GenomeNet

Database: UniProt
Entry: P13497
LinkDB: P13497
Original site: P13497 
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   13-FEB-2019, entry version 214.
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 IN COMPLEX WITH ZINC
RP   IONS, ZINC-BINDING SITES, 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:
CC       Reaction=Cleavage of the C-terminal propeptide at Ala-|-Asp in
CC         type I and II procollagens and at Arg-|-Asp in type III.;
CC         EC=3.4.24.19;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU01211,
CC         ECO:0000269|PubMed:18824173};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU01211, ECO:0000269|PubMed:18824173};
CC   -!- ACTIVITY 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       Self; NbExp=4; IntAct=EBI-489827, EBI-489827;
CC       Q9H2X0:CHRD; NbExp=2; IntAct=EBI-489827, EBI-947551;
CC       P20908:COL5A1; NbExp=2; IntAct=EBI-489827, EBI-2464511;
CC       P07585:DCN; NbExp=2; IntAct=EBI-12509497, EBI-9663608;
CC       O14793:MSTN; NbExp=2; IntAct=EBI-489827, EBI-8542977;
CC       Q15113:PCOLCE; NbExp=3; IntAct=EBI-489827, EBI-8869614;
CC       P97299:Sfrp2 (xeno); NbExp=2; IntAct=EBI-12509497, EBI-15892646;
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.
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   RefSeq; XP_016869227.1; XM_017013738.1. [P13497-5]
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   PDB; 6BSL; X-ray; 1.45 A; A/B=121-321.
DR   PDB; 6BSM; X-ray; 2.33 A; A=121-320.
DR   PDB; 6BTN; X-ray; 2.05 A; A/B=121-321.
DR   PDB; 6BTO; X-ray; 2.05 A; A/B=121-321.
DR   PDB; 6BTP; X-ray; 1.93 A; A/B=121-320.
DR   PDB; 6BTQ; X-ray; 1.75 A; A/B=121-321.
DR   PDBsum; 3EDG; -.
DR   PDBsum; 3EDH; -.
DR   PDBsum; 6BSL; -.
DR   PDBsum; 6BSM; -.
DR   PDBsum; 6BTN; -.
DR   PDBsum; 6BTO; -.
DR   PDBsum; 6BTP; -.
DR   PDBsum; 6BTQ; -.
DR   ProteinModelPortal; P13497; -.
DR   SMR; P13497; -.
DR   BioGrid; 107117; 45.
DR   DIP; DIP-33403N; -.
DR   ELM; P13497; -.
DR   IntAct; P13497; 14.
DR   MINT; P13497; -.
DR   STRING; 9606.ENSP00000305714; -.
DR   BindingDB; P13497; -.
DR   ChEMBL; CHEMBL3898; -.
DR   GuidetoPHARMACOLOGY; 2333; -.
DR   MEROPS; M12.005; -.
DR   GlyConnect; 1045; -.
DR   iPTMnet; P13497; -.
DR   PhosphoSitePlus; P13497; -.
DR   BioMuta; BMP1; -.
DR   DMDM; 13124688; -.
DR   EPD; P13497; -.
DR   jPOST; P13497; -.
DR   PaxDb; P13497; -.
DR   PeptideAtlas; P13497; -.
DR   PRIDE; P13497; -.
DR   ProteomicsDB; 52914; -.
DR   ProteomicsDB; 52915; -. [P13497-2]
DR   ProteomicsDB; 52916; -. [P13497-3]
DR   ProteomicsDB; 52917; -. [P13497-4]
DR   ProteomicsDB; 52918; -. [P13497-5]
DR   ProteomicsDB; 52919; -. [P13497-6]
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.4; human. [P13497-1]
DR   CTD; 649; -.
DR   DisGeNET; 649; -.
DR   EuPathDB; HostDB:ENSG00000168487.17; -.
DR   GeneCards; BMP1; -.
DR   HGNC; HGNC:1067; BMP1.
