Bone morphogenetic protein 1, also known as BMP1, is a protein which in humans is encoded by the BMP1gene.[5][6] There are seven isoforms of the protein created by alternate splicing.
BMP1 belongs to the peptidase M12A family of bone morphogenetic proteins (BMPs). It induces bone and cartilage development. Unlike other BMPs, it does not belong to the TGFβ superfamily. It was initially discovered to work like other BMPs by inducing bone and cartilage development. It however, is a metalloprotease that cleaves the C-terminus of procollagen I, II and III. It has an astacin-like protease domain.
It has been shown to cleave laminin 5 and is localized in the basal epithelial layer of bovine skin.
The BMP1 locus encodes a protein that is capable of inducing formation of cartilage in vivo. Although other bone morphogenetic proteins are members of the TGF-beta superfamily, BMP1 encodes a protein that is not closely related to other known growth factors. BMP1 protein and procollagen C proteinase (PCP), a secreted metalloprotease requiring calcium and needed for cartilage and bone formation, are identical. PCP or BMP1 protein cleaves the C-terminal propeptides of procollagen I, II, and III and its activity is increased by the procollagen C-endopeptidase enhancer protein. The BMP1 gene is expressed as alternatively spliced variants that share an N-terminal protease domain but differ in their C-terminal region[5]
Structureedit
A partial structure of BMP1 was determined through X-Ray diffraction with a resolution of 1.27 Å.[7] Crystallization experiments were done by vapor diffusion at a pH of 7.5. This is important because it is close to the pH of the human body, where BMP1 resides in vivo. This BMP1 fragment is 202 residues in length. Its secondary structure is made up of 30% helices, or 10 helices, 61 residues in length, and 15% beta sheets, or 11 strands, 32 residues in length. It contains ligands of an acetyl group and a Zinc ion.
A Ramachandran plot was constructed for BMP1.[8] This plot shows that BMP1 most prefers Phi and Psi angles (Phi, Psi) of around (-60°,-45°) and (-60°, 140°). These preferred angles are an estimate of the most clustered data of the Ramachandran plot. The preferred region is much greater in range. 97% of the residues were in preferred regions and 100% of the residues were in the allowed region, with no outliers.
Referencesedit
^ abcGRCh38: Ensembl release 89: ENSG00000168487 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000022098 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ab"Entrez Gene: BMP1 bone morphogenetic protein 1".
^Tabas JA, Zasloff M, Wasmuth JJ, Emanuel BS, Altherr MR, McPherson JD, Wozney JM, Kaplan FS (February 1991). "Bone morphogenetic protein: chromosomal localization of human genes for BMP1, BMP2A, and BMP3". Genomics. 9 (2): 283–9. doi:10.1016/0888-7543(91)90254-C. PMID 2004778.
^PDB: 3EDG; Mac Sweeney A, Gil-Parrado S, Vinzenz D, Bernardi A, Hein A, Bodendorf U, Erbel P, Logel C, Gerhartz B (December 2008). "Structural basis for the substrate specificity of bone morphogenetic protein 1/tolloid-like metalloproteases". J. Mol. Biol. 384 (1): 228–39. doi:10.1016/j.jmb.2008.09.029. PMID 18824173.
^(PDF). www.rcsb.org. Archived from the original (PDF) on 2012-10-12.
Further readingedit
Tabas JA, Zasloff M, Wasmuth JJ, et al. (1991). "Bone morphogenetic protein: chromosomal localization of human genes for BMP1, BMP2A, and BMP3". Genomics. 9 (2): 283–9. doi:10.1016/0888-7543(91)90254-C. PMID 2004778.
Wozney JM, Rosen V, Celeste AJ, et al. (1989). "Novel regulators of bone formation: molecular clones and activities". Science. 242 (4885): 1528–34. doi:10.1126/science.3201241. PMID 3201241.
