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Protein

Protein ultraspiracle

Gene

usp

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for ecdysone. May be an important modulator of insect metamorphosis. Plays an important part in embryonic and post-embryonic development. Binds to ecdysone response elements (ECRES) such as in the promoter region of s15 chorion gene.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi104 – 16966Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri104 – 12421NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri140 – 16425NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: FlyBase
  • ecdysteroid hormone receptor activity Source: FlyBase
  • hormone binding Source: FlyBase
  • juvenile hormone binding Source: FlyBase
  • lipid binding Source: FlyBase
  • protein heterodimerization activity Source: FlyBase
  • protein homodimerization activity Source: FlyBase
  • RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding Source: FlyBase
  • transcription regulatory region sequence-specific DNA binding Source: FlyBase
  • zinc ion binding Source: InterPro

GO - Biological processi

  • border follicle cell migration Source: FlyBase
  • cellular response to ecdysone Source: FlyBase
  • dendrite morphogenesis Source: FlyBase
  • ecdysone biosynthetic process Source: FlyBase
  • germ cell development Source: FlyBase
  • metamorphosis Source: CACAO
  • muscle organ development Source: FlyBase
  • mushroom body development Source: FlyBase
  • negative regulation of cell differentiation Source: FlyBase
  • negative regulation of transcription, DNA-templated Source: FlyBase
  • neuron development Source: FlyBase
  • neuron remodeling Source: FlyBase
  • positive regulation of transcription, DNA-templated Source: FlyBase
  • positive regulation of transcription from RNA polymerase II promoter Source: GOC
  • pupariation Source: FlyBase
  • regulation of development, heterochronic Source: FlyBase
  • regulation of glucose metabolic process Source: FlyBase
  • regulation of organ growth Source: FlyBase
  • response to ecdysone Source: FlyBase
  • response to starvation Source: FlyBase
  • transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-DME-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-DME-204174. Regulation of pyruvate dehydrogenase (PDH) complex.
R-DME-381340. Transcriptional regulation of white adipocyte differentiation.
R-DME-383280. Nuclear Receptor transcription pathway.
R-DME-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
R-DME-5362517. Signaling by Retinoic Acid.
SignaLinkiP20153.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein ultraspiracle
Alternative name(s):
Chorion factor 1
Nuclear receptor subfamily 2 group B member 4
XR2C
Gene namesi
Name:usp
Synonyms:Cf1, NR2B4
ORF Names:CG4380
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0003964. usp.

Subcellular locationi

GO - Cellular componenti

  • activator ecdysone receptor complex Source: FlyBase
  • dendrite Source: FlyBase
  • ecdysone receptor holocomplex Source: FlyBase
  • nucleus Source: FlyBase
  • polytene chromosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2366581.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 508508Protein ultraspiraclePRO_0000053582Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP20153.
PRIDEiP20153.

PTM databases

iPTMnetiP20153.

Expressioni

Gene expression databases

BgeeiP20153.
ExpressionAtlasiP20153. differential.
GenevisibleiP20153. DM.

Interactioni

Subunit structurei

Heterodimer of USP and ECR. Only the heterodimer is capable of high-affinity binding to ecdysone.1 Publication

GO - Molecular functioni

  • protein heterodimerization activity Source: FlyBase
  • protein homodimerization activity Source: FlyBase

Protein-protein interaction databases

BioGridi57709. 6 interactions.
DIPiDIP-645N.
IntActiP20153. 3 interactions.
MINTiMINT-824030.
STRINGi7227.FBpp0305937.

Structurei

Secondary structure

1
508
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni105 – 1073Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi118 – 1203Combined sources
Helixi122 – 13413Combined sources
Turni150 – 1523Combined sources
Helixi153 – 1553Combined sources
Helixi157 – 16711Combined sources
Helixi171 – 1733Combined sources
Helixi240 – 25314Combined sources
Helixi272 – 2743Combined sources
Helixi275 – 29723Combined sources
Helixi302 – 3043Combined sources
Helixi307 – 32923Combined sources
Turni330 – 3334Combined sources
Beta strandi363 – 3697Combined sources
Beta strandi371 – 3733Combined sources
Helixi374 – 3807Combined sources
Helixi383 – 39210Combined sources
Helixi394 – 4007Combined sources
Helixi404 – 41512Combined sources
Helixi426 – 44722Combined sources
Helixi454 – 47926Combined sources
Helixi487 – 4959Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HG4X-ray2.40A/B/C/D/E/F230-508[»]
1R0OX-ray2.24A94-179[»]
2HANX-ray1.95A94-179[»]
ProteinModelPortaliP20153.
SMRiP20153. Positions 98-502.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20153.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 103103ModulatingBy similarityAdd
BLAST
Regioni170 – 22354HingeAdd
BLAST
Regioni224 – 508285Ligand-bindingBy similarityAdd
BLAST

