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Protein

Proteasome subunit alpha type-5

Gene

Prosalpha5

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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-174113. SCF-beta-TrCP mediated degradation of Emi1.
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-209360. Ubiquitination and proteolysis of phosphorylated CI.
R-DME-209406. Degradation of NF-kappa-B inhibitor, CACT.
R-DME-209461. Ubiquitination and degradation of phosphorylated ARM.
R-DME-216167. Nuclear CI is degraded.
R-DME-2871837. FCERI mediated NF-kB activation.
R-DME-350562. Regulation of ornithine decarboxylase (ODC).
R-DME-432395. Degradation of TIM.
R-DME-432524. Degradation of PER.
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-538848. Degradation of CLK.
R-DME-538864. Degradation of CRY.
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-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:
Proteasome subunit alpha type-5 (EC:3.4.25.1)
Gene namesi
Name:Prosalpha5
Synonyms:ProsMA5
ORF Names:CG10938
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0016697. Prosalpha5.

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_00001241211 – 244Proteasome subunit alpha type-5Add BLAST244

Proteomic databases

PaxDbiQ95083.
PRIDEiQ95083.

Expressioni

Gene expression databases

BgeeiFBgn0016697.
GenevisibleiQ95083. 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).By similarity

Protein-protein interaction databases

BioGridi62645. 38 interactors.
DIPiDIP-19014N.
IntActiQ95083. 9 interactors.
MINTiMINT-966233.
STRINGi7227.FBpp0086066.

Structurei

3D structure databases

ProteinModelPortaliQ95083.
SMRiQ95083.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0176. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00550000074958.
InParanoidiQ95083.
KOiK02729.
OMAiQMGYDRA.
OrthoDBiEOG091G0GX6.
PhylomeDBiQ95083.

Family and domain databases

CDDicd03753. proteasome_alpha_type_5. 1 hit.
Gene3Di3.60.20.10. 1 hit.
InterProiView protein in InterPro
IPR029055. Ntn_hydrolases_N.
IPR023332. Proteasome_alpha-type.
IPR033812. Proteasome_alpha_type_5.
IPR000426. Proteasome_asu_N.
IPR001353. Proteasome_sua/b.
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.

Q95083-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI CTPEGVVLAV
60 70 80 90 100
EKRITSPLMV PSTVEKIVEV DKHIGCATSG LMADARTLIE RARVECQNHW
110 120 130 140 150
FVYNERMSIE SCAQAVSTLA IQFGDSGDSD GAAAMSRPFG VAILFAGIEA
160 170 180 190 200
GQPQLWHMDP SGTFVRHGAK AIGSGSEGAQ QNLQDLFRPD LTLDEAIDIS
210 220 230 240
LNTLKQVMEE KLNSTNVEVM TMTKEREFYM FTKEEVEQHI KNIA
Length:244
Mass (Da):26,884
Last modified:December 8, 2000 - v2
Checksum:iC58F3232A17FB711
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti166R → G in AAB93421 (PubMed:9409776).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U64721 Genomic DNA. Translation: AAB93421.1.
AE013599 Genomic DNA. Translation: AAF57875.1.
AY061404 mRNA. Translation: AAL28952.1.
RefSeqiNP_477202.2. NM_057854.4.
NP_725669.1. NM_166221.4.
UniGeneiDm.3609.

Genome annotation databases

EnsemblMetazoaiFBtr0086910; FBpp0086066; FBgn0016697.
FBtr0086911; FBpp0086067; FBgn0016697.
GeneIDi36951.
KEGGidme:Dmel_CG10938.

Similar proteinsi

Entry informationi

Entry nameiPSA5_DROME
AccessioniPrimary (citable) accession number: Q95083
Secondary accession number(s): Q0E942, Q9V809
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 8, 2000
Last modified: November 22, 2017
This is version 152 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