| IED ID | IndEnz0002000069 |
| Enzyme Type ID | protease000069 |
| Protein Name |
Mitochondrial intermediate peptidase MIP EC 3.4.24.59 |
| Gene Name | Mipep Mip |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MLLAAGTRYAYRLCGRRAAAALQGRAGRSCARSVSTSWSPVGAAFNVKPQGHLWDLLGERRGLFGVPELSTPEGFQVAQEEALRKTEWLVERACSTPPGPQTVLIFDELSDCLCRVADLADFVKIGHPEQAFREAAQEACRSIGTMVEKLNTNVELYQSLQKLLDDKKLMDSLDAETRRVAELFMFDFEISGIHLDEEKRRRAVDLNVKILDLSSAFLMGTNFPIKIQKHLLPEHIQHHFARDGRHLVIDGLHAEASDDLVREAAYKIFLYPNADQLKCLEELLSSRDLLANLVGYLPFPTGPPGTIAQTPETVMQFLEKLSEKLCERTRKDFEMMQGMKTKLNPQNSELMPWDPPYYSGVIRAERYNIEPSLYCPFLSLGACMEGLNVLFNRLLGVTLYAEQPFKGEVWCIDVRKLAVVHESEGLLGYIYCDFFQRANKPQQDCHFTIRGGRLKEDGSYQLPVVVLMLNLPHASRDFPTLLTPGMMENLFHEMGHAMHSMLGRTRYQHVTGTRCPTDFAEVPSILMEYFSNDYRVVSQFAKHYQTGQPLPKAMVSRLCESKKVCAAAEMQLQVFYAALDQIYHGQHPLKKSTTDILMETQEQFYGLPYVPDTAWQLRFSHLVGYGAKYYSYLMSRAVASMVWKECFLQDPFNRAAGERYRREMLAHGGGKEPMLMIQGMLQKCPSIDDFVDALVSDLNLDFETFFMDSK |
| Enzyme Length | 710 |
| Uniprot Accession Number | Q01992 |
| Absorption | |
| Active Site | ACT_SITE 493; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | ACTIVITY REGULATION: Activity is divalent cation-dependent. It is stimulated by manganese, magnesium or calcium ions and reversibly inhibited by zinc, cobalt and iron. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion.; EC=3.4.24.59; |
| DNA Binding | |
| EC Number | 3.4.24.59 |
| Enzyme Function | FUNCTION: Cleaves proteins, imported into the mitochondrion, to their mature size. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (3); Modified residue (1); Transit peptide (1) |
| Keywords | Acetylation;Calcium;Cobalt;Direct protein sequencing;Hydrolase;Iron;Magnesium;Manganese;Metal-binding;Metalloprotease;Mitochondrion;Protease;Reference proteome;Transit peptide;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion matrix. |
| Modified Residue | MOD_RES 124; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q99797 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 80,674 |
| Kinetics | |
| Metal Binding | METAL 492; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 496; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 499; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |