| IED ID | IndEnz0002014468 |
| Enzyme Type ID | protease014468 |
| Protein Name |
Bone morphogenetic protein 1 BMP-1 EC 3.4.24.19 Mammalian tolloid protein mTld Procollagen C-proteinase PCP |
| Gene Name | Bmp1 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MPGVARPPLPLLSLPLLLLLLLLPRAGRPLDLADYTYDLGEEDAPELLNYKDPCKAAAFLGDIALDEEDLRAFQVQQAAVLRQQTARRPSIKAAGNSSALGGQGTSGQPQRESRGRWRGRPRSRRAATSRPERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAISIGKNCDKFGIVVHELGHVIGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEVQEVESLGETYDFDSIMHYARNTFSRGIFLDTIVPKYEVNGVKPSIGQRTRLSKGDIAQARKLYKCPACGETLQDSTGNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSMDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGGKLPEPIVSTDSRLWVEFRSSSNWVGKGFFAVYEAICGGDVKKDNGHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSNLIGRYCGYEKPDDIKSTSSRLWLKFVSDGSINKAGFAVNFFKEVDECSRPNRGGCEQRCLNTLGSYKCSCDPGYELAPDKRRCEAACGGFLTKLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSEKPEVITSQYNNMRVEFKSDNTVSKKGFKAHFFSDKDECSKDNGGCQQDCVNTFGSYECQCRSGFVLHDNKHDCKEAGCEHKVTSTSGTITSPNWPDKYPSKKECTWAISSTPGHRVKLTFVEMDIESQPECAYDHLEVFDGRDAKAPVLGRFCGSKKPEPVLATGNRMFLRFYSDNSVQRKGFQASHSTECGGQVRADVKTKDLYSHAQFGDNNYPGGVDCEWVIVAEEGYGVELVFQTFEVEEETDCGYDYIELFDGYDSTAPRLGRYCGSGPPEEVYSAGDSVLVKFHSDDTISKKGFHLRYTSTKFQDTLHSRK |
| Enzyme Length | 991 |
| Uniprot Accession Number | P98063 |
| Absorption | |
| Active Site | ACT_SITE 219; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
| Activity Regulation | ACTIVITY REGULATION: Activity is increased by the procollagen C-endopeptidase enhancer protein. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of the C-terminal propeptide at Ala-|-Asp in type I and II procollagens and at Arg-|-Asp in type III.; EC=3.4.24.19; |
| DNA Binding | |
| EC Number | 3.4.24.19 |
| Enzyme Function | FUNCTION: Metalloprotease that plays key roles in regulating the formation of the extracellular matrix (ECM) via processing of various precursor proteins into mature functional enzymes or structural proteins. Thereby participates in several developmental and physiological processes such as cartilage and bone formation, muscle growth and homeostasis, wound healing and tissue repair (PubMed:24419319, PubMed:8951074, PubMed:28068493). Roles in ECM formation include cleavage of the C-terminal propeptides from procollagens such as procollagen I, II and III or the proteolytic activation of the enzyme lysyl oxidase LOX, necessary to formation of covalent cross-links in collagen and elastic fibers (PubMed:20181949). Additional substrates include matricellular thrombospondin-1/THBS1 whose cleavage leads to cell adhesion disruption and TGF-beta activation (By similarity). {ECO:0000250|UniProtKB:P13497, ECO:0000269|PubMed:20181949, ECO:0000269|PubMed:24419319, ECO:0000269|PubMed:28068493, ECO:0000269|PubMed:8951074}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (1); Disulfide bond (19); Domain (8); Frameshift (1); Glycosylation (5); Metal binding (3); Modified residue (2); Propeptide (1); Region (1); Sequence conflict (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;Methylation;Osteogenesis;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:20181949}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:20181949}. Secreted {ECO:0000250|UniProtKB:P13497}. Note=Co-localizes with POSTN in the Golgi. |
| Modified Residue | MOD_RES 939; /note=Omega-N-methylarginine; /evidence=ECO:0000250|UniProtKB:Q9WVM6; MOD_RES 942; /note=Omega-N-methylarginine; /evidence=ECO:0000250|UniProtKB:Q9WVM6 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10331975; 10462412; 10479448; 10896944; 11044609; 11217851; 11518254; 12393877; 12421715; 12466851; 12808086; 1303276; 1346779; 1370487; 14681479; 15071597; 15292192; 1537334; 16087734; 16125875; 16141072; 16602821; 17015622; 17018525; 17391983; 17548836; 18286185; 19079247; 19617627; 1971251; 19914233; 20359476; 20460368; 20658214; 21297990; 21677750; 21697095; 22560297; 22682244; 23103586; 23213481; 24006456; 24019467; 24586749; 24952961; 25131634; 26721501; 27363389; 27760309; 27847137; 27913639; 28000152; 28071719; 28164238; 28923241; 28928204; 29031500; 30446646; 31388055; 3201241; 32209430; 32546759; 33206546; 7798260; 8287471; 8553073; 8661043; 8765971; 9152011; 9555025; |
| Motif | |
| Gene Encoded By | |
| Mass | 111,666 |
| Kinetics | |
| Metal Binding | METAL 218; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 222; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 228; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.19; |