAQPQPP QPPPPPTHDK WEAHSPHSAS PDAFTFDTQS NTAATPSSTA EATSTETLRV
     SPMIREFVQT VDDREWQNAL FGLLQSQTYN QCEVDLFELM CKVLDQNLFS QVDWARNTVF
     FKYLKVDDQM KLLQDSWSVM LVLDHLHQRM HNGLPDETTL HNGQKFDLLC LGLLGVPSLA
     DHFNELQNKL AELKFDVPDY ICVKFMLLLN PEVRGIVNVK CVREGYQTVQ AALLDYTLTC
     YPTIQDKFGK LVMVVPEIHA LAARGEEHLY QRHCAGQAPT QTLLMEMLHA KRKS