Domaini

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri104 – 12421NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri140 – 16425NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
GeneTreeiENSGT00760000118948.
InParanoidiP20153.
KOiK14030.
OMAiMDTKHFL.
OrthoDBiEOG72RMZ5.
PhylomeDBiP20153.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR000003. Retinoid-X_rcpt/HNF4.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00545. RETINOIDXR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20153-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDNCDQDASF RLSHIKEEVK PDISQLNDSN NSSFSPKAES PVPFMQAMSM
60 70 80 90 100
VHVLPGSNSA SSNNNSAGDA QMAQAPNSAG GSAAAAVQQQ YPPNHPLSGS
110 120 130 140 150
KHLCSICGDR ASGKHYGVYS CEGCKGFFKR TVRKDLTYAC RENRNCIIDK
160 170 180 190 200
RQRNRCQYCR YQKCLTCGMK REAVQEERQR GARNAAGRLS ASGGGSSGPG
210 220 230 240 250
SVGGSSSQGG GGGGGVSGGM GSGNGSDDFM TNSVSRDFSI ERIIEAEQRA
260 270 280 290 300
ETQCGDRALT FLRVGPYSTV QPDYKGAVSA LCQVVNKQLF QMVEYARMMP
310 320 330 340 350
HFAQVPLDDQ VILLKAAWIE LLIANVAWCS IVSLDDGGAG GGGGGLGHDG
360 370 380 390 400
SFERRSPGLQ PQQLFLNQSF SYHRNSAIKA GVSAIFDRIL SELSVKMKRL
410 420 430 440 450
NLDRRELSCL KAIILYNPDI RGIKSRAEIE MCREKVYACL DEHCRLEHPG
460 470 480 490 500
DDGRFAQLLL RLPALRSISL KCQDHLFLFR ITSDRPLEEL FLEQLEAPPP

PGLAMKLE
Length:508
Mass (Da):55,244
Last modified:February 1, 1991 - v1
Checksum:i58BA37A9FD9EBE80
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti213 – 2131G → E in CAA36827 (PubMed:2165589).Curated
Sequence conflicti339 – 3391Missing in CAA36827 (PubMed:2165589).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53417 mRNA. Translation: CAA37496.1.
X52591 mRNA. Translation: CAA36827.1.
AE014298 Genomic DNA. Translation: AAF45707.1.
AL031765 Genomic DNA. Translation: CAA21122.1.
AY069393 mRNA. Translation: AAL39538.1.
X53379 mRNA. Translation: CAA37459.1.
PIRiA35872.
T13737.
RefSeqiNP_001259168.1. NM_001272239.2.
NP_476781.1. NM_057433.4.
UniGeneiDm.25.

Genome annotation databases

EnsemblMetazoaiFBtr0070346; FBpp0070332; FBgn0003964.
FBtr0333803; FBpp0305937; FBgn0003964.
GeneIDi31165.
KEGGidme:Dmel_CG4380.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53417 mRNA. Translation: CAA37496.1.
X52591 mRNA. Translation: CAA36827.1.
AE014298 Genomic DNA. Translation: AAF45707.1.
AL031765 Genomic DNA. Translation: CAA21122.1.
AY069393 mRNA. Translation: AAL39538.1.
X53379 mRNA. Translation: CAA37459.1.
PIRiA35872.
T13737.
RefSeqiNP_001259168.1. NM_001272239.2.
NP_476781.1. NM_057433.4.
UniGeneiDm.25.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HG4X-ray2.40A/B/C/D/E/F230-508[»]
1R0OX-ray2.24A94-179[»]
2HANX-ray1.95A94-179[»]
ProteinModelPortaliP20153.
SMRiP20153. Positions 98-502.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi57709. 6 interactions.
DIPiDIP-645N.
IntActiP20153. 3 interactions.
MINTiMINT-824030.
STRINGi7227.FBpp0305937.

Chemistry

ChEMBLiCHEMBL2366581.

PTM databases

iPTMnetiP20153.

Proteomic databases

PaxDbiP20153.
PRIDEiP20153.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070346; FBpp0070332; FBgn0003964.
FBtr0333803; FBpp0305937; FBgn0003964.
GeneIDi31165.
KEGGidme:Dmel_CG4380.

Organism-specific databases

CTDi31165.
FlyBaseiFBgn0003964. usp.

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
GeneTreeiENSGT00760000118948.
InParanoidiP20153.
KOiK14030.
OMAiMDTKHFL.
OrthoDBiEOG72RMZ5.
PhylomeDBiP20153.

Enzyme and pathway databases

ReactomeiR-DME-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-DME-204174. Regulation of pyruvate dehydrogenase (PDH) complex.
R-DME-381340. Transcriptional regulation of white adipocyte differentiation.
R-DME-383280. Nuclear Receptor transcription pathway.
R-DME-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
R-DME-5362517. Signaling by Retinoic Acid.
SignaLinkiP20153.

Miscellaneous databases

EvolutionaryTraceiP20153.
GenomeRNAii31165.
PROiP20153.

Gene expression databases

BgeeiP20153.
ExpressionAtlasiP20153. differential.
GenevisibleiP20153. DM.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR000003. Retinoid-X_rcpt/HNF4.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00545. RETINOIDXR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Relationship between the product of the Drosophila ultraspiracle locus and the vertebrate retinoid X receptor."
    Oro A.E., McKeown M., Evans R.M.
    Nature 347:298-301(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Larva.
  2. "A steroid/thyroid hormone receptor superfamily member in Drosophila melanogaster that shares extensive sequence similarity with a mammalian homologue."
    Henrich V.C., Sliter T.J., Lubahn D.B., Macintyre A., Gilbert L.I.
    Nucleic Acids Res. 18:4143-4148(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Canton-S.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Oregon-R.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  7. "Proteins that bind to Drosophila chorion cis-regulatory elements: a new C2H2 zinc finger protein and a C2C2 steroid receptor-like component."
    Shea M.J., King D.L., Conboy M.J., Mariani B.D., Kafatos F.C.
    Genes Dev. 4:1128-1140(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-294.
    Tissue: Ovary.
  8. "Functional ecdysone receptor is the product of EcR and Ultraspiracle genes."
    Yao T.-P., Froman B.M., Jiang Z., Cherbas L., Chen J.-D., McKeown M.M., Cherbas P., Evans R.M.
    Nature 366:476-479(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  9. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiUSP_DROME
AccessioniPrimary (citable) accession number: P20153
Secondary accession number(s): Q9W535
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 6, 2016
This is version 187 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.