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Protein

Proteasome subunit alpha type-4-like

Gene

Prosalpha3T

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-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-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-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-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-4-like (EC:3.4.25.1)
Gene namesi
ORF Names:CG1736
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0261395. Prosalpha3T.

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

Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001241101 – 251Proteasome subunit alpha type-4-likeAdd BLAST251

Proteomic databases

PaxDbiQ9VA12.
PRIDEiQ9VA12.

Expressioni

Tissue specificityi

Testis, prominent after meiosis II. After meiosis, predominantly localized to the haploid spermatid nuclei of the 64-cell cysts, remaining during the elongation and condensation of the spermatid nuclei. In mature, motile sperm, expression is seen exclusively in the sperm head.1 Publication

Gene expression databases

BgeeiFBgn0261395.
GenevisibleiQ9VA12. 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

BioGridi68527. 1 interactor.
STRINGi7227.FBpp0085100.

Structurei

3D structure databases

ProteinModelPortaliQ9VA12.
SMRiQ9VA12.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0178. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00550000074827.
HOGENOMiHOG000263951.
InParanoidiQ9VA12.
KOiK02728.
OMAiRFGFQLY.
OrthoDBiEOG091G0F2L.
PhylomeDBiQ9VA12.

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.
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.

Q9VA12-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARFFDSRTT IFSPEGRLYQ VEYAMEAASQ SGTCVGLLAK NGVLLATERS
60 70 80 90 100
VDKLMDTSIP VPRISWLNEN IACCATGNTA DGNVLVNQLR MIAQQYQFNF
110 120 130 140 150
GEMIPCEQLV TNLCDIKQAY TQYGGKRPFG VSFLYMGWDC RFGFQLYQSD
160 170 180 190 200
PSGNYSGWKA TCIGRKSGAA MEMLQKELFS KGYVSPSVEE AKDVAIKVMG
210 220 230 240 250
MTLGRDSLTP EKLEIAFVQR YGNTTVFHIL EKNEIHRLIE RNNNLKRRVG

S
Length:251
Mass (Da):28,169
Last modified:May 1, 2000 - v1
Checksum:iB1AFF83978DB14D3
GO

Sequence cautioni

The sequence ACD81826 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti74 – 75CA → WP in AAN63094 (PubMed:12421421).Curated2
Sequence conflicti133F → L in AAN63094 (PubMed:12421421).Curated1
Sequence conflicti141 – 142RF → AS in AAN63094 (PubMed:12421421).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF57116.1.
AY147240 Genomic DNA. Translation: AAN63094.1.
BT032812 mRNA. Translation: ACD81826.1. Different initiation.
RefSeqiNP_651843.1. NM_143586.3.

Genome annotation databases

EnsemblMetazoaiFBtr0085738; FBpp0085100; FBgn0261395.
GeneIDi43679.
KEGGidme:Dmel_CG1736.
UCSCiCG1736-RA. d. melanogaster.

Similar proteinsi

Entry informationi

Entry nameiPSA4L_DROME
AccessioniPrimary (citable) accession number: Q9VA12
Secondary accession number(s): B3DN24, Q8IS89
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: May 1, 2000
Last modified: November 22, 2017
This is version 132 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