Takahara K, Lyons GE, Greenspan DS (1995). "Bone morphogenetic protein-1 and a mammalian tolloid homologue (mTld) are encoded by alternatively spliced transcripts which are differentially expressed in some tissues". J. Biol. Chem. 269 (51): 32572–8. doi:10.1016/S0021-9258(18)31672-7. PMID 7798260.
Yoshiura K, Tamura T, Hong HS, et al. (1993). "Mapping of the bone morphogenetic protein 1 gene (BMP1) to 8p21: removal of BMP1 from candidacy for the bone disorder in Langer-Giedion syndrome". Cytogenet. Cell Genet. 64 (3–4): 208–9. doi:10.1159/000133577. PMID 8404039.
Takahara K, Lee S, Wood S, Greenspan DS (1996). "Structural organization and genetic localization of the human bone morphogenetic protein 1/mammalian tolloid gene". Genomics. 29 (1): 9–15. doi:10.1006/geno.1995.1209. PMID 8530106.
Kessler E, Takahara K, Biniaminov L, et al. (1996). "Bone morphogenetic protein-1: the type I procollagen C-proteinase". Science. 271 (5247): 360–2. Bibcode:1996Sci...271..360K. doi:10.1126/science.271.5247.360. PMID 8553073. S2CID 26378870.
Li SW, Sieron AL, Fertala A, et al. (1996). "The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1". Proc. Natl. Acad. Sci. U.S.A. 93 (10): 5127–30. Bibcode:1996PNAS...93.5127L. doi:10.1073/pnas.93.10.5127. PMC39418. PMID 8643539.
Janitz M, Heiser V, Böttcher U, et al. (1998). "Three alternatively spliced variants of the gene coding for the human bone morphogenetic protein-1". J. Mol. Med. 76 (2): 141–6. doi:10.1007/s001090050202. PMID 9500680. S2CID 26374071.
Scott IC, Blitz IL, Pappano WN, et al. (1999). "Mammalian BMP-1/Tolloid-related metalloproteinases, including novel family member mammalian Tolloid-like 2, have differential enzymatic activities and distributions of expression relevant to patterning and skeletogenesis". Dev. Biol. 213 (2): 283–300. doi:10.1006/dbio.1999.9383. PMID 10479448.
Amano S, Scott IC, Takahara K, et al. (2000). "Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 gamma 2 chain". J. Biol. Chem. 275 (30): 22728–35. doi:10.1074/jbc.M002345200. PMID 10806203.
Scott IC, Blitz IL, Pappano WN, et al. (2001). "Homologues of Twisted gastrulation are extracellular cofactors in antagonism of BMP signalling". Nature. 410 (6827): 475–8. Bibcode:2001Natur.410..475S. doi:10.1038/35068572. PMID 11260715. S2CID 4392365.
Garrigue-Antar L, Barker C, Kadler KE (2001). "Identification of amino acid residues in bone morphogenetic protein-1 important for procollagen C-proteinase activity". J. Biol. Chem. 276 (28): 26237–42. doi:10.1074/jbc.M010814200. PMID 11283002.
Unsöld C, Pappano WN, Imamura Y, et al. (2002). "Biosynthetic processing of the pro-alpha 1(V)2pro-alpha 2(V) collagen heterotrimer by bone morphogenetic protein-1 and furin-like proprotein convertases". J. Biol. Chem. 277 (7): 5596–602. doi:10.1074/jbc.M110003200. PMID 11741999.
Rattenholl A, Pappano WN, Koch M, et al. (2002). "Proteinases of the bone morphogenetic protein-1 family convert procollagen VII to mature anchoring fibril collagen". J. Biol. Chem. 277 (29): 26372–8. doi:10.1074/jbc.M203247200. PMID 11986329.
Garrigue-Antar L, Hartigan N, Kadler KE (2003). "Post-translational modification of bone morphogenetic protein-1 is required for secretion and stability of the protein". J. Biol. Chem. 277 (45): 43327–34. doi:10.1074/jbc.M207342200. PMID 12218058.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC139241. PMID 12477932.
