| IED ID | IndEnz0002016512 |
| Enzyme Type ID | protease016512 |
| Protein Name |
Bone morphogenetic protein 1 BMP-1 EC 3.4.24.19 Mammalian tolloid protein mTld Procollagen C-proteinase PCP |
| Gene Name | BMP1 PCOLC |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MPGVARLPLLLGLLLLPRPGRPLDLADYTYDLAEEDDSEPLNYKDPCKAAAFLGDIALDEEDLRAFQVQQAVDLRRHTARKSSIKAAVPGNTSTPSCQSTNGQPQRGACGRWRGRSRSRRAATSRPERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAISIGKNCDKFGIVVHELGHVVGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEPQEVESLGETYDFDSIMHYARNTFSRGIFLDTIVPKYEVNGVKPPIGQRTRLSKGDIAQARKLYKCPACGETLQDSTGNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSLDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGSKLPEPIVSTDSRLWVEFRSSSNWVGKGFFAVYEAICGGDVKKDYGHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSTLIGRYCGYEKPDDIKSTSSRLWLKFVSDGSINKAGFAVNFFKEVDECSRPNRGGCEQRCLNTLGSYKCSCDPGYELAPDKRRCEAACGGFLTKLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSEKPEVITSQYNNMRVEFKSDNTVSKKGFKAHFFSDKDECSKDNGGCQQDCVNTFGSYECQCRSGFVLHDNKHDCKEAGCDHKVTSTSGTITSPNWPDKYPSKKECTWAISSTPGHRVKLTFMEMDIESQPECAYDHLEVFDGRDAKAPVLGRFCGSKKPEPVLATGSRMFLRFYSDNSVQRKGFQASHATECGGQVRADVKTKDLYSHAQFGDNNYPGGVDCEWVIVAEEGYGVELVFQTFEVEEETDCGYDYMELFDGYDSTAPRLGRYCGSGPPEEVYSAGDSVLVKFHSDDTITKKGFHLRYTSTKFQDTLHSRK |
| Enzyme Length | 986 |
| Uniprot Accession Number | P13497 |
| Absorption | |
| Active Site | ACT_SITE 214; /evidence="ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000269|PubMed:18824173" |
| 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 (PubMed:33206546). Thereby participates in several developmental and physiological processes such as cartilage and bone formation, muscle growth and homeostasis, wound healing and tissue repair (PubMed:33169406, PubMed:32636307). 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:31152061, PubMed:33206546). Additional substrates include matricellular thrombospondin-1/THBS1 whose cleavage leads to cell adhesion disruption and TGF-beta activation (PubMed:32636307). {ECO:0000269|PubMed:31152061, ECO:0000269|PubMed:32636307, ECO:0000269|PubMed:33169406, ECO:0000269|PubMed:33206546}.; FUNCTION: [Isoform BMP1-3]: Plays an important role in bone repair by acting as a coactivator of BMP7. {ECO:0000269|PubMed:21453682}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (10); Beta strand (9); Chain (1); Compositional bias (1); Disulfide bond (19); Domain (8); Glycosylation (5); Helix (11); Metal binding (3); Modified residue (2); Mutagenesis (1); Natural variant (5); Propeptide (1); Region (1); Sequence conflict (2); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Alternative splicing;Calcium;Chondrogenesis;Cleavage on pair of basic residues;Cytokine;Developmental protein;Differentiation;Disease variant;Disulfide bond;EGF-like domain;Extracellular matrix;Glycoprotein;Golgi apparatus;Growth factor;Hydrolase;Metal-binding;Metalloprotease;Methylation;Osteogenesis;Osteogenesis imperfecta;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
| Interact With | Itself; Q9H2X0; P20908; O14793; Q15113; P07585; P97299 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:12637569}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:12637569}. Secreted {ECO:0000269|PubMed:33206546}. Note=Co-localizes with POSTN in the Golgi. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform BMP1-3]: Secreted {ECO:0000269|PubMed:21453682}. |
| Modified Residue | MOD_RES 934; /note=Omega-N-methylarginine; /evidence=ECO:0000250|UniProtKB:Q9WVM6; MOD_RES 937; /note=Omega-N-methylarginine; /evidence=ECO:0000250|UniProtKB:Q9WVM6 |
| 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:0000269|PubMed:12637569}. |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (8) |
| Cross Reference PDB | 3EDG; 3EDH; 6BSL; 6BSM; 6BTN; 6BTO; 6BTP; 6BTQ; |
| Mapped Pubmed ID | 10479448; 11313359; 11741999; 11986329; 12646579; 12684035; 15525470; 15591058; 15868410; 16169070; 16548525; 17071617; 17407447; 17548836; 17580958; 18624398; 18658137; 19812315; 20043912; 2253219; 23829672; 25543063; 26496610; 30034610; 3095317; 3223920; 3905801; 8636146; 8920930; 9428515; |
| Motif | |
| Gene Encoded By | |
| Mass | 111,249 |
| Kinetics | |
| Metal Binding | METAL 213; /note="Zinc; via tele nitrogen; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000269|PubMed:18824173"; METAL 217; /note="Zinc; via tele nitrogen; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000269|PubMed:18824173"; METAL 223; /note="Zinc; via tele nitrogen; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000269|PubMed:18824173" |
| Rhea ID | |
| Cross Reference Brenda | 2.7.11.4;3.4.24.19;3.4.24.21; |