Reviewed,
UniProtKB/Swiss-Prot P17220 (PSA2_RAT)
Last modified
February 9, 2010.
Version 96.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Proteasome subunit alpha type-2 EC=3.4.25.1 Alternative name(s): Proteasome component C3 Macropain subunit C3 Multicatalytic endopeptidase complex subunit C3 | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 234 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| 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. PSMA2 may have a potential regulatory effect on another component(s) of the proteasome complex through tyrosine phosphorylation. |
| Catalytic activity | Cleavage of peptide bonds with very broad specificity. |
| Subunit structure | 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. |
| Subcellular location | |
| Tissue specificity | Ubiquitous. |
| Post-translational modification | Phosphorylated on tyrosine residues; which may be important for nuclear import. Ref.4 |
| Sequence similarities | Belongs to the peptidase T1A family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Nucleus Proteasome |
| Molecular function | Hydrolase Protease Threonine protease |
| PTM | Acetylation Phosphoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleusInferred from electronic annotation. Source: UniProtKB-SubCell proteasome core complex, alpha-subunit complexInferred from electronic annotation. Source: InterPro |
| Molecular function | threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.2 | ||||||
| Chain | 2 – 234 | 233 | Proteasome subunit alpha type-2 | PRO_0000124079 | |||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine Ref.2 | ||||||
| Modified residue | 7 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 24 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 57 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 70 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 76 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 98 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 121 | 1 | Phosphotyrosine Probable | ||||||
| Modified residue | 171 | 1 | N6-acetyllysine By similarity | ||||||
Experimental info | |||||||||
| Mutagenesis | 121 | 1 | Y → F: Abolishes nuclear localization and phosphorylation. Ref.4 | ||||||
Sequences
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References
| [1] | "Molecular cloning of cDNA for proteasomes from rat liver: primary structure of component C3 with a possible tyrosine phosphorylation site." Tanaka K., Fujiwara T., Kumatori A., Shin S., Yoshimura T., Ichihara A., Tokunaga F., Aruga R., Iwanaga S., Kakizuka A., Nakanishi S. Biochemistry 29:3777-3785(1990) [PubMed: 2340272] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: Wistar. Tissue: Liver. |
| [2] | "The NH2-terminal residues of rat liver proteasome (multicatalytic proteinase complex) subunits, C2, C3 and C8, are N alpha-acetylated." Tokunaga F., Aruga R., Iwanaga S., Tanaka K., Ichihara A., Takao T., Shimonishi Y. FEBS Lett. 263:373-375(1990) [PubMed: 2335242] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-30. Tissue: Liver. |
| [3] | Lubec G., Afjehi-Sadat L. Submitted (NOV-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 5-39 AND 71-84, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord. |
| [4] | "Nuclear multicatalytic proteinase subunit RRC3 is important for growth regulation in hepatocytes." Benedict C.M., Clawson G.A. Biochemistry 35:11612-11621(1996) [PubMed: 8794741] [Abstract] Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-121, PHOSPHORYLATION AT TYR-121. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | J02897 mRNA. Translation: AAA40838.1. |
| IPI | IPI00231757. |
| PIR | SNRTC3. A34535. |
| RefSeq | NP_058975.1. |
| UniGene | Rn.1617 |
3D structure databases | |
| SMR | P17220. Positions 2-234. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | T01.972. |
PTM databases | |
| PhosphoSite | P17220. |
Proteomic databases | |
| PRIDE | P17220. |
Genome annotation databases | |
| GeneID | 29669. |
| KEGG | rno:29669. |
Organism-specific databases | |
| CTD | 29669. |
| RGD | 61842. Psma2. |
Phylogenomic databases | |
| eggNOG | maNOG09688. |
| HOVERGEN | P17220. |
| OrthoDB | EOG9BK7P5. |
| PhylomeDB | P17220. |
Enzyme and pathway databases | |
| BRENDA | 3.4.25.1. 248. |
Gene expression databases | |
| Genevestigator | P17220. |
Family and domain databases | |
| InterPro | IPR000426. Proteasome_asu_CS. IPR001353. Proteasome_sua/b. [Graphical view] |
| Pfam | PF00227. Proteasome. 1 hit. PF10584. Proteasome_A_N. 1 hit. [Graphical view] |
| PROSITE | PS00388. PROTEASOME_A_1. 1 hit. PS51475. PROTEASOME_A_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 609987. |
Entry information
| Entry name | PSA2_RAT | ||||||||
| Accession | Primary (citable) accession number: P17220 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


