Q9V5C6 · PSA3_DROME
- ProteinProteasome subunit alpha type-3
- GeneProsalpha7
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids253 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
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).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | proteasome complex | |
Cellular Component | proteasome core complex | |
Cellular Component | proteasome core complex, alpha-subunit complex | |
Cellular Component | synapse | |
Biological Process | follicle cell of egg chamber development | |
Biological Process | proteasome-mediated ubiquitin-dependent protein catabolic process |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProteasome subunit alpha type-3
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ9V5C6
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000124097 | 1-253 | Proteasome subunit alpha type-3 | |||
Sequence: MSTIGTGYDLSASQFSPDGRVFQIDYASKAVEKSGTVIGIRGKDAVVLAVEKIITSKLYEPDAGGRIFTIEKNIGMAVAGLVADGNFVADIARQEAANYRQQFEQAIPLKHLCHRVAGYVHAYTLYSAVRPFGLSIILASWDEVEGPQLYKIEPSGSSFGYFACASGKAKQLAKTEMEKLKMDMRTDELVESAGEIIYKVHDELKDKDFRFEMGLVGRVTGGLHLINPSELTEKARKAGDAANKDEDSDNETH | ||||||
Modified residue | 248 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
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
Interacts with ntc
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 230-253 | Disordered | ||||
Sequence: ELTEKARKAGDAANKDEDSDNETH |
Sequence similarities
Belongs to the peptidase T1A family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length253
- Mass (Da)27,675
- Last updated2000-05-01 v1
- Checksum7B19D8DA350E2B7E
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 17 | in Ref. 1; AAB82572 | ||||
Sequence: P → A | ||||||
Sequence conflict | 30 | in Ref. 1; AAB82572 | ||||
Sequence: Missing | ||||||
Sequence conflict | 62 | in Ref. 1; AAB82572 | ||||
Sequence: D → H | ||||||
Sequence conflict | 140-157 | in Ref. 5; AAT27293 | ||||
Sequence: Missing | ||||||
Sequence conflict | 167 | in Ref. 1; AAB82572 | ||||
Sequence: Missing | ||||||
Sequence conflict | 182 | in Ref. 1; AAB82572 | ||||
Sequence: M → T | ||||||
Sequence conflict | 235-253 | in Ref. 1; AAB82572 | ||||
Sequence: ARKAGDAANKDEDSDNETH → DEDTACGQQDEGRRQRQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF025793 EMBL· GenBank· DDBJ | AAB82572.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE013599 EMBL· GenBank· DDBJ | AAF58889.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY069616 EMBL· GenBank· DDBJ | AAL39761.1 EMBL· GenBank· DDBJ | mRNA | ||
BT014669 EMBL· GenBank· DDBJ | AAT27293.1 EMBL· GenBank· DDBJ | mRNA |