Hartigan N, Garrigue-Antar L, Kadler KE (2003). "Bone morphogenetic protein-1 (BMP-1). Identification of the minimal domain structure for procollagen C-proteinase activity". J. Biol. Chem. 278 (20): 18045–9. doi:10.1074/jbc.M211448200. PMID 12637537.
Leighton M, Kadler KE (2003). "Paired basic/Furin-like proprotein convertase cleavage of Pro-BMP-1 in the trans-Golgi network". J. Biol. Chem. 278 (20): 18478–84. doi:10.1074/jbc.M213021200. PMID 12637569.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Hillman RT, Green RE, Brenner SE (2005). "An unappreciated role for RNA surveillance". Genome Biol. 5 (2): R8. doi:10.1186/gb-2004-5-2-r8. PMC395752. PMID 14759258.
External linksedit
bone+morphogenetic+protein+1 at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Human BMP1 genome location and BMP1 gene details page in the UCSC Genome Browser.
Human PCP2 genome location and PCP2 gene details page in the UCSC Genome Browser.
bone, morphogenetic, protein, also, known, bmp1, protein, which, humans, encoded, bmp1, gene, there, seven, isoforms, protein, created, alternate, splicing, bmp1available, structurespdbortholog, search, pdbe, rcsblist, codes3edg, 3edhidentifiersaliasesbmp1, bo. Bone morphogenetic protein 1 also known as BMP1 is a protein which in humans is encoded by the BMP1 gene 5 6 There are seven isoforms of the protein created by alternate splicing BMP1Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes3EDG 3EDHIdentifiersAliasesBMP1 bone morphogenetic protein 1 OI13 PCOLC PCP PCP2 TLDExternal IDsOMIM 112264 MGI 88176 HomoloGene 55955 GeneCards BMP1 OMA BMP1 orthologsGene location Human Chr Chromosome 8 human 1 Band8p21 3Start22 165 140 bp 1 End22 212 326 bp 1 Gene location Mouse Chr Chromosome 14 mouse 2 Band14 D2 14 36 32 cMStart70 474 558 bp 2 End70 520 234 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed instromal cell of endometriumleft uterine tubeleft coronary arterycanal of the cervixright coronary arterygastric mucosaascending aortaplacentatibial nerveright lungTop expressed incerebellar cortexlipbody of femurexternal carotid arteryinternal carotid arterycalvariamolarcerebellar vermisascending aortaankle jointMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functioncalcium ion binding zinc ion binding metal ion binding peptidase activity protein binding metalloendopeptidase activity growth factor activity hydrolase activity metallopeptidase activity serine type endopeptidase activity cytokine activity identical protein bindingCellular componentGolgi apparatus extracellular region vesicle extracellular spaceBiological processskeletal system development cell differentiation ossification extracellular matrix disassembly proteolysis multicellular organism development cartilage development positive regulation of cartilage development cartilage condensation high density lipoprotein particle assembly regulation of signaling receptor activity signal transductionSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez64912153EnsemblENSG00000168487ENSMUSG00000022098UniProtP13497P98063RefSeq mRNA NM 001199NM 006128NM 006129NM 006130NM 006131NM 006132NM 009755NM 001360021RefSeq protein NP 001190NP 006120NP 033885NP 001346950Location UCSC Chr 8 22 17 22 21 MbChr 14 70 47 70 52 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Function 2 Structure 3 References 4 Further reading 5 External linksFunction editBMP1 belongs to the peptidase M12A family of bone morphogenetic proteins BMPs It induces bone and cartilage development Unlike other BMPs it does not belong to the TGFb superfamily It was initially discovered to work like other BMPs by inducing bone and cartilage development It however is a metalloprotease that cleaves the C terminus of procollagen I II and III It has an astacin like protease domain