USP_MANSE
ID USP_MANSE Reviewed; 461 AA.
AC P54779;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, 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 Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Sphinginae; Sphingini; Manduca.
OX NCBI_TaxID=7130;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Epidermis;
RX PubMed=9013254; DOI=10.1046/j.1365-2583.1997.00153.x;
RA Jindra M., Huang J.Y., Malone F., Asahina M., Riddiford L.M.;
RT "Identification and mRNA developmental profiles of two ultraspiracle
RT isoforms in the epidermis and wings of Manduca sexta.";
RL Insect Mol. Biol. 6:41-53(1997).
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.
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; U44837; AAB64234.1; -; mRNA.
DR AlphaFoldDB; P54779; -.
DR SMR; P54779; -.
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..461
FT /note="Protein ultraspiracle homolog"
FT /id="PRO_0000053584"
FT DOMAIN 203..452
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 113..185
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 113..133
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 149..173
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..112
FT /note="Modulating"
FT /evidence="ECO:0000250"
FT REGION 26..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..192
FT /note="Hinge"
SQ SEQUENCE 461 AA; 52066 MW; 2FD5318A5E963A55 CRC64;
MSSVAKKDKR TMSVTALINR AWPLTPAPHQ QQSMPSSQPS NFLQPLATPS TTPSVELDIQ
WLNIEPGFMS PMSPPEMKPD TAMLDGLRDD STPPPAFKNY PPNHPLSGSK HLCSICGDRA
SGKHYGVYSC EGCKGFFKRT VRKDLTYACR EDRNCIIDKR QRNRCQYCRY QKCLACGMKR
EAVQEERQRA ARGTEDAHPS SSVQELSIER LLEIESLVAD PPEEFQFLRV GPESGVPAKY
RAPVSSLCQI GNKQIAALVV WARDIPHFGQ LELEDQILLI KNSWNELLLF AIAWRSMEYL
TDERENVDSR STAPPQLMCL MPGMTLHRNS ALQAGVGQIF DRVLSELSLK MRTLRMDQAE
YVALKAIILL NPDVKGLKNK PEVVVLREKM FSCLDEYVRR SRCAEEGRFA ALLLRLPALR
SISLKCFEHL YFFHLVADTS IASYIHDALR NHAPSIDTSI L