| IED ID | IndEnz0002016620 |
| Enzyme Type ID | protease016620 |
| Protein Name |
Disintegrin and metalloproteinase domain-containing protein 9 ADAM 9 EC 3.4.24.- Meltrin-gamma Metalloprotease/disintegrin/cysteine-rich protein 9 Myeloma cell metalloproteinase |
| Gene Name | Adam9 Kiaa0021 Mdc9 Mltng |
| Organism | Mus musculus (Mouse) |
| 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 Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MGPRALSPLASLRLRWLLACGLLGPVLEAGRPDLEQTVHLSSYEIITPWRLTRERREALGPSSQQISYVIQAQGKQHIIHLERNTDLLPNDFVVYTYDKEGSLLSDHPNVQSHCHYRGYVEGVQNSAVAVSACFGLRGLLHLENASFGIEPLHNSSHFEHIFYPMDGIHQEPLRCGVSNRDTEKEGTQGDEEEHPSVTQLLRRRRAVLPQTRYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKFLITRWRHDSAQLVLKKGFGGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGRECFCGAKSCIMNSGASGSRNFSSCSAEDFEKLTLNKGGSCLLNIPKPDEAYSAPSCGNKLVDPGEECDCGTAKECEVDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPDVFIQNGYPCQNSKAYCYNGMCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGFSGSEYKKCATGNALCGKLQCENVQDMPVFGIVPAIIQTPSRGTKCWGVDFQLGSDVPDPGMVNEGTKCDAGKICRNFQCVNASVLNYDCDIQGKCHGHGVCNSNKNCHCEDGWAPPHCDTKGYGGSVDSGPTYNAKSTALRDGLLVFFFLIVPLVAAAIFLFIKRDELRKTFRKKRSQMSDGRNQANVSRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQPAQFPSRPPPPQPKISSQGNLIPARPAPAPPLYSSLT |
| Enzyme Length | 845 |
| Uniprot Accession Number | Q61072 |
| Absorption | |
| Active Site | ACT_SITE 348; /evidence="ECO:0000250|UniProtKB:P78536, ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Synthesized as an inactive form which is proteolytically cleaved to generate an active enzyme. Processing at the upstream site is particularly important for activation of the proenzyme, whereas processing at the boundary between the pro-domain and the catalytic domain does not appear to be essential (PubMed:25795784). Inhibited by hydroxamic acid-based inhibitors (PubMed:9920899). {ECO:0000269|PubMed:25795784, ECO:0000269|PubMed:9920899}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Cleaves and releases a number of molecules with important roles in tumorigenesis and angiogenesis, such as TEK, KDR, EPHB4, CD40, VCAM1 and CDH5 (PubMed:19273593). May mediate cell-cell, cell-matrix interactions and regulate the motility of cells via interactions with integrins (PubMed:10825303). {ECO:0000269|PubMed:10825303, ECO:0000269|PubMed:19273593}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (1); Disulfide bond (7); Domain (3); Erroneous initiation (1); Glycosylation (6); Metal binding (3); Mutagenesis (5); Region (1); Sequence conflict (3); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1) |
| Keywords | Cell membrane;Direct protein sequencing;Disulfide bond;EGF-like domain;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;Signal;Transmembrane;Transmembrane helix;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25795784, ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically cleaved in the trans-Golgi network before it reaches the plasma membrane to generate a mature protein. The removal of the pro-domain occurs via cleavage at two different sites. Processed most likely by a pro-protein convertase such as furin, at the boundary between the pro-domain and the catalytic domain. An additional upstream cleavage pro-protein convertase site (Arg-56/Glu-57) has an important role in the activation of ADAM9. {ECO:0000269|PubMed:25795784, ECO:0000269|PubMed:9920899}.; PTM: Phosphorylation is induced in vitro by phorbol-12-myristate-13-acetate (PMA) (PubMed:9920899). {ECO:0000269|PubMed:9920899}. |
| Signal Peptide | SIGNAL 1..29; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10523497; 10725249; 10842103; 11955914; 12135759; 12463424; 14516789; 14993236; 15361064; 15739225; 15907280; 15936750; 16141072; 16230393; 16236709; 16311053; 16336960; 16806063; 17072319; 17107962; 17344430; 18393804; 18799693; 19213735; 19574220; 20376065; 21068328; 21135106; 22480688; 22622419; 22632802; 23833070; 24006456; 24586749; 25063875; 25778452; 28553955; 28928095; 30814516; 32078829; 32290105; 32535037; 32612155; 32906814; 33911034; 9857183; |
| Motif | |
| Gene Encoded By | |
| Mass | 92,079 |
| Kinetics | |
| Metal Binding | METAL 347; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 351; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 357; /note=Zinc; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B9; |