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Protein

Proteasome subunit alpha type-3

Gene

Prosalpha7

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 (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

  • ovarian follicle cell development Source: FlyBase
  • 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-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-432395 Degradation of TIM
R-DME-432524 Degradation of PER
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-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

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-3 (EC:3.4.25.1)
Alternative name(s):
20S proteasome subunit alpha-7
Gene namesi
ORF Names:CG1519
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0023175 Prosalpha7

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_00001240971 – 253Proteasome subunit alpha type-3Add BLAST253

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei248Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9V5C6
PRIDEiQ9V5C6

PTM databases

iPTMnetiQ9V5C6

Expressioni

Gene expression databases

BgeeiFBgn0023175
GenevisibleiQ9V5C6 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 ntc.By similarity1 Publication

Protein-protein interaction databases

BioGridi61847, 49 interactors
DIPiDIP-22157N
IntActiQ9V5C6, 10 interactors
STRINGi7227.FBpp0089041

Structurei

3D structure databases

ProteinModelPortaliQ9V5C6
SMRiQ9V5C6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0184 Eukaryota
ENOG410XP01 LUCA
GeneTreeiENSGT00550000074912
InParanoidiQ9V5C6
KOiK02727
OMAiFELEMTW
OrthoDBiEOG091G0GQL
PhylomeDBiQ9V5C6

Family and domain databases

Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR037555 Proteasome_alpha_3
IPR000426 Proteasome_asu_N
IPR001353 Proteasome_sua/b
PANTHERiPTHR11599:SF10 PTHR11599:SF10, 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.

Q9V5C6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTIGTGYDL SASQFSPDGR VFQIDYASKA VEKSGTVIGI RGKDAVVLAV
60 70 80 90 100
EKIITSKLYE PDAGGRIFTI EKNIGMAVAG LVADGNFVAD IARQEAANYR
110 120 130 140 150
QQFEQAIPLK HLCHRVAGYV HAYTLYSAVR PFGLSIILAS WDEVEGPQLY
160 170 180 190 200
KIEPSGSSFG YFACASGKAK QLAKTEMEKL KMDMRTDELV ESAGEIIYKV
210 220 230 240 250
HDELKDKDFR FEMGLVGRVT GGLHLINPSE LTEKARKAGD AANKDEDSDN

ETH
Length:253
Mass (Da):27,675
Last modified:May 1, 2000 - v1
Checksum:i7B19D8DA350E2B7E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti17P → A in AAB82572 (Ref. 1) Curated1
Sequence conflicti30Missing in AAB82572 (Ref. 1) Curated1
Sequence conflicti62D → H in AAB82572 (Ref. 1) Curated1
Sequence conflicti140 – 157Missing in AAT27293 (Ref. 5) CuratedAdd BLAST18
Sequence conflicti167Missing in AAB82572 (Ref. 1) Curated1
Sequence conflicti182M → T in AAB82572 (Ref. 1) Curated1
Sequence conflicti235 – 253ARKAG…DNETH → DEDTACGQQDEGRRQRQ in AAB82572 (Ref. 1) CuratedAdd BLAST19

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF025793 Genomic DNA Translation: AAB82572.1
AE013599 Genomic DNA Translation: AAF58889.1
AY069616 mRNA Translation: AAL39761.1
BT014669 mRNA Translation: AAT27293.1
RefSeqiNP_724834.1, NM_165703.3
UniGeneiDm.2041

Genome annotation databases

EnsemblMetazoaiFBtr0089998; FBpp0089041; FBgn0023175
GeneIDi36018
KEGGidme:Dmel_CG1519

Similar proteinsi

Entry informationi

Entry nameiPSA3_DROME
AccessioniPrimary (citable) accession number: Q9V5C6
Secondary accession number(s): O17313, Q8MKU6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: May 1, 2000
Last modified: May 23, 2018
This is version 162 of the entry and version 1 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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