| IED ID | IndEnz0002018568 |
| Enzyme Type ID | protease018568 |
| Protein Name |
Disintegrin and metalloproteinase domain-containing protein 10 ADAM 10 EC 3.4.24.81 Kuzbanian protein homolog xKuz |
| Gene Name | adam10 kuz |
| Organism | Xenopus laevis (African clawed frog) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog) |
| Enzyme Sequence | MGLLRLVFLLSWAASAGGLYGNPLNKYIRHYEGLSYNVDSLHQKHQRAKRAVSQEDQFVHLDFQAHGRQFNLRMKKDTSLFSPDFKLEVGGETVNYDTSHIYTGQLFGEQGTLSHGSVVDGKSKGLLKPLKAHSYVEPSERFFKDQAVPFHSVMYHEDDIKYPHKYGSEGGCADSSVFKRMKEYQMSVQEEPEKHDHKEDHEDSGPVILRKKRAAQAEKNTCQLFIQTDHLFYKRYGETREAVIAQISSHVKAIDTIYQSTDFSGIRNISFMVKRIRINVTSDEKDPTNPFRFPNIGVEKFLELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGICERNKLYSDGKKKSLNTGIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHDSGNECTPGEAKNLGFKENGNFIMYARTTSGDKLNNNKFSICSVRNISQVLDKKENSCFVESGQPICGNGLVEPGEQCDCGYSDQCKDECCYDANQPENLKCTLKPGKQCSPSQGPCCTTDCTFKRASENCREESDCAKMGTCNGNSAQCPPSEPRENLTECNRATQVCIKGQCSGSICERYDLEECTCGSTDEKDDKELCHVCCMEKMKPHTCASTGSEAWKAYFKGKTITLQPGSPCNEFKGYCDVFMRCRLVDADGPLARLKKAIFNPELYENIAEWIVAHWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQTTQQPSRQRPRENYQMGHMRH |
| Enzyme Length | 749 |
| Uniprot Accession Number | Q8JIY1 |
| Absorption | |
| Active Site | ACT_SITE 385; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endopeptidase of broad specificity.; EC=3.4.24.81; Evidence={ECO:0000250|UniProtKB:O14672}; |
| DNA Binding | |
| EC Number | 3.4.24.81 |
| Enzyme Function | FUNCTION: Controls the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis. {ECO:0000250, ECO:0000269|PubMed:9244301}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (2); Disulfide bond (17); Domain (2); Glycosylation (4); Metal binding (4); Modified residue (1); Motif (3); Propeptide (1); Region (1); Sequence conflict (4); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Notch signaling pathway;Phosphoprotein;Protease;SH3-binding;Signal;Transmembrane;Transmembrane helix;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. |
| Modified Residue | MOD_RES 720; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:O14672 |
| Post Translational Modification | PTM: The precursor is cleaved by furin and PCSK7. {ECO:0000250|UniProtKB:Q10741}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 170..177; /note=Cysteine switch; /evidence=ECO:0000305; MOTIF 709..716; /note=SH3-binding; /evidence=ECO:0000255; MOTIF 723..729; /note=SH3-binding; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 84,068 |
| Kinetics | |
| Metal Binding | METAL 172; /note=Zinc; in inhibited form; /evidence=ECO:0000250|UniProtKB:P03956; METAL 384; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000250|UniProtKB:O14672; METAL 388; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000250|UniProtKB:O14672; METAL 394; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000250|UniProtKB:O14672 |
| Rhea ID | |
| Cross Reference Brenda |