ID BMP1_HUMAN Reviewed; 986 AA. AC P13497; A8K6F5; B2RN46; D3DSR0; Q13292; Q13872; Q14874; Q99421; AC Q99422; Q99423; Q9UL38; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2001, sequence version 2. DT 11-NOV-2015, entry version 181. DE RecName: Full=Bone morphogenetic protein 1; DE Short=BMP-1; DE EC=3.4.24.19; DE AltName: Full=Mammalian tolloid protein; DE Short=mTld; DE AltName: Full=Procollagen C-proteinase; DE Short=PCP; DE Flags: Precursor; GN Name=BMP1; Synonyms=PCOLC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BMP1-3). RC TISSUE=Skin; RX PubMed=8643539; DOI=10.1073/pnas.93.10.5127; RA Li S.W., Sieron A.L., Fertala A., Hojima Y., Arnold W.V., RA Prockop D.J.; RT "The C-proteinase that processes procollagens to fibrillar collagens RT is identical to the protein previously identified as bone morphogenic RT protein-1."; RL Proc. Natl. Acad. Sci. U.S.A. 93:5127-5130(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BMP1-1). RX PubMed=3201241; DOI=10.1126/science.3201241; RA Wozney J.M., Rosen V., Celeste A.J., Mitsock L.M., Whitters M.J., RA Kriz R.W., Hewick R.M., Wang E.A.; RT "Novel regulators of bone formation: molecular clones and RT activities."; RL Science 242:1528-1534(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BMP1-4; BMP1-5 AND BMP1-6). RC TISSUE=Placenta; RX PubMed=9500680; DOI=10.1007/s001090050202; RA Janitz M., Heiser V., Boettcher U., Landt O., Lauster R.; RT "Three alternatively spliced variants of the gene coding for the human RT bone morphogenetic protein-1."; RL J. Mol. Med. 76:141-146(1998). RN [4] RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BMP1-3 AND BMP1-7). RC TISSUE=Placenta; RX PubMed=7798260; RA Takahara K., Lyons G.E., Greenspan D.S.; RT "Bone morphogenetic protein-1 and a mammalian tolloid homologue (mTld) RT are encoded by alternatively spliced transcripts which are RT differentially expressed in some tissues."; RL J. Biol. Chem. 269:32572-32578(1994). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BMP1-5). RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BMP1-3). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP DISULFIDE BOND AT 183-CYS--CYS-186. RX PubMed=11283002; DOI=10.1074/jbc.M010814200; RA Garrigue-Antar L., Barker C., Kadler K.E.; RT "Identification of amino acid residues in bone morphogenetic protein-1 RT important for procollagen C-proteinase activity."; RL J. Biol. Chem. 276:26237-26242(2001). RN [9] RP SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF RP 119-ARG--ARG-120. RX PubMed=12637569; DOI=10.1074/jbc.M213021200; RA Leighton M., Kadler K.E.; RT "Paired basic/Furin-like proprotein convertase cleavage of Pro-BMP-1 RT in the trans-Golgi network."; RL J. Biol. Chem. 278:18478-18484(2003). RN [10] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:R8.1-R8.16(2004). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 121-321, ZINC-BINDING SITES, RP COFACTOR, ACTIVE SITE, AND DISULFIDE BONDS. RX PubMed=18824173; DOI=10.1016/j.jmb.2008.09.029; RA Mac Sweeney A., Gil-Parrado S., Vinzenz D., Bernardi A., Hein A., RA Bodendorf U., Erbel P., Logel C., Gerhartz B.; RT "Structural basis for the substrate specificity of bone morphogenetic RT protein 1/tolloid-like metalloproteases."; RL J. Mol. Biol. 384:228-239(2008). RN [12] RP VARIANT [LARGE SCALE ANALYSIS] HIS-45. