ID   USP_CHOFU               Reviewed;         472 AA.
AC   O76202;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Protein ultraspiracle homolog;
DE   AltName: Full=Nuclear receptor subfamily 2 group B member 4;
GN   Name=USP; Synonyms=NR2B4;
OS   Choristoneura fumiferana (Spruce budworm moth) (Archips fumiferana).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Tortricoidea;
OC   Tortricidae; Tortricinae; Choristoneura.
OX   NCBI_TaxID=7141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9581288;
RX   DOI=10.1002/(sici)1520-6408(1998)22:2<169::aid-dvg6>3.0.co;2-4;
RA   Perera S.C., Palli S.R., Ladd T.R., Krell P.J., Retnakaran A.;
RT   "The ultraspiracle gene of the spruce budworm, Choristoneura fumiferana:
RT   cloning of cDNA and developmental expression of mRNA.";
RL   Dev. Genet. 22:169-179(1998).
CC   -!- FUNCTION: Receptor for ecdysone. May be an important modulator of
CC       insect metamorphosis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of USP and ECR. Only the heterodimer is capable of
CC       high-affinity binding to ecdysone (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC       DNA-binding domain and a C-terminal ligand-binding domain.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF016368; AAC31795.1; -; mRNA.
DR   AlphaFoldDB; O76202; -.
DR   SMR; O76202; -.
DR   BindingDB; O76202; -.
DR   ChEMBL; CHEMBL2366580; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0003707; F:nuclear steroid 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; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR   InterPro; IPR000003; Retinoid-X_rcpt/HNF4.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR00545; RETINOIDXR.
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   DNA-binding; Metal-binding; Nucleus; Receptor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..472
FT                   /note="Protein ultraspiracle homolog"
FT                   /id="PRO_0000053585"
FT   DOMAIN          212..462
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        119..191
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         119..139
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         155..179
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..118
FT                   /note="Modulating"
FT                   /evidence="ECO:0000250"
FT   REGION          192..198
FT                   /note="Hinge"
SQ   SEQUENCE   472 AA;  53139 MW;  837F22DCC366C479 CRC64;
     MSSVAKKDKP TMSVTALINW ARPAPPGPPQ PQSASPAPAA MLQQLPTQSM QSLNHIPTVD
     CSLDMQWLNL EPGFMSPMSP PEMKPDTAML DGLRDDATSP PNFKNYPPNH PLSGSKHLCS
     ICGDRASGKH YGVYSCEGCK GFFKRTVRKD LSYACREERN CIIDKRQRNR CQYCRYQKCL
     ACGMKREAVQ EERQRNARGA EDAHPSSSVQ VSDELSIERL TEMESLVADP SEEFQFLRVG
     PDSNVPPRYR APVSSLCQIG NKQIAALVVW ARDIPHFGQL ELDDQVVLIK ASWNELLLFA
     IAWRSMEYLE DERENGDGTR STTQPQLMCL MPGMTLHRNS AQQAGVGAIF DRVLSELSLK
     MRTLRMDQAE YVALKAIVLL NPDVKGLKNR QEVDVLREKM FSCLDDYCRR SRSNEEGRFA
     SLLLRLPALR SISLKSFEHL YFFHLVAEGS ISGYIREALR NHAPPIDVNA MM