| IED ID | IndEnz0002012470 |
| Enzyme Type ID | protease012470 |
| Protein Name |
ATP-dependent zinc metalloprotease YME1L1 EC 3.4.24.- ATP-dependent metalloprotease FtsH1 Meg-4 Presenilin-associated metalloprotease PAMP YME1-like protein 1 |
| Gene Name | YME1L1 FTSH1 YME1L UNQ1868/PRO4304 |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MFSLSSTVQPQVTVPLSHLINAFHTPKNTSVSLSGVSVSQNQHRDVVPEHEAPSSECMFSDFLTKLNIVSIGKGKIFEGYRSMFMEPAKRMKKSLDTTDNWHIRPEPFSLSIPPSLNLRDLGLSELKIGQIDQLVENLLPGFCKGKNISSHWHTSHVSAQSFFENKYGNLDIFSTLRSSCLYRHHSRALQSICSDLQYWPVFIQSRGFKTLKSRTRRLQSTSERLAETQNIAPSFVKGFLLRDRGSDVESLDKLMKTKNIPEAHQDAFKTGFAEGFLKAQALTQKTNDSLRRTRLILFVLLLFGIYGLLKNPFLSVRFRTTTGLDSAVDPVQMKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQMDVSMGGRVAEELIFGTDHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTGKLSPETQSAIEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEGKKLEVR |
| Enzyme Length | 773 |
| Uniprot Accession Number | Q96TA2 |
| Absorption | |
| Active Site | ACT_SITE 600; /evidence=ECO:0000250|UniProtKB:P0AAI3 |
| 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:26923599, PubMed:27786171). Plays an important role in regulating mitochondrial morphology and function by cleaving OPA1 at position S2, giving rise to a form of OPA1 that promotes maintenance of normal mitochondrial structure and mitochondrial protein metabolism (PubMed:18076378, PubMed:26923599, PubMed:27495975). 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:22262461). Required for normal, constitutive degradation of PRELID1 (PubMed:27495975). Catalyzes the degradation of OMA1 in response to membrane depolarization (PubMed:26923599). Required to control the accumulation of nonassembled respiratory chain subunits (NDUFB6, OX4 and ND1) (PubMed:22262461). {ECO:0000269|PubMed:18076378, ECO:0000269|PubMed:22262461, ECO:0000269|PubMed:26923599, ECO:0000269|PubMed:27495975, ECO:0000269|PubMed:27786171}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 379..386; /note=ATP; /evidence=ECO:0000255 |
| Features | Active site (1); Alternative sequence (2); Chain (1); Metal binding (3); Mutagenesis (2); Natural variant (1); Nucleotide binding (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) |
| Keywords | ATP-binding;Alternative splicing;Disease variant;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:10843804, ECO:0000269|PubMed:22262461}. Mitochondrion {ECO:0000269|PubMed:26923599, ECO:0000269|PubMed:27495975}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically processed by mitochondrial processing peptidase (MPP) to generate the mature form. {ECO:0000269|PubMed:27495975}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16385451; 20186120; 20562859; 20711500; 21988832; 22593156; 23455922; 23602568; 24267889; 24344204; 24725412; 25609649; 26496610; 27642048; 27737933; |
| Motif | |
| Gene Encoded By | |
| Mass | 86,455 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 mM for ATP {ECO:0000269|PubMed:27786171}; |
| Metal Binding | METAL 599; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P0AAI3; METAL 603; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P0AAI3; METAL 677; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P0AAI3 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B18; |