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). RN [13] RP VARIANT OI13 ARG-12, CHARACTERIZATION OF VARIANT OI13 ARG-12, AND RP INVOLVEMENT IN OI13. RX PubMed=22482805; DOI=10.1016/j.ajhg.2012.02.026; RA Asharani P.V., Keupp K., Semler O., Wang W., Li Y., Thiele H., RA Yigit G., Pohl E., Becker J., Frommolt P., Sonntag C., Altmuller J., RA Zimmermann K., Greenspan D.S., Akarsu N.A., Netzer C., Schonau E., RA Wirth R., Hammerschmidt M., Nurnberg P., Wollnik B., Carney T.J.; RT "Attenuated BMP1 function compromises osteogenesis, leading to bone RT fragility in humans and zebrafish."; RL Am. J. Hum. Genet. 90:661-674(2012). RN [14] RP VARIANT OI13 LEU-249, AND CHARACTERIZATION OF VARIANT OI13 LEU-249. RX PubMed=22052668; DOI=10.1002/humu.21647; RA Martinez-Glez V., Valencia M., Caparros-Martin J.A., Aglan M., RA Temtamy S., Tenorio J., Pulido V., Lindert U., Rohrbach M., Eyre D., RA Giunta C., Lapunzina P., Ruiz-Perez V.L.; RT "Identification of a mutation causing deficient BMP1/mTLD proteolytic RT activity in autosomal recessive osteogenesis imperfecta."; RL Hum. Mutat. 33:343-350(2012). RN [15] RP VARIANT OI13 VAL-270, AND CHARACTERIZATION OF VARIANT OI13 VAL-270. RX PubMed=25402547; DOI=10.1002/humu.22731; RA Cho S.Y., Asharani P.V., Kim O.H., Iida A., Miyake N., Matsumoto N., RA Nishimura G., Ki C.S., Hong G., Kim S.J., Sohn Y.B., Park S.W., RA Lee J., Kwun Y., Carney T.J., Huh R., Ikegawa S., Jin D.K.; RT "Identification and in vivo functional characterization of novel RT compound heterozygous BMP1 variants in osteogenesis imperfecta."; RL Hum. Mutat. 36:191-195(2015). CC -!- FUNCTION: Cleaves the C-terminal propeptides of procollagen I, II CC and III. Induces cartilage and bone formation. May participate in CC dorsoventral patterning during early development by cleaving CC chordin (CHRD). Responsible for the proteolytic activation of CC lysyl oxidase LOX. CC -!- CATALYTIC ACTIVITY: Cleavage of the C-terminal propeptide at CC Ala-|-Asp in type I and II procollagens and at Arg-|-Asp in type CC III. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:18824173}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:18824173}; CC -!- ENZYME REGULATION: Activity is increased by the procollagen C- CC endopeptidase enhancer protein. CC -!- SUBUNIT: Interacts with POSTN, the interaction promotes deposition CC on the extracellular matrix. {ECO:0000250}. CC -!- INTERACTION: CC O14793:MSTN; NbExp=2; IntAct=EBI-489827, EBI-8542977; CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network CC {ECO:0000269|PubMed:12637569}. Secreted, extracellular space, CC extracellular matrix {ECO:0000269|PubMed:12637569}. Note=Co- CC localizes with POSTN in the Golgi. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=BMP1-3; CC IsoId=P13497-1; Sequence=Displayed; CC Name=BMP1-1; CC IsoId=P13497-2; Sequence=VSP_005461, VSP_005462; CC Name=BMP1-2; CC IsoId=P13497-7; Sequence=Not described; CC Name=BMP1-4; CC IsoId=P13497-3; Sequence=VSP_005463, VSP_005464; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay.; CC Name=BMP1-5; CC IsoId=P13497-4; Sequence=VSP_005465, VSP_005466; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay.; CC Name=BMP1-6; CC IsoId=P13497-5; Sequence=VSP_005467, VSP_005468; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay.; CC Name=BMP1-7; CC IsoId=P13497-6; Sequence=VSP_005469, VSP_005470; CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- PTM: Proteolytically activated in the trans-Golgi network by CC furin-like/paired basic proprotein convertases, cleavage is not CC required for secretion. {ECO:0000269|PubMed:12637569}. CC -!