Q5RF14 (MIPEP_PONAB) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 6, 2013.
Version 52.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Mitochondrial intermediate peptidase Short name=MIP EC=3.4.24.59 | ||
| Gene names |
| ||
| Organism | Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome] | ||
| Taxonomic identifier | 9601 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo![]() |
Protein attributes
| Sequence length | 713 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 | Cleaves proteins, imported into the mitochondrion, to their mature size By similarity. |
| Catalytic activity | Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion. |
| Cofactor | Binds 1 zinc ion By similarity. |
| Enzyme regulation | Activity is divalent cation-dependent. It is stimulated by manganese, magnesium or calcium ions and reversibly inhibited by zinc, cobalt and iron By similarity. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Mitochondrion matrix By similarity. |
| Sequence similarities | Belongs to the peptidase M3 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | Calcium Cobalt Iron Magnesium Manganese Metal-binding Zinc |
| Molecular function | Hydrolase Metalloprotease Protease |
| PTM | Acetylation |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 35 | 35 | Mitochondrion By similarity | ||||||
| Chain | 36 – 713 | 678 | Mitochondrial intermediate peptidase | PRO_0000319049 | |||||
Sites | |||||||||
| Active site | 496 | 1 | By similarity | ||||||
| Metal binding | 495 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 499 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 502 | 1 | Zinc; catalytic By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 126 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CR857347 mRNA. Translation: CAH89643.1. |
| RefSeq | NP_001124737.1. NM_001131265.1. |
| UniGene | Pab.19458. |
3D structure databases | |
| ProteinModelPortal | Q5RF14. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M03.006. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 100171586. |
| KEGG | pon:100171586. |
Organism-specific databases | |
| CTD | 4285. |
Phylogenomic databases | |
| HOGENOM | HOG000230535. |
| HOVERGEN | HBG008215. |
| InParanoid | Q5RF14. |
| KO | K01410. |
Family and domain databases | |
| Gene3D | 1.10.1370.10. 2 hits. 1.20.1050.40. 1 hit. 3.40.390.10. 1 hit. |
| InterPro | IPR024079. MetalloPept_cat_dom. IPR024077. Neurolysin/TOP_dom2. IPR024080. Neurolysin/TOP_N. IPR001567. Pept_M3A_M3B. [Graphical view] |
| Pfam | PF01432. Peptidase_M3. 1 hit. [Graphical view] |
| PROSITE | PS00142. ZINC_PROTEASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MIPEP_PONAB | ||||||||
| Accession | Primary (citable) accession number: Q5RF14 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
