IED ID | IndEnz0002001706 |
Enzyme Type ID | protease001706 |
Protein Name |
Tolloid-like protein 2 EC 3.4.24.- Metalloprotease xolloid Xenopus tolloid |
Gene Name | tll2 xld |
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 | MSCGSPQVMMTLWTLTCVGLILLGAIRLSLGLDYDLESFDYLMEDNPEEFDYKDPCKAAAYWGDIALDEDDLKWIFKNKSNDLRNTRHNQTHPTTDNFSEKLGTGSQNETSSNLNSKKVKKGSRLKLLIAEKAATETNSTFQVQTSNDRVRRAATSRTERIWPGGIIPYAIAGNFTGTQRAIFKQAMRHWKKHTCVTFVERTDEESFIVFTYRPCGCCSYVGRRGGGPQAISIGKNCDKFGIVVHELGHVVGFWHEHTRPDRDEHVSIIRENIQPGQEYNFLKMEPGEVSSLGETYDFDSIMHYARNTFSRGVFLDTILPRRIDTSVRPTIGQRIRLSQGDIAQAKKLYKCPACGETLQDSSGNFSAPGYPSGYPSYTHCIWRISVTPGEKIILNFTTMDLFKSRLCWYDYIEIRDGYWRKAALLGRLCGDKLPDPIISSDSKLWIEFRSSSNILGKGFFAAYEAICGGDIKKDSGQIQSPNYPDDYRPAKECIWKITVSEGFLVGLSFQAFEIERHDNCAYDYLEVRDGFSEDHALIGRFCGYEKPEDIKSTSNKLWIKFASDGSINKAGFSANFFKEMDECSRPDNGGCSQRCVNTLGSYKCVCEPGFELTADKKSCEAACGGFITQLNGTITSPGWPKEYPTNKNCVWQVVAPAQYRISLQFEVFELEGNDVCKYDYLEIRSGLSSESKLHGKFCGPEKPEVITSQGNTVRIEFKSDNTVSKKGFKANFFSDKDECSKDNGGCQHDCVNTFGSYICQCKNGFILHENGHDCKEAGCEQKLLNAEGTISSPNWPEKYPSRKECTWDISVTAGHRVKLVFTDFEIEQHQECAYDHLELYDGPNGKAAILGRFCGSKEPSPVVASTNNMFLRFYSDASVQRKGFQAKYSPECGGRLKAEIQTNDIYSHAQFGDNNYPVQSNCEWVIVAEDGYGVELIFQTFEIEEESDCGYDYMEVYDGYDSTAPRLGRYCGSGPPEEMYSAGDSIMIRFHTDDTINKKGFHGQYTSTKFQDALHMRRK |
Enzyme Length | 1019 |
Uniprot Accession Number | O57382 |
Absorption | |
Active Site | ACT_SITE 246; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.24.- |
Enzyme Function | FUNCTION: Protease which specifically processes prolysyl oxidase and maybe also chordin. Required for the embryonic development. Predominant protease, which in the development, influences dorsal-ventral patterning and skeletogenesis. In embryos, inhibits the development of dorsoanterior structures and ventralizes activin-induced dorsal mesoderm in animal caps. {ECO:0000269|PubMed:9520331}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Compositional bias (1); Disulfide bond (19); Domain (8); Glycosylation (4); Metal binding (3); Propeptide (1); Region (1); Signal peptide (1) |
Keywords | Calcium;Cleavage on pair of basic residues;Developmental protein;Differentiation;Disulfide bond;EGF-like domain;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Repeat;Secreted;Signal;Zinc;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9520331}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 114,892 |
Kinetics | |
Metal Binding | METAL 245; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 249; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 255; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
Rhea ID | |
Cross Reference Brenda |