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Protein

Proteasome subunit alpha type-4

Gene

Prosalpha3

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

Functioni

The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: FlyBase

Keywordsi

Molecular functionHydrolase, Protease, Threonine protease

Enzyme and pathway databases

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-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-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-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-8939902 Regulation of RUNX2 expression and activity
R-DME-8941858 Regulation of RUNX3 expression and activity
R-DME-8948751 Regulation of PTEN stability and activity
R-DME-9020702 Interleukin-1 signaling
R-DME-983168 Antigen processing: Ubiquitination & Proteasome degradation

Protein family/group databases

MEROPSiT01.973

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-4 (EC:3.4.25.1)
Alternative name(s):
PROS-Dm29
Proteasome 29 kDa subunit
Gene namesi
Name:Prosalpha3
Synonyms:PROS-29, Pros29
ORF Names:CG9327
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0261394 Prosalpha3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001241091 – 264Proteasome subunit alpha type-4Add BLAST264

Proteomic databases

PaxDbiP18053
PRIDEiP18053

Expressioni

Gene expression databases

BgeeiFBgn0261394
GenevisibleiP18053 DM

Interactioni

Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel (By similarity). Interacts with PI31.By similarity1 Publication

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi63019, 41 interactors
DIPiDIP-19125N
IntActiP18053, 15 interactors
STRINGi7227.FBpp0071451

Structurei

3D structure databases

ProteinModelPortaliP18053
SMRiP18053
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0178 Eukaryota
COG0638 LUCA
GeneTreeiENSGT00550000074827
InParanoidiP18053
KOiK02728
OMAiMSKTMDS
OrthoDBiEOG091G0F2L
PhylomeDBiP18053

Family and domain databases

Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR000426 Proteasome_asu_N
IPR016050 Proteasome_bsu_CS
IPR001353 Proteasome_sua/b
IPR034647 Proteasome_subunit_alpha4
PANTHERiPTHR11599:SF13 PTHR11599:SF13, 1 hit
PfamiView protein in Pfam
PF00227 Proteasome, 1 hit
PF10584 Proteasome_A_N, 1 hit
SMARTiView protein in SMART
SM00948 Proteasome_A_N, 1 hit
SUPFAMiSSF56235 SSF56235, 1 hit
PROSITEiView protein in PROSITE
PS00388 PROTEASOME_ALPHA_1, 1 hit
PS51475 PROTEASOME_ALPHA_2, 1 hit

Sequencei

Sequence statusi: Complete.

P18053-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARRYDSRTT IFSPEGRLYQ VEYAMEAISH AGTCLGILAE DGILLAAECR
60 70 80 90 100
STNKLLDSAI PSEKIYRLND NMVCSVAGIT SDANVLTSEL RLIAQRYQFS
110 120 130 140 150
YGEVIPCEQL VSHLCDIKQA YTQYGGKRPF GVSLLYMGWD NKYGYQLYQS
160 170 180 190 200
DPSGNYGGWK ATCIGNNFGA AISMLKQELA DKENVKLTLA DAKDLAIKVL
210 220 230 240 250
SMTLDTTKLT PEKVEMATLQ RVDNKTVYSV LEKPDVEKLI EKYTKVQAEA
260
EAAKKEKQAK QPTK
Length:264
Mass (Da):29,412
Last modified:December 8, 2000 - v2
Checksum:iE5209BC634008B8B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti68L → R in CAA36555 (PubMed:2374736).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52319 mRNA Translation: CAA36555.1
AE013599 Genomic DNA Translation: AAF46651.1
AY084140 mRNA Translation: AAL89878.1
PIRiS10318
RefSeqiNP_476691.1, NM_057343.5
UniGeneiDm.712

Genome annotation databases

EnsemblMetazoaiFBtr0071522; FBpp0071451; FBgn0261394
GeneIDi37378
KEGGidme:Dmel_CG9327

Similar proteinsi

Entry informationi

Entry nameiPSA4_DROME
AccessioniPrimary (citable) accession number: P18053
Secondary accession number(s): Q9W2N9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: December 8, 2000
Last modified: July 18, 2018
This is version 175 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

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