It has been shown to cleave laminin 5 and is localized in the basal epithelial layer of bovine skin The BMP1 locus encodes a protein that is capable of inducing formation of cartilage in vivo Although other bone morphogenetic proteins are members of the TGF beta superfamily BMP1 encodes a protein that is not closely related to other known growth factors BMP1 protein and procollagen C proteinase PCP a secreted metalloprotease requiring calcium and needed for cartilage and bone formation are identical PCP or BMP1 protein cleaves the C terminal propeptides of procollagen I II and III and its activity is increased by the procollagen C endopeptidase enhancer protein The BMP1 gene is expressed as alternatively spliced variants that share an N terminal protease domain but differ in their C terminal region 5 Structure editA partial structure of BMP1 was determined through X Ray diffraction with a resolution of 1 27 A 7 Crystallization experiments were done by vapor diffusion at a pH of 7 5 This is important because it is close to the pH of the human body where BMP1 resides in vivo This BMP1 fragment is 202 residues in length Its secondary structure is made up of 30 helices or 10 helices 61 residues in length and 15 beta sheets or 11 strands 32 residues in length It contains ligands of an acetyl group and a Zinc ion A Ramachandran plot was constructed for BMP1 8 This plot shows that BMP1 most prefers Phi and Psi angles Phi Psi of around 60 45 and 60 140 These preferred angles are an estimate of the most clustered data of the Ramachandran plot The preferred region is much greater in range 97 of the residues were in preferred regions and 100 of the residues were in the allowed region with no outliers References edit a b c GRCh38 Ensembl release 89 ENSG00000168487 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000022098 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine a b Entrez Gene BMP1 bone morphogenetic protein 1 Tabas JA Zasloff M Wasmuth JJ Emanuel BS Altherr MR McPherson JD Wozney JM Kaplan FS February 1991 Bone morphogenetic protein chromosomal localization of human genes for BMP1 BMP2A and BMP3 Genomics 9 2 283 9 doi 10 1016 0888 7543 91 90254 C PMID 2004778 PDB 3EDG Mac Sweeney A Gil Parrado S Vinzenz D Bernardi A Hein A Bodendorf U Erbel P Logel C Gerhartz B December 2008 Structural basis for the substrate specificity of bone morphogenetic protein 1 tolloid like metalloproteases J Mol Biol 384 1 228 39 doi 10 1016 j jmb 2008 09 029 PMID 18824173 MolProbity Ramachandran analysis of 3EDG model 1 PDF www rcsb org Archived from the original PDF on 2012 10 12 Further reading editTabas JA Zasloff M Wasmuth JJ et al 1991 Bone morphogenetic protein chromosomal localization of human genes for BMP1 BMP2A and BMP3 Genomics 9 2 283 9 doi 10 1016 0888 7543 91 90254 C PMID 2004778 Wozney JM Rosen V Celeste AJ et al 1989 Novel regulators of bone formation molecular clones and activities Science 242 4885 1528 34 doi 10 1126 science 3201241 PMID 3201241 Takahara K Lyons GE Greenspan DS 1995 Bone morphogenetic protein 1 and a mammalian tolloid homologue mTld are encoded by alternatively spliced transcripts which are differentially expressed in some tissues J Biol Chem 269 51 32572 8 doi 10 1016 S0021 9258 18 31672 7 PMID 7798260 Yoshiura K Tamura T Hong HS et al 1993 Mapping of the bone morphogenetic protein 1 gene BMP1 to 8p21 removal of BMP1 from candidacy for the bone disorder in Langer Giedion syndrome Cytogenet Cell Genet 64 3 4 208 9 doi 10 1159 000133577 PMID 8404039 Takahara K Lee S Wood S Greenspan DS 1996 Structural organization and genetic localization of the human bone morphogenetic protein 1 mammalian tolloid gene Genomics 29 1 9 15 doi 10 1006 geno 1995 1209 PMID 8530106 Kessler E Takahara K Biniaminov L et al 1996 Bone