| IED ID | IndEnz0002013704 |
| Enzyme Type ID | protease013704 |
| Protein Name |
ATP-dependent zinc metalloprotease YME1L EC 3.4.24.- YME1-like ATPase |
| Gene Name | YME1L CG3499 |
| Organism | Drosophila melanogaster (Fruit fly) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly) |
| Enzyme Sequence | MFSTTTHSVPYLYLGNFSRKPHYYSVNRTKLHGSAGAARLSKSTSTSSRSHDLVLDLRNLLSRSSASIQGMVERAARLNGILDRRLVDDVLAKVTSMLPSMRDVRVTLEESATQIGRVQLQNYQFEVSLTGAAGSVPTGANVKVIPTITPGLLRPLFSQQQLNQIRGFKTDRSIEAEQKRNPTMTSRLKNALANSPQRLDGDTPLQAEKLRRLLAKSEEHGFNKAESLKIAFAEGYLAAANSEDSPKSGKTMKYLKTLQTIVVIVVFLGIFLSFFTTSNGSVFRSIQLGNQVEVDPEEINVTFEDVKGCDEAKQELKEVVEFLKSPEKFSNLGGKLPKGVLLVGPPGTGKTLLARAVAGEAKVPFFHAAGPEFDEVLVGQGARRVRDLFKAAKARAPCVIFIDEIDSVGAKRTNSVLHPYANQTINQLLSEMDGFHQNAGVIVLGATNRRDDLDQALLRPGRFDVEVMVSTPDFTGRKEILSLYLTKILHDEIDLDMLARGTSGFTGADLENMINQAALRAAIDGAETVSMKHLETARDKVLMGPERKARLPDEEANTITAYHEGGHAIVAFYTKESHPLHKVTIMPRGPSLGHTAYIPEKERYHVTKAQLLAMMDTMMGGRAAEELVFGTDKITSGASSDLKQATSIATHMVRDWGMSDKVGLRTIEASKGLGTGDTLGPNTIEAVDAEIKRILSDSYERAKAILRKHTREHKALAEALLKYETLDADDIKAILNESQT |
| Enzyme Length | 740 |
| Uniprot Accession Number | F3YDF1 |
| Absorption | |
| Active Site | ACT_SITE 564; /evidence=ECO:0000250|UniProtKB:Q9WZ49 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: ATP-dependent metalloprotease that catalyzes the degradation of folded and unfolded proteins with a suitable degron sequence in the mitochondrial intermembrane region (PubMed:26160069). Plays an important role in regulating mitochondrial morphology and function by cleaving Opa1, giving rise to a form of Opa1 that promotes maintenance of normal mitochondrial structure and mitochondrial protein metabolism (PubMed:31125351). Ensures cell proliferation, maintains normal cristae morphology and complex I respiration activity, promotes antiapoptotic activity and protects mitochondria from the accumulation of oxidatively damaged membrane proteins (PubMed:26160069, PubMed:31125351). Required to control the accumulation of nonassembled respiratory chain subunits such as ND-30 (PubMed:26160069). {ECO:0000269|PubMed:26160069, ECO:0000269|PubMed:31125351}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 347..351; /note=ATP; /evidence=ECO:0000250|UniProtKB:Q9WZ49 |
| Features | Active site (1); Alternative sequence (2); Chain (1); Metal binding (3); Nucleotide binding (1); Topological domain (2); Transmembrane (1) |
| Keywords | ATP-binding;Alternative splicing;Hydrolase;Membrane;Metal-binding;Metalloprotease;Mitochondrion;Mitochondrion inner membrane;Nucleotide-binding;Protease;Reference proteome;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:26160069}; Single-pass membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10996302; 11309190; 12865422; 20220848; 20371351; 21074052; 23071443; 24874806; 24952591; 25215488; 25312911; 26870755; 27346357; 30865561; 31555733; 31722958; 31907391; 32344153; 32958650; |
| Motif | |
| Gene Encoded By | |
| Mass | 81,081 |
| Kinetics | |
| Metal Binding | METAL 563; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9WZ49; METAL 567; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9WZ49; METAL 641; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9WZ49 |
| Rhea ID | |
| Cross Reference Brenda |