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Protein

Proteasome subunit alpha type-7-1A

Gene

Prosalpha4T1

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

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-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-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-7-1A (EC:3.4.25.1)
Alternative name(s):
Testis-specific alpha4-t1 proteasome subunit
Testis-specific proteasome 28 kDa subunit 1A
Gene namesi
Name:Prosalpha4T1
Synonyms:Pros28.1A
ORF Names:CG17268
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0265606. Prosalpha4T1.

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_00001241541 – 249Proteasome subunit alpha type-7-1AAdd BLAST249

Proteomic databases

PaxDbiQ24178.
PRIDEiQ24178.

Expressioni

Tissue specificityi

Testis specific.

Gene expression databases

BgeeiFBgn0265606.
ExpressionAtlasiQ24178. differential.
GenevisibleiQ24178. 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

BioGridi67432. 1 interactor.
DIPiDIP-19969N.
IntActiQ24178. 3 interactors.
MINTiMINT-1548416.
STRINGi7227.FBpp0083336.

Structurei

3D structure databases

ProteinModelPortaliQ24178.
SMRiQ24178.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0183. Eukaryota.
ENOG410XP21. LUCA.
InParanoidiQ24178.
KOiK02731.
OMAiNTVREFF.
OrthoDBiEOG091G0GX6.
PhylomeDBiQ24178.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiView protein in InterPro
IPR029055. Ntn_hydrolases_N.
IPR023332. Proteasome_alpha-type.
IPR035190. Proteasome_alpha7.
IPR000426. Proteasome_asu_N.
IPR001353. Proteasome_sua/b.
PANTHERiPTHR11599:SF76. PTHR11599:SF76. 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.

Q24178-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSRYGRALT IFSPDGHLLQ VEYAQEAVRK GSTAVGVRGA NCVVLGVEKS
60 70 80 90 100
SVSEMQEDRT VRKISMLDRH VALAFAGLTA DARILINRGQ VECQSHRLNF
110 120 130 140 150
ENQVTLEYIT RYLAQLKQKY TQCNGRRPFG ISCLIGGIDA DGSARLFHTE
160 170 180 190 200
PSGIFHEYKA TATGRWANTV REFFEKAYSD HEVTTKCDAI KLAMRALLEV
210 220 230 240
TQMSQMRLEV AVLENGKPMK MLDSVVISEI VKIVQNEKEL QAKAHKMKR
Length:249
Mass (Da):27,940
Last modified:December 8, 2000 - v2
Checksum:i18B642DE3F1AE453
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti24A → G in AAC47280 (PubMed:8878681).Curated1
Sequence conflicti123C → V in AAC47280 (PubMed:8878681).Curated1
Sequence conflicti127 – 128RP → PS in AAC47280 (PubMed:8878681).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti29R → P in strain: CPA-46. 1
Natural varianti236N → K in strain: CPA-46. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U46008 Genomic DNA. Translation: AAC47280.1.
AY542403 Genomic DNA. Translation: AAS86247.1.
AY542404 Genomic DNA. Translation: AAS86248.1.
AY542405 Genomic DNA. Translation: AAS86249.1.
AY542406 Genomic DNA. Translation: AAS86250.1.
AY542407 Genomic DNA. Translation: AAS86251.1.
AY542408 Genomic DNA. Translation: AAS86252.1.
AY542409 Genomic DNA. Translation: AAS86253.1.
AE014297 Genomic DNA. Translation: AAF55802.1.
AY075276 mRNA. Translation: AAL68143.1.
PIRiS72225.
RefSeqiNP_650910.1. NM_142653.3.
UniGeneiDm.5563.

Genome annotation databases

EnsemblMetazoaiFBtr0083928; FBpp0083336; FBgn0265606.
GeneIDi42457.
KEGGidme:Dmel_CG17268.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPSA72_DROME
AccessioniPrimary (citable) accession number: Q24178
Secondary accession number(s): Q6QH19, Q8T8U0, Q9VDJ1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: December 8, 2000
Last modified: September 27, 2017
This is version 153 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