DR   HPA; HPA014572; -.
DR   MalaCards; BMP1; -.
DR   MIM; 112264; gene.
DR   MIM; 614856; phenotype.
DR   neXtProt; NX_P13497; -.
DR   OpenTargets; ENSG00000168487; -.
DR   Orphanet; 314029; High bone mass osteogenesis imperfecta.
DR   Orphanet; 216812; Osteogenesis imperfecta type 3.
DR   PharmGKB; PA25377; -.
DR   eggNOG; KOG3714; Eukaryota.
DR   eggNOG; ENOG410ZPX7; LUCA.
DR   GeneTree; ENSGT00940000157176; -.
DR   HOVERGEN; HBG004859; -.
DR   InParanoid; P13497; -.
DR   KO; K05502; -.
DR   OMA; KGFEASH; -.
DR   OrthoDB; 170905at2759; -.
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-2214320; Anchoring fibril formation.
DR   Reactome; R-HSA-2243919; Crosslinking of collagen fibrils.
DR   Reactome; R-HSA-8963896; HDL assembly.
DR   ChiTaRS; BMP1; human.
DR   EvolutionaryTrace; P13497; -.
DR   GeneWiki; Bone_morphogenetic_protein_1; -.
DR   GenomeRNAi; 649; -.
DR   PMAP-CutDB; P13497; -.
DR   PRO; PR:P13497; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   Bgee; ENSG00000168487; Expressed in 197 organ(s), highest expression level in placenta.
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:0031982; C:vesicle; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
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:0034380; P:high-density lipoprotein particle assembly; TAS:Reactome.
DR   GO; GO:0007275; P:multicellular organism 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; TAS:ProtInc.
DR   CDD; cd00041; CUB; 5.
DR   CDD; cd04281; ZnMc_BMP1_TLD; 1.
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_cys_sf.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR034036; ZnMP_TLD/BMP1.
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; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF49854; SSF49854; 5.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
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; Methylation; Osteogenesis; Osteogenesis imperfecta;
KW   Polymorphism; Protease; Reference proteome; Repeat; Secreted; Signal;
KW   Zinc; Zymogen.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   PROPEP       23    120       {ECO:0000269|PubMed:12637569}.
FT                                /FTId=PRO_0000028889.
FT   CHAIN       121    986       Bone morphogenetic protein 1.
FT                                /FTId=PRO_0000028890.
FT   DOMAIN      121    320       Peptidase M12A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01211}.
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   ACT_SITE    214    214       {ECO:0000255|PROSITE-ProRule:PRU01211,
FT                                ECO:0000269|PubMed:18824173}.
FT   METAL       213    213       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211,
FT                                ECO:0000269|PubMed:18824173}.
FT   METAL       217    217       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211,
FT                                ECO:0000269|PubMed:18824173}.
FT   METAL       223    223       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211,
FT                                ECO:0000269|PubMed:18824173}.
FT   MOD_RES     934    934       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:Q9WVM6}.
FT   MOD_RES     937    937       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:Q9WVM6}.
FT   CARBOHYD     91     91       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    142    142       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    332    332       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    363    363       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    599    599       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    163    319       {ECO:0000255|PROSITE-ProRule:PRU01211,
FT                                ECO:0000269|PubMed:18824173}.
FT   DISULFID    183    205       {ECO:0000255|PROSITE-ProRule:PRU01211,
FT                                ECO:0000269|PubMed:18824173}.
FT   DISULFID    185    186       {ECO:0000255|PROSITE-ProRule:PRU01211,
FT                                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                                dbSNP:rs398122891).
FT                                {ECO:0000269|PubMed:22052668}.
FT                                /FTId=VAR_067224.
FT   VARIANT     270    270       M -> V (in OI13; partial loss of
FT                                activity; dbSNP:rs786205219).
FT                                {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   STRAND      122    124       {ECO:0000244|PDB:6BTP}.
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      183    185       {ECO:0000244|PDB:6BSL}.
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
//
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