Reviewed,
UniProtKB/Swiss-Prot P20069 (MPPA_RAT)
Last modified
June 16, 2009.
Version 90.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Mitochondrial-processing peptidase subunit alpha EC=3.4.24.64 Alternative name(s): Alpha-MPP P-55 | ||||
| Gene names |
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| 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 | 524 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 mitochondrial processing protease (MPP-I) cleaves presequences from mitochondrial protein precursors. Most MPP-I cleavage sites follow an arginine at position -2. |
| Catalytic activity | Release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2. |
| Subunit structure | Heterodimer of alpha and beta subunits. |
| Subcellular location | |
| Sequence similarities | Belongs to the peptidase M16 family. |
| Caution | Does not seem to have a protease activity as it lack the zinc-binding site. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Molecular function | Hydrolase Metalloprotease Protease |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | proteolysis Ref.1 Inferred from direct assay. Source: RGD |
| Cellular component | mitochondrial matrix Ref.1 Traceable author statement. Source: RGD |
| Molecular function | metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "The general mitochondrial matrix processing protease from rat liver: structural characterization of the catalytic subunit." Kleiber J., Kalousek F., Swaroop M., Rosenberg L.E. Proc. Natl. Acad. Sci. U.S.A. 87:7978-7982(1990) [PubMed: 2236012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 33-44; 113-121; 188-202; 223-231; 235-242; 362-369 AND 486-511. Strain: Sprague-Dawley. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| M57728 mRNA. Translation: AAA41632.1. | |
| IPI | IPI00195551. |
| PIR | A36205. |
| UniGene | Rn.11175 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1HR6 based on UniProtKB P11914. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M16.971. |
Genome annotation databases | |
| Ensembl | ENSRNOG00000026775. Rattus norvegicus. [Contig view] |
Organism-specific databases | |
| RGD | 727897. Pmpca. |
Phylogenomic databases | |
| HOVERGEN | P20069. |
Enzyme and pathway databases | |
| BRENDA | 3.4.24.64. 248. |
Gene expression databases | |
| ArrayExpress | P20069. |
| GermOnline | ENSRNOG00000026775. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR011237. Pept_M16_core. IPR011765. Pept_M16_N. IPR001431. Pept_M16_Zn_BS. IPR007863. Peptidase_M16_C. [Graphical view] |
| Gene3D | G3DSA:3.30.830.10. Pept_M16_core. 2 hits. |
| Pfam | PF00675. Peptidase_M16. 1 hit. PF05193. Peptidase_M16_C. 1 hit. [Graphical view] |
| PROSITE | PS00143. INSULINASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MPPA_RAT | ||||||||
| Accession | Primary (citable) accession number: P20069 | ||||||||
| Entry history |
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| 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


