Detail Information for IndEnz0002001706
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