Bmp1
entrez
12153
canonical
uniprot
P98063
canonical
ensembl
ENSMUSG00000022098
resolver
ensp
ENSMUSP00000022693
resolver
ensp
ENSMUSP00000323572
resolver
enst
ENSMUST00000022693
resolver
genesymbol
Bmp1
resolver
uniprot
Q6NZM2
resolver
uniprot_entry
BMP1_MOUSE
resolver
uniprot_sec
Q6NZM2
resolver
activity_regulation
ACTIVITY REGULATION: Activity is increased by the procollagen C-endopeptidase enhancer protein.
uniprot
proteins
amino_acid_sequence
MPGVARPPLPLLSLPLLLLLLLLPRAGRPLDLADYTYDLGEEDAPELLNYKDPCKAAAFLGDIALDEEDLRAFQVQQAAVLRQQTARRPSIKAAGNSSALGGQGTSGQPQRESRGRWRGRPRSRRAATSRPERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAISIGKNCDKFGIVVHELGHVIGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEVQEVESLGETYDFDSIMHYARNTFSRGIFLDTIVPKYEVNGVKPSIGQRTRLSKGDIAQARKLYKCPACGETLQDSTGNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSMDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGGKLPEPIVSTDSRLWVEFRSSSNWVGKGFFAVYEAICGGDVKKDNGHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSNLIGRYCGYEKPDDIKSTSSRLWLKFVSDGSINKAGFAVNFFKEVDECSRPNRGGCEQRCLNTLGSYKCSCDPGYELAPDKRRCEAACGGFLTKLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSEKPEVITSQYNNMRVEFKSDNTVSKKGFKAHFFSDKDECSKDNGGCQQDCVNTFGSYECQCRSGFVLHDNKHDCKEAGCEHKVTSTSGTITSPNWPDKYPSKKECTWAISSTPGHRVKLTFVEMDIESQPECAYDHLEVFDGRDAKAPVLGRFCGSKKPEPVLATGNRMFLRFYSDNSVQRKGFQASHSTECGGQVRADVKTKDLYSHAQFGDNNYPGGVDCEWVIVAEEGYGVELVFQTFEVEEETDCGYDYIELFDGYDSTAPRLGRYCGSGPPEEVYSAGDSVLVKFHSDDTISKKGFHLRYTSTKFQDTLHSRK
uniprot
proteins
ec_number
3.4.24.19
uniprot
proteins
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:28068493, PubMed:8951074). 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}.
uniprot
proteins
mass_dalton
111666
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20181949
uniprot
proteins
pubmed
24419319
uniprot
proteins
pubmed
28068493
uniprot
proteins
pubmed
8174772
uniprot
proteins
pubmed
8951074
uniprot
proteins
sequence_length
991
uniprot
proteins
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.
uniprot
proteins