| IED ID | IndEnz0002009127 |
| Enzyme Type ID | protease009127 |
| Protein Name |
Paraplegin EC 3.4.24.- |
| Gene Name | Spg7 |
| 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 | MAAALLLLRALRQSPEPGPWRLWAQLSGRSPGLFSGAGGRRPYVVRGTPIGLAAAGGHTPQSLLLRILTPSFEGVSGLLLKRHIVPSAIRLWQLSGSTLYFNTSGLKQKNKDDDKPKGKAPEDDEEERRRKEREDQMYRERLRTLFIIAIVMSLLNSLSTSGGSISWADFVNEMLAKGEVQRVQVVPESDVVEVYLHPGAVVFGRPRLALMYRMQVANIDKFEEKLRAAEDELNIESKDRIPVSYKRTGFFGNALYALGMTAVGLAILWYVFRLAGMTGREGGFSAFNQLKMARFTIVDGKTGKGVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGFSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFYSQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTFNFEYAVERVIAGTAKKSKILSKEEQRVVAFHESGHALVGWLLEHTEAVMKVSIAPRTNAALGFSQMLPRDQYLFTKEQLFERMCMALGGRAAEAISFSRVTSGAQDDLRKVTRIAYSMVKQFGMAPSIGPVSFPEAQEGLVGIGRRPFSQGLQQMMDHEARLLVARAYRHTEKVLLDNLDKLQALANALLEKEVINYEDIEALIGPPPHGPKKMIAPQKWIDAEKEKQASGEEEAPAP |
| Enzyme Length | 781 |
| Uniprot Accession Number | Q7TT47 |
| Absorption | |
| Active Site | ACT_SITE 575; /evidence=ECO:0000250|UniProtKB:Q9WZ49 |
| Activity Regulation | |
| Binding Site | BINDING 312; /note=ATP; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q9UQ90; BINDING 492; /note=ATP; /evidence=ECO:0000250|UniProtKB:Q9UQ90 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: ATP-dependent zinc metalloprotease. Plays a role in the formation and regulation of the mitochondrial permeability transition pore (mPTP) and its proteolytic activity is dispensable for this function (PubMed:26387735). {ECO:0000269|PubMed:26387735, ECO:0000305}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 349..357; /note=ATP; /evidence=ECO:0000250|UniProtKB:Q9UQ90 |
| Features | Active site (1); Alternative sequence (1); Binding site (2); Chain (1); Compositional bias (1); Metal binding (3); Modified residue (1); Nucleotide binding (1); Propeptide (1); Region (2); Topological domain (3); Transit peptide (1); Transmembrane (2) |
| Keywords | ATP-binding;Alternative splicing;Hydrolase;Membrane;Metal-binding;Metalloprotease;Mitochondrion;Mitochondrion inner membrane;Nitration;Nucleotide-binding;Protease;Reference proteome;Transit peptide;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9UQ90}; Multi-pass membrane protein {ECO:0000255}. |
| Modified Residue | MOD_RES 505; /note=3'-nitrotyrosine; /evidence=ECO:0000250|UniProtKB:Q3ULF4 |
| Post Translational Modification | PTM: Upon import into the mitochondrion, the N-terminal transit peptide is cleaved by the mitochondrial-processing peptidase (MPP) to generate an intermediate form which undergoes a second proteolytic cleavage mediated by proteases AFG3L1 and/or AFG3L2 removing an additional N-terminal fragment to generate the proteolytically active mature form. {ECO:0000250|UniProtKB:Q3ULF4}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 86,103 |
| Kinetics | |
| Metal Binding | METAL 574; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9WZ49; METAL 578; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9WZ49; METAL 650; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9WZ49 |
| Rhea ID | |
| Cross Reference Brenda |