- DISEASE: Osteogenesis imperfecta 13 (OI13) [MIM:614856]: An CC autosomal recessive form of osteogenesis imperfecta, a connective CC tissue disorder characterized by low bone mass, bone fragility and CC susceptibility to fractures after minimal trauma. Disease severity CC ranges from very mild forms without fractures to intrauterine CC fractures and perinatal lethality. Extraskeletal manifestations, CC which affect a variable number of patients, are dentinogenesis CC imperfecta, hearing loss, and blue sclerae. OI13 is characterized CC by normal teeth, faint blue sclerae, severe growth deficiency, CC borderline osteoporosis, severe bone deformity, and recurrent CC fractures affecting both upper and lower limbs. CC {ECO:0000269|PubMed:22052668, ECO:0000269|PubMed:22482805, CC ECO:0000269|PubMed:25402547}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the peptidase M12A family. {ECO:0000305}. CC -!- SIMILARITY: Contains 5 CUB domains. {ECO:0000255|PROSITE- CC ProRule:PRU00059}. CC -!- SIMILARITY: Contains 2 EGF-like domains. {ECO:0000255|PROSITE- CC ProRule:PRU00076}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U50330; AAA93462.1; -; mRNA. DR EMBL; M22488; AAA51833.1; -; mRNA. DR EMBL; Y08723; CAA69973.1; -; mRNA. DR EMBL; Y08724; CAA69974.1; -; mRNA. DR EMBL; Y08725; CAA69975.1; -; mRNA. DR EMBL; L35278; AAC41703.1; -; mRNA. DR EMBL; L35279; AAC41710.1; -; mRNA. DR EMBL; AK291620; BAF84309.1; -; mRNA. DR EMBL; CH471080; EAW63698.1; -; Genomic_DNA. DR EMBL; CH471080; EAW63703.1; -; Genomic_DNA. DR EMBL; CH471080; EAW63704.1; -; Genomic_DNA. DR EMBL; BC136679; AAI36680.1; -; mRNA. DR CCDS; CCDS34856.1; -. [P13497-2] DR CCDS; CCDS6026.1; -. [P13497-1] DR PIR; A37278; BMHU1. DR PIR; A58788; A58788. DR PIR; B58788; B58788. DR RefSeq; NP_001190.1; NM_001199.3. [P13497-2] DR RefSeq; NP_006120.1; NM_006129.4. [P13497-1] DR RefSeq; XP_011542919.1; XM_011544617.1. [P13497-4] DR UniGene; Hs.1274; -. DR PDB; 3EDG; X-ray; 1.27 A; A=121-321. DR PDB; 3EDH; X-ray; 1.25 A; A=121-321. DR PDBsum; 3EDG; -. DR PDBsum; 3EDH; -. DR ProteinModelPortal; P13497; -. DR SMR; P13497; 121-976. DR BioGrid; 107117; 38. DR DIP; DIP-33403N; -. DR IntAct; P13497; 6. DR MINT; MINT-1394084; -. DR STRING; 9606.ENSP00000305714; -. DR BindingDB; P13497; -. DR ChEMBL; CHEMBL3898; -. DR GuidetoPHARMACOLOGY; 2333; -. DR MEROPS; M12.005; -. DR PhosphoSite; P13497; -. DR BioMuta; BMP1; -. DR DMDM; 13124688; -. DR MaxQB; P13497; -. DR PaxDb; P13497; -. DR PeptideAtlas; P13497; -. DR PRIDE; P13497; -. DR Ensembl; ENST00000306349; ENSP00000306121; ENSG00000168487. [P13497-2] DR Ensembl; ENST00000306385; ENSP00000305714; ENSG00000168487. [P13497-1] DR Ensembl; ENST00000471755; ENSP00000428665; ENSG00000168487. [P13497-4] DR Ensembl; ENST00000520970; ENSP00000428332; ENSG00000168487. [P13497-2] DR Ensembl; ENST00000521385; ENSP00000430406; ENSG00000168487. [P13497-5] DR GeneID; 649; -. DR KEGG; hsa:649; -. DR UCSC; uc003xbb.3; human. [P13497-2] DR UCSC; uc003xbg.3; human. [P13497-1] DR