| IED ID | IndEnz0002002748 |
| Enzyme Type ID | protease002748 |
| Protein Name |
AFG3-like protein 2 EC 3.4.24.- Paraplegin-like protein |
| Gene Name | AFG3L2 |
| 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 | MAHRCLRLWGRGGCWPRGLQQLLVPGGVGPGEQPCLRTLYRFVTTQARASRNSLLTDIIAAYQRFCSRPPKGFEKYFPNGKNGKKASEPKEVMGEKKESKPAATTRSSGGGGGGGGKRGGKKDDSHWWSRFQKGDIPWDDKDFRMFFLWTALFWGGVMFYLLLKRSGREITWKDFVNNYLSKGVVDRLEVVNKRFVRVTFTPGKTPVDGQYVWFNIGSVDTFERNLETLQQELGIEGENRVPVVYIAESDGSFLLSMLPTVLIIAFLLYTIRRGPAGIGRTGRGMGGLFSVGETTAKVLKDEIDVKFKDVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSTLEKDKLARKLASLTPGFSGADVANVCNEAALIAARHLSDSINQKHFEQAIERVIGGLEKKTQVLQPEEKKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKEQYLYTKEQLLDRMCMTLGGRVSEEIFFGRITTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDLPRQGDMVLEKPYSEATARLIDDEVRILINDAYKRTVALLTEKKADVEKVALLLLEKEVLDKNDMVELLGPRPFAEKSTYEEFVEGTGSLDEDTSLPEGLKDWNKEREKEKEEPPGEKVAN |
| Enzyme Length | 797 |
| Uniprot Accession Number | Q9Y4W6 |
| Absorption | |
| Active Site | ACT_SITE 575; /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 protease which is essential for axonal and neuron development. In neurons, mediates degradation of SMDT1/EMRE before its assembly with the uniporter complex, limiting the availability of SMDT1/EMRE for MCU assembly and promoting efficient assembly of gatekeeper subunits with MCU (PubMed:27642048). Required for paraplegin (SPG7) maturation (PubMed:30252181). After its cleavage by mitochondrial-processing peptidase (MPP), it converts paraplegin into a proteolytically active mature form (By similarity). Required for the maturation of PINK1 into its 52kDa mature form after its cleavage by mitochondrial-processing peptidase (MPP) (PubMed:22354088, PubMed:30252181). Involved in the regulation of OMA1-dependent processing of OPA1 (PubMed:32600459, PubMed:30252181). {ECO:0000250|UniProtKB:Q8JZQ2, ECO:0000269|PubMed:22354088, ECO:0000269|PubMed:27642048, ECO:0000269|PubMed:30252181, ECO:0000269|PubMed:32600459}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 348..355; /note=ATP; /evidence=ECO:0000255 |
| Features | Active site (1); Beta strand (17); Chain (1); Compositional bias (2); Helix (23); Metal binding (3); Modified residue (1); Mutagenesis (1); Natural variant (32); Nucleotide binding (1); Propeptide (1); Region (2); Sequence conflict (2); Transit peptide (1); Transmembrane (2); Turn (9) |
| Keywords | 3D-structure;ATP-binding;Disease variant;Hydrolase;Membrane;Metal-binding;Metalloprotease;Mitochondrion;Mitochondrion inner membrane;Neurodegeneration;Nucleotide-binding;Protease;Reference proteome;Spinocerebellar ataxia;Transit peptide;Transmembrane;Transmembrane helix;Zinc |
| Interact With | P42858 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10395799, ECO:0000269|PubMed:22354088}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q8JZQ2}; Multi-pass membrane protein {ECO:0000255}. |
| Modified Residue | MOD_RES 117; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q8JZQ2 |
| Post Translational Modification | PTM: Upon import into the mitochondrion, the N-terminal transit peptide is cleaved to generate an intermediate form which undergoes autocatalytic proteolytic processing to generate the proteolytically active mature form. {ECO:0000250|UniProtKB:Q8JZQ2, ECO:0000269|PubMed:30252181}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1); Electron microscopy (1) |
| Cross Reference PDB | 2LNA; 6NYY; |
| Mapped Pubmed ID | 14743216; 16169070; 19615732; 19748354; 20186120; 20562859; 20711500; 20877624; 21080425; 21827917; 21900206; 21911578; 22157815; 22252130; 22593156; 23414517; 23602568; 23606334; 23663784; 24055473; 24344204; 24422629; 24725412; 24814845; 25251419; 25420100; 25561175; 25609649; 25927548; 26496610; 29545505; 29932645; 30389403; 30910913; 31111429; 31327635; 32248051; 33075064; 34333379; |
| Motif | |
| Gene Encoded By | |
| Mass | 88,584 |
| Kinetics | |
| Metal Binding | METAL 574; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9WZ49; METAL 578; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9WZ49; METAL 649; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9WZ49 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B18; |