Detail Information for IndEnz0002018568
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