USP_CHOFU
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