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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)DescriptionActionsGraphical viewLength
DNA bindingi104 – 169Nuclear receptorPROSITE-ProRule annotationAdd BLAST66
Zinc fingeri104 – 124NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri140 – 164NR C4-typePROSITE-ProRule annotationAdd BLAST25

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-383280. Nuclear Receptor transcription pathway.
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 databases

ChEMBLiCHEMBL2366581.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000535821 – 508Protein ultraspiracleAdd BLAST508

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei35Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP20153.
PRIDEiP20153.

PTM databases

iPTMnetiP20153.

Expressioni

Gene expression databases

BgeeiFBgn0003964.
ExpressionAtlasiP20153. baseline.
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 interactors.
DIPiDIP-645N.
IntActiP20153. 3 interactors.
MINTiMINT-824030.
STRINGi7227.FBpp0305937.

Structurei

Secondary structure

1508
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni105 – 107Combined sources3
Beta strandi113 – 115Combined sources3
Beta strandi118 – 120Combined sources3
Helixi122 – 134Combined sources13
Turni150 – 152Combined sources3
Helixi153 – 155Combined sources3
Helixi157 – 167Combined sources11
Helixi171 – 173Combined sources3
Helixi240 – 253Combined sources14
Helixi272 – 274Combined sources3
Helixi275 – 297Combined sources23
Helixi302 – 304Combined sources3
Helixi307 – 329Combined sources23
Turni330 – 333Combined sources4
Beta strandi363 – 369Combined sources7
Beta strandi371 – 373Combined sources3
Helixi374 – 380Combined sources7
Helixi383 – 392Combined sources10
Helixi394 – 400Combined sources7
Helixi404 – 415Combined sources12
Helixi426 – 447Combined sources22
Helixi454 – 479Combined sources26
Helixi487 – 495Combined sources9

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP20153.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 103ModulatingBy similarityAdd BLAST103
Regioni170 – 223HingeAdd BLAST54
Regioni224 – 508Ligand-bindingBy similarityAdd BLAST285

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)DescriptionActionsGraphical viewLength
Zinc fingeri104 – 124NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri140 – 164NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
GeneTreeiENSGT00760000118948.
InParanoidiP20153.
KOiK14030.
OMAiMDTKHFL.
OrthoDBiEOG091G0YX6.
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)DescriptionActionsGraphical viewLength
Sequence conflicti213G → E in CAA36827 (PubMed:2165589).Curated1
Sequence conflicti339Missing in CAA36827 (PubMed:2165589).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HG4X-ray2.40A/B/C/D/E/F230-508[»]
1R0OX-ray2.24A94-179[»]
2HANX-ray1.95A94-179[»]
ProteinModelPortaliP20153.
SMRiP20153.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

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.
OrthoDBiEOG091G0YX6.
PhylomeDBiP20153.

Enzyme and pathway databases

ReactomeiR-DME-383280. Nuclear Receptor transcription pathway.
SignaLinkiP20153.

Miscellaneous databases

EvolutionaryTraceiP20153.
GenomeRNAii31165.
PROiP20153.

Gene expression databases

BgeeiFBgn0003964.
ExpressionAtlasiP20153. baseline.
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...

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: November 30, 2016
This is version 191 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.