Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable 26S proteasome non-ATPase regulatory subunit 3

Gene

Rpn3

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.By similarity

GO - Molecular functioni

  • enzyme regulator activity Source: InterPro
  • zinc ion binding Source: FlyBase

GO - Biological processi

Enzyme and pathway databases

BRENDAi3.4.25.1. 1994.
ReactomeiR-DME-1169091. Activation of NF-kappaB in B cells.
R-DME-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-DME-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-DME-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-DME-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-DME-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-DME-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-DME-195253. Degradation of beta-catenin by the destruction complex.
R-DME-202424. Downstream TCR signaling.
R-DME-2871837. FCERI mediated NF-kB activation.
R-DME-350562. Regulation of ornithine decarboxylase (ODC).
R-DME-446652. Interleukin-1 family signaling.
R-DME-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-DME-4608870. Asymmetric localization of PCP proteins.
R-DME-4641257. Degradation of AXIN.
R-DME-4641258. Degradation of DVL.
R-DME-5358346. Hedgehog ligand biogenesis.
R-DME-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-DME-5607764. CLEC7A (Dectin-1) signaling.
R-DME-5610780. Degradation of GLI1 by the proteasome.
R-DME-5610785. GLI3 is processed to GLI3R by the proteasome.
R-DME-5632684. Hedgehog 'on' state.
R-DME-5658442. Regulation of RAS by GAPs.
R-DME-5676590. NIK-->noncanonical NF-kB signaling.
R-DME-5689603. UCH proteinases.
R-DME-5689880. Ub-specific processing proteases.
R-DME-6798695. Neutrophil degranulation.
R-DME-68949. Orc1 removal from chromatin.
R-DME-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-DME-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-DME-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-DME-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-DME-8941858. Regulation of RUNX3 expression and activity.
R-DME-8948751. Regulation of PTEN stability and activity.
R-DME-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 26S proteasome non-ATPase regulatory subunit 3
Short name:
26S proteasome subunit S3
Alternative name(s):
Diphenol oxidase A2 component
Short name:
DOX-A2
Regulatory particle non-ATPase 3
Gene namesi
Name:Rpn3
Synonyms:Dox-A2
ORF Names:CG42641
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0261396. Rpn3.

Subcellular locationi

Keywords - Cellular componenti

Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001738211 – 494Probable 26S proteasome non-ATPase regulatory subunit 3Add BLAST494

Proteomic databases

PaxDbiP25161.
PRIDEiP25161.

Expressioni

Tissue specificityi

Blood (crystal) cells and cuticle.

Gene expression databases

BgeeiFBgn0261396.
ExpressionAtlasiP25161. differential.
GenevisibleiP25161. DM.

Interactioni

Subunit structurei

The 26S proteasome is composed of a core protease, known as the 20S proteasome, capped at one or both ends by the 19S regulatory complex (RC). The RC is composed of at least 18 different subunits in two subcomplexes, the base and the lid, which form the portions proximal and distal to the 20S proteolytic core, respectively (By similarity).By similarity

Protein-protein interaction databases

BioGridi61163. 21 interactors.
DIPiDIP-18295N.
IntActiP25161. 6 interactors.
MINTiMINT-982894.
STRINGi7227.FBpp0291495.

Structurei

3D structure databases

ProteinModelPortaliP25161.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini319 – 423PCIAdd BLAST105

Sequence similaritiesi

Belongs to the proteasome subunit S3 family.Curated

Phylogenomic databases

eggNOGiKOG2581. Eukaryota.
ENOG410XS40. LUCA.
GeneTreeiENSGT00490000043406.
InParanoidiP25161.
KOiK03033.
OMAiAMRYPPK.
OrthoDBiEOG091G05QN.
PhylomeDBiP25161.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.10. 1 hit.
InterProiView protein in InterPro
IPR013586. 26S_Psome_reg_C.
IPR000717. PCI_dom.
IPR035267. PSMD3.
IPR011990. TPR-like_helical_dom.
IPR011991. WHTH_DNA-bd_dom.
PANTHERiPTHR10758:SF6. PTHR10758:SF6. 1 hit.
PfamiView protein in Pfam
PF01399. PCI. 1 hit.
PF08375. Rpn3_C. 1 hit.
SMARTiView protein in SMART
SM00088. PINT. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.

Sequencei

Sequence statusi: Complete.

P25161-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNATDIGAN DVEMEVDPTA ETLADEKKNQ DVAAVQEIRE QIRQIEKGVA
60 70 80 90 100
SKESRFILRV LRNLPNTRRK LNGVVFRNLA QSIYPAGADR EAAVALMPAV
110 120 130 140 150
EKDATELPDV PKKQVATKAP IAEVDAYFYL LLLVKLIDAS DLKRAGISAD
160 170 180 190 200
ALMAKISIQN RRTLDLIGAK SYFYFSRVAE LKNSLEGIRS FLHARLRTAT
210 220 230 240 250
LRNDFEGQAV LINCLLRNYL HYALYDQADK LVKKSVYPES ASNNEWARFL
260 270 280 290 300
YYLGRIKAAK LEYSDAHKHL VQALRKSPQH AAIGFRQTVQ KLIIVVELLL
310 320 330 340 350
GNIPERVVFR QAGLRQSLGA YFQLTQAVRL GNLKRFGDVV SQYGPKFQLD
360 370 380 390 400
HTFTLIIRLR HNVIKTAIRS IGLSYSRISP QDIAKRLMLD SAEDAEFIVS
410 420 430 440 450
KAIRDGVIEA TLDPAQNFMR SKESTDIYST REPQLAFHER ISFCLNLHNQ
460 470 480 490
SVKAMRYPPK SYGKDLESAE ERREREQQDL ELAKEMAEDD EDGF
Length:494
Mass (Da):56,004
Last modified:May 1, 1992 - v1
Checksum:i8659CBCAFF95B735
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti204D → H in AAL90075 (PubMed:12537569).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63010 Genomic DNA. Translation: AAB00732.1.
AE014134 Genomic DNA. Translation: AAF53749.1.
AY089337 mRNA. Translation: AAL90075.1.
BT044249 mRNA. Translation: ACH92314.1.
PIRiJH0665.
RefSeqiNP_001260557.1. NM_001273628.1.
NP_477300.1. NM_057952.4.
UniGeneiDm.4848.

Genome annotation databases

EnsemblMetazoaiFBtr0302289; FBpp0291495; FBgn0261396.
FBtr0336843; FBpp0307804; FBgn0261396.
GeneIDi35176.
KEGGidme:Dmel_CG42641.

Similar proteinsi

Entry informationi

Entry nameiPSMD3_DROME
AccessioniPrimary (citable) accession number: P25161
Secondary accession number(s): B5RIX5, Q8T460, Q9VJ09
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: September 27, 2017
This is version 155 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Caution

Was originally thought to be the diphenol oxidase A2 component involved in catecholamine metabolism, melanin formation, and sclerotization of the cuticle.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families