Reviewed,
UniProtKB/Swiss-Prot P24495 (PSA2_XENLA)
Last modified
October 13, 2009.
Version 78.
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 Short name=xC3 | ||
| Gene names |
| ||
| Organism | Xenopus laevis (African clawed frog) | ||
| Taxonomic identifier | 8355 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus |
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 transcript 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 By similarity. |
| 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 By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the peptidase T1A family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Nucleus Proteasome |
| Molecular function | Hydrolase Protease Threonine protease |
| PTM | Acetylation Phosphoprotein |
| 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 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 By similarity | ||||||
| Chain | 2 – 234 | 233 | Proteasome subunit alpha type-2 | PRO_0000124080 | |||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
| Modified residue | 121 | 1 | Phosphotyrosine By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Deduced primary structure of a Xenopus proteasome subunit XC3 and expression of its mRNA during early development." Fujii G., Tashiro K., Emori Y., Saigo K., Tanaka K., Shiokawa K. Biochem. Biophys. Res. Commun. 178:1233-1239(1991) [PubMed: 1872843] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | NIH - Xenopus Gene Collection (XGC) project Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Embryo. |
Cross-references
Sequence databases | |
|---|---|
| S51111 mRNA. Translation: AAB19485.1. BC072254 mRNA. Translation: AAH72254.1. | |
| PIR | JH0421. |
| RefSeq | NP_001084053.1. |
| UniGene | Xl.2546 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1RYP based on UniProtKB P23639. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | T01.972. |
Proteomic databases | |
| PRIDE | P24495. |
Genome annotation databases | |
| GeneID | 399279. |
| KEGG | xla:399279. |
Organism-specific databases | |
| CTD | 399279. |
| Xenbase | XB-FEAT-964710. psma2. |
Phylogenomic databases | |
| HOVERGEN | P24495. |
Enzyme and pathway databases | |
| BRENDA | 3.4.25.1. 648. |
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 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PSA2_XENLA | ||||||||
| Accession | Primary (citable) accession number: P24495 Secondary accession number(s): Q6INM4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Xenopus annotation project | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