morphogenetic protein 1 the type I procollagen C proteinase Science 271 5247 360 2 Bibcode 1996Sci 271 360K doi 10 1126 science 271 5247 360 PMID 8553073 S2CID 26378870 Li SW Sieron AL Fertala A et al 1996 The C proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein 1 Proc Natl Acad Sci U S A 93 10 5127 30 Bibcode 1996PNAS 93 5127L doi 10 1073 pnas 93 10 5127 PMC 39418 PMID 8643539 Janitz M Heiser V Bottcher U et al 1998 Three alternatively spliced variants of the gene coding for the human bone morphogenetic protein 1 J Mol Med 76 2 141 6 doi 10 1007 s001090050202 PMID 9500680 S2CID 26374071 Scott IC Blitz IL Pappano WN et al 1999 Mammalian BMP 1 Tolloid related metalloproteinases including novel family member mammalian Tolloid like 2 have differential enzymatic activities and distributions of expression relevant to patterning and skeletogenesis Dev Biol 213 2 283 300 doi 10 1006 dbio 1999 9383 PMID 10479448 Amano S Scott IC Takahara K et al 2000 Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 gamma 2 chain J Biol Chem 275 30 22728 35 doi 10 1074 jbc M002345200 PMID 10806203 Scott IC Blitz IL Pappano WN et al 2001 Homologues of Twisted gastrulation are extracellular cofactors in antagonism of BMP signalling Nature 410 6827 475 8 Bibcode 2001Natur 410 475S doi 10 1038 35068572 PMID 11260715 S2CID 4392365 Garrigue Antar L Barker C Kadler KE 2001 Identification of amino acid residues in bone morphogenetic protein 1 important for procollagen C proteinase activity J Biol Chem 276 28 26237 42 doi 10 1074 jbc M010814200 PMID 11283002 Unsold C Pappano WN Imamura Y et al 2002 Biosynthetic processing of the pro alpha 1 V 2pro alpha 2 V collagen heterotrimer by bone morphogenetic protein 1 and furin like proprotein convertases J Biol Chem 277 7 5596 602 doi 10 1074 jbc M110003200 PMID 11741999 Rattenholl A Pappano WN Koch M et al 2002 Proteinases of the bone morphogenetic protein 1 family convert procollagen VII to mature anchoring fibril collagen J Biol Chem 277 29 26372 8 doi 10 1074 jbc M203247200 PMID 11986329 Garrigue Antar L Hartigan N Kadler KE 2003 Post translational modification of bone morphogenetic protein 1 is required for secretion and stability of the protein J Biol Chem 277 45 43327 34 doi 10 1074 jbc M207342200 PMID 12218058 Strausberg RL Feingold EA Grouse LH et al 2003 Generation and initial analysis of more than 15 000 full length human and mouse cDNA sequences Proc Natl Acad Sci U S A 99 26 16899 903 Bibcode 2002PNAS 9916899M doi 10 1073 pnas 242603899 PMC 139241 PMID 12477932 Hartigan N Garrigue Antar L Kadler KE 2003 Bone morphogenetic protein 1 BMP 1 Identification of the minimal domain structure for procollagen C proteinase activity J Biol Chem 278 20 18045 9 doi 10 1074 jbc M211448200 PMID 12637537 Leighton M Kadler KE 2003 Paired basic Furin like proprotein convertase cleavage of Pro BMP 1 in the trans Golgi network J Biol Chem 278 20 18478 84 doi 10 1074 jbc M213021200 PMID 12637569 Ota T Suzuki Y Nishikawa T et al 2004 Complete sequencing and characterization of 21 243 full length human cDNAs Nat Genet 36 1 40 5 doi 10 1038 ng1285 PMID 14702039 Hillman RT Green RE Brenner SE 2005 An unappreciated role for RNA surveillance Genome Biol 5 2 R8 doi 10 1186 gb 2004 5 2 r8 PMC 395752 PMID 14759258 External links editbone morphogenetic protein 1 at the U S National Library of Medicine Medical Subject Headings MeSH Human BMP1 genome location and BMP1 gene details page in the UCSC Genome Browser Human PCP2 genome location and PCP2 gene details page in the UCSC Genome Browser The MEROPS online database for peptidases and their inhibitors M12 005 permanent dead link Retrieved from https en wikipedia org w index php title Bone morphogenetic protein 1 amp oldid 1212885298, wikipedia, wiki, book, books, library,