CTD; 649; -. DR GeneCards; BMP1; -. DR HGNC; HGNC:1067; BMP1. DR HPA; HPA014572; -. DR MIM; 112264; gene. DR MIM; 614856; phenotype. DR neXtProt; NX_P13497; -. DR Orphanet; 216812; Osteogenesis imperfecta type 3. DR PharmGKB; PA25377; -. DR eggNOG; KOG3714; Eukaryota. DR eggNOG; ENOG410ZPX7; LUCA. DR GeneTree; ENSGT00760000119018; -. DR HOVERGEN; HBG004859; -. DR InParanoid; P13497; -. DR KO; K05502; -. DR OMA; FCGGKLP; -. DR OrthoDB; EOG7N8ZTV; -. DR PhylomeDB; P13497; -. DR TreeFam; TF314351; -. DR BRENDA; 3.4.24.19; 2681. DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix. DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes. DR Reactome; R-HSA-194223; HDL-mediated lipid transport. DR Reactome; R-HSA-2214320; Anchoring fibril formation. DR Reactome; R-HSA-2243919; Crosslinking of collagen fibrils. DR ChiTaRS; BMP1; human. DR EvolutionaryTrace; P13497; -. DR GeneWiki; Bone_morphogenetic_protein_1; -. DR GenomeRNAi; 649; -. DR NextBio; 2632; -. DR PMAP-CutDB; P13497; -. DR PRO; PR:P13497; -. DR Proteomes; UP000005640; Chromosome 8. DR Bgee; P13497; -. DR CleanEx; HS_BMP1; -. DR ExpressionAtlas; P13497; baseline and differential. DR Genevisible; P13497; HS. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0031988; C:membrane-bounded vesicle; IEA:Ensembl. DR GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004222; F:metalloendopeptidase activity; TAS:Reactome. DR GO; GO:0008237; F:metallopeptidase activity; NAS:UniProtKB. DR GO; GO:0008233; F:peptidase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0001502; P:cartilage condensation; TAS:ProtInc. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome. DR GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome. DR GO; GO:0042157; P:lipoprotein metabolic process; TAS:Reactome. DR GO; GO:0007275; P:multicellular organismal development; TAS:ProtInc. DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW. DR GO; GO:0061036; P:positive regulation of cartilage development; IDA:MGI. DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB. DR GO; GO:0001501; P:skeletal system development; NAS:UniProtKB. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR Gene3D; 2.60.120.290; -; 5. DR Gene3D; 3.40.390.10; -; 1. DR InterPro; IPR015446; BMP_1/tolloid-like. DR InterPro; IPR000859; CUB_dom. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR009030; Growth_fac_rcpt_N_dom. DR InterPro; IPR024079; MetalloPept_cat_dom. DR InterPro; IPR001506; Peptidase_M12A. DR InterPro; IPR006026; Peptidase_Metallo. DR Pfam; PF01400; Astacin; 1. DR Pfam; PF00431; CUB; 5. DR Pfam; PF07645; EGF_CA; 1. DR PIRSF; PIRSF001199; BMP_1/tolloid-like; 1. DR PRINTS; PR00480; ASTACIN. DR SMART; SM00042; CUB; 5. DR SMART; SM00179; EGF_CA; 2. DR SMART; SM00235; ZnMc; 1. DR SUPFAM; SSF49854; SSF49854; 5. DR SUPFAM; SSF57184; SSF57184; 2. DR PROSITE; PS00010; ASX_HYDROXYL; 2. DR PROSITE; PS01180; CUB; 5. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS50026; EGF_3; 2. DR PROSITE; PS01187; EGF_CA; 2. