Detail Information for IndEnz0002014233
IED ID IndEnz0002014233
Enzyme Type ID protease014233
Protein Name Bone morphogenetic protein 1
BMP-1
EC 3.4.24.-
Gene Name bmp1
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 MDYSYDLEEVVEETIDYKDPCKAAAFWGDIALDEEDLANFKIDRIVDLTKHTIHTVSGAATNISRPEKGRRTRKERRRSREKRASTSRPERVWPDGVIPYVISGNFSGSQRAIFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAISIGKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVSIIRENIQPGQEYNFLKMEPEEVESLGETYDFDSIMHYARNTFSRGIFLDTILPKYDVNGVRPPIGQRTRLSSGDVAQARKLYKCPACGETLQDSQGNFSSPGFPNGYSAYMHCVWRLSVTPGEKIILNFTSLDLYRSRLCWYDYIEVRDGFWKKAPLRGRFCGDKIPESIISTESRLWIEFRSSSNWVGKGFQAVYEALCGGEVKKDSGHIQSPNYPDDYRPNKACVWKLSVSEGFHVGISFQSFEIERHDSCAYDYLEIRDGSSETSPLVGRFCGYDKPDDIKSSTNQLWIKFVSDGSINKAGFSLNYFKEVDECSRPNNGGCEQRCVNTLGSYKCACDPGYELGQDKKSCEAACGGFLTKLNGSINSPGWPKEYPPNKNCIWQLVAPTQYRISLKFDQFETEGNDVCKYDFVEVRSGLTSDSKLHGKFCGSELPAVITSQYNNMRIEFKSDNTVSKKGFQANFFSEKKNNIQKLQQLNEVNRGQQNQAPKRVRPRMRLRTVKKTRPP
Enzyme Length 707
Uniprot Accession Number P98070
Absorption
Active Site ACT_SITE 177; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: Metalloprotease involved in pattern formation in gastrula and later differentiation of developing organs. Able to cleave chordin (chrd), suggesting that it may act in dorsoventral patterning during early development by regulating the chordin (chrd) activity. {ECO:0000269|PubMed:10864466, ECO:0000269|PubMed:8262384}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Compositional bias (1); Disulfide bond (12); Domain (5); Glycosylation (5); Metal binding (3); Propeptide (1); Region (2); Signal peptide (1)
Keywords Calcium;Chondrogenesis;Cleavage on pair of basic residues;Cytokine;Developmental protein;Differentiation;Disulfide bond;EGF-like domain;Extracellular matrix;Glycoprotein;Golgi apparatus;Growth factor;Hydrolase;Metal-binding;Metalloprotease;Osteogenesis;Protease;Repeat;Secreted;Signal;Zinc
Interact With B5MFE9
Induction
Subcellular Location SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000250}. Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Modified Residue
Post Translational Modification PTM: Proteolytically activated in the trans-Golgi network by furin-like/paired basic proprotein convertases, cleavage is not required for secretion. {ECO:0000250}.
Signal Peptide SIGNAL 1..?; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 21295563; 22825851;
Motif
Gene Encoded By
Mass 80,674
Kinetics
Metal Binding METAL 176; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 180; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 186; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211
Rhea ID
Cross Reference Brenda 3.4.24.19;