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Chondrogenesis; KW Cleavage on pair of basic residues; Complete proteome; Cytokine; KW Developmental protein; Differentiation; Disease mutation; KW Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein; KW Golgi apparatus; Growth factor; Hydrolase; Metal-binding; KW Metalloprotease; Osteogenesis; Osteogenesis imperfecta; Polymorphism; KW Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen. FT SIGNAL 1 22 {ECO:0000255}. FT PROPEP 23 120 {ECO:0000255}. FT /FTId=PRO_0000028889. FT CHAIN 121 986 Bone morphogenetic protein 1. FT /FTId=PRO_0000028890. FT DOMAIN 322 434 CUB 1. {ECO:0000255|PROSITE- FT ProRule:PRU00059}. FT DOMAIN 435 546 CUB 2. {ECO:0000255|PROSITE- FT ProRule:PRU00059}. FT DOMAIN 547 588 EGF-like 1; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 591 703 CUB 3. {ECO:0000255|PROSITE- FT ProRule:PRU00059}. FT DOMAIN 704 743 EGF-like 2; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 747 859 CUB 4. {ECO:0000255|PROSITE- FT ProRule:PRU00059}. FT DOMAIN 860 976 CUB 5. {ECO:0000255|PROSITE- FT ProRule:PRU00059}. FT REGION 121 321 Metalloprotease. FT ACT_SITE 214 214 {ECO:0000255|PROSITE-ProRule:PRU10095, FT ECO:0000269|PubMed:18824173}. FT METAL 213 213 Zinc; catalytic. FT METAL 217 217 Zinc; catalytic. FT METAL 223 223 Zinc; catalytic. FT CARBOHYD 91 91 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 142 142 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 332 332 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 363 363 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 599 599 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 163 319 {ECO:0000269|PubMed:18824173}. FT DISULFID 183 205 {ECO:0000269|PubMed:18824173}. FT DISULFID 185 186 {ECO:0000269|PubMed:18824173}. FT DISULFID 322 348 {ECO:0000250}. FT DISULFID 375 397 {ECO:0000250}. FT DISULFID 435 461 {ECO:0000250}. FT DISULFID 488 510 {ECO:0000250}. FT DISULFID 551 563 {ECO:0000250}. FT DISULFID 559 572 {ECO:0000250}. FT DISULFID 574 587 {ECO:0000250}. FT DISULFID 591 617 {ECO:0000250}. FT DISULFID 644 666 {ECO:0000250}. FT DISULFID 707 718 {ECO:0000250}. FT DISULFID 714 727 {ECO:0000250}. FT DISULFID 729 742 {ECO:0000250}. FT DISULFID 747 773 {ECO:0000250}. FT DISULFID 800 822 {ECO:0000250}. FT DISULFID 860 890 {ECO:0000250}. FT DISULFID 917 939 {ECO:0000250}. FT VAR_SEQ 245 302 QEYNFLKMEPQEVESLGETYDFDSIMHYARNTFSRGIFLDT FT IVPKYEVNGVKPPIGQR -> VLHSSLLLLSCGSRNGASFP FT CSLESSTHQALCWTGLFLRPSPFPRLPLAAPRTLRAGV FT (in isoform BMP1-4). FT {ECO:0000303|PubMed:9500680}. FT /FTId=VSP_005463. FT VAR_SEQ 303 986 Missing (in isoform BMP1-4). FT {ECO:0000303|PubMed:9500680}. FT /FTId=VSP_005464. FT VAR_SEQ 589 622 AACGGFLTKLNGSITSPGWPKEYPPNKNCIWQLV -> GCY FT DLQVGKPLLWDRHCFRLSTHGPEMLGTALRG (in FT isoform BMP1-5). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:9500680}. FT /FTId=VSP_005465. FT VAR_SEQ 623 986 Missing (in isoform BMP1-5). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:9500680}. FT /FTId=VSP_005466. FT VAR_SEQ 703 823 DKDECSKDNGGCQQDCVNTFGSYECQCRSGFVLHDNKHDCK FT EAGCDHKVTSTSGTITSPNWPDKYPSKKECTWAISSTPGHR FT VKLTFMEMDIESQPECAYDHLEVFDGRDAKAPVLGRFCG FT -> VLEGAGDRHSHLSGLELLLCPHALVDTVPAPPSALHGD FT THAHTHTHVHTHCPIAQETCRGPPLGASRLSPQGPGHLTLA FT PQEGSYLDFWDTHRGDPKPRRRRKSLKTFSLTPATFRGIWA FT L (in isoform BMP1-7). {ECO:0000305}. FT /FTId=VSP_005469. FT VAR_SEQ 703 730 DKDECSKDNGGCQQDCVNTFGSYECQCR -> EKRPALQPP FT RGRPHQLKFRVQKRNRTPQ (in isoform BMP1-1). FT {ECO:0000303|PubMed:3201241}. FT /FTId=VSP_005461. FT VAR_SEQ 703 717 DKDECSKDNGGCQQD -> GGELFGLLGHPPRRP (in FT isoform BMP1-6). FT {ECO:0000303|PubMed:9500680}. FT /FTId=VSP_005467. FT VAR_SEQ 718 986 Missing (in isoform BMP1-6). FT {ECO:0000303|PubMed:9500680}. FT /FTId=VSP_005468. FT VAR_SEQ 731 986 Missing (in isoform BMP1-1). FT {ECO:0000303|PubMed:3201241}. FT /FTId=VSP_005462. FT VAR_SEQ 824 986 Missing (in isoform BMP1-7). FT {ECO:0000305}. FT /FTId=VSP_005470. FT VARIANT 12 12 G -> R (in OI13; the mutation leads to FT severely reduced post-translational N- FT glycosylation of the protein and impairs FT protein secretion; leads to both reduced FT secretion and subsequent reduced FT processing of the substrates CHRD and FT COL1A1; dbSNP:rs318240762). FT {ECO:0000269|PubMed:22482805}. FT /FTId=VAR_069096. FT VARIANT 45 45 D -> H (in a breast cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_036141. FT VARIANT 249 249 F -> L (in OI13; leads to a protein with FT deficient procollagen I C-terminal FT propeptide proteolytic activity). FT {ECO:0000269|PubMed:22052668}. FT /FTId=VAR_067224. FT VARIANT 270 270 M -> V (in OI13; partial loss of FT activity). {ECO:0000269|PubMed:25402547}. FT /FTId=VAR_072248. FT VARIANT 719 719 V -> I (in dbSNP:rs11996036). FT /FTId=VAR_051584. FT MUTAGEN 119 120 RR->AA: Doesn't abolish secretion. FT {ECO:0000269|PubMed:12637569}. FT CONFLICT 748 748 D -> N (in Ref. 4; AAC41710). FT {ECO:0000305}. FT CONFLICT 934 934 R -> S (in Ref. 4; AAC41710). FT {ECO:0000305}. FT HELIX 126 128 {ECO:0000244|PDB:3EDH}. FT HELIX 131 133 {ECO:0000244|PDB:3EDH}. FT STRAND 134 139 {ECO:0000244|PDB:3EDH}. FT HELIX 145 161 {ECO:0000244|PDB:3EDH}. FT STRAND 165 168 {ECO:0000244|PDB:3EDH}. FT STRAND 173 180 {ECO:0000244|PDB:3EDH}. FT STRAND 194 201 {ECO:0000244|PDB:3EDH}. FT HELIX 203 205 {ECO:0000244|PDB:3EDH}. FT HELIX 208 219 {ECO:0000244|PDB:3EDH}. FT HELIX 224 226 {ECO:0000244|PDB:3EDH}. FT HELIX 230 232 {ECO:0000244|PDB:3EDH}. FT STRAND 234 236 {ECO:0000244|PDB:3EDH}. FT HELIX 238 240 {ECO:0000244|PDB:3EDH}. FT HELIX 246 249 {ECO:0000244|PDB:3EDH}. FT HELIX 254 256 {ECO:0000244|PDB:3EDH}. FT TURN 274 277 {ECO:0000244|PDB:3EDH}. FT STRAND 278 280 {ECO:0000244|PDB:3EDH}. FT STRAND 285 290 {ECO:0000244|PDB:3EDH}. FT HELIX 307 316 {ECO:0000244|PDB:3EDH}. SQ SEQUENCE 986 AA; 111249 MW; F89201913AC3CBEA CRC64; MPGVARLPLL LGLLLLPRPG RPLDLADYTY DLAEEDDSEP LNYKDPCKAA AFLGDIALDE EDLRAFQVQQ AVDLRRHTAR KSSIKAAVPG NTSTPSCQST NGQPQRGACG RWRGRSRSRR AATSRPERVW PDGVIPFVIG GNFTGSQRAV FRQAMRHWEK HTCVTFLERT DEDSYIVFTY RPCGCCSYVG RRGGGPQAIS IGKNCDKFGI VVHELGHVVG FWHEHTRPDR DRHVSIVREN IQPGQEYNFL KMEPQEVESL GETYDFDSIM HYARNTFSRG IFLDTIVPKY EVNGVKPPIG QRTRLSKGDI AQARKLYKCP ACGETLQDST GNFSSPEYPN GYSAHMHCVW RISVTPGEKI ILNFTSLDLY RSRLCWYDYV EVRDGFWRKA PLRGRFCGSK LPEPIVSTDS RLWVEFRSSS NWVGKGFFAV YEAICGGDVK KDYGHIQSPN YPDDYRPSKV CIWRIQVSEG FHVGLTFQSF EIERHDSCAY DYLEVRDGHS ESSTLIGRYC GYEKPDDIKS TSSRLWLKFV SDGSINKAGF AVNFFKEVDE CSRPNRGGCE QRCLNTLGSY KCSCDPGYEL APDKRRCEAA CGGFLTKLNG SITSPGWPKE YPPNKNCIWQ LVAPTQYRIS LQFDFFETEG NDVCKYDFVE VRSGLTADSK LHGKFCGSEK PEVITSQYNN MRVEFKSDNT VSKKGFKAHF FSDKDECSKD NGGCQQDCVN TFGSYECQCR SGFVLHDNKH DCKEAGCDHK VTSTSGTITS PNWPDKYPSK KECTWAISST PGHRVKLTFM EMDIESQPEC AYDHLEVFDG RDAKAPVLGR FCGSKKPEPV LATGSRMFLR FYSDNSVQRK GFQASHATEC GGQVRADVKT KDLYSHAQFG DNNYPGGVDC EWVIVAEEGY GVELVFQTFE VEEETDCGYD YMELFDGYDS TAPRLGRYCG SGPPEEVYSA GDSVLVKFHS DDTITKKGFH LRYTSTKFQD TLHSRK //