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Bone morphogenetic protein 1 (BMP-1) (EC 3 4 24 19) (Mammalian tolloid protein) (mTld) (Procollagen C-proteinase) (PCP)

 BMP1_HUMAN              Reviewed;         986 AA.
P13497; A8K6F5; B2RN46; D3DSR0; Q13292; Q13872; Q14874; Q99421;
Q99422; Q99423; Q9UL38;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
21-FEB-2001, sequence version 2.
07-NOV-2018, entry version 211.
RecName: Full=Bone morphogenetic protein 1;
Short=BMP-1;
EC=3.4.24.19;
AltName: Full=Mammalian tolloid protein;
Short=mTld;
AltName: Full=Procollagen C-proteinase;
Short=PCP;
Flags: Precursor;
Name=BMP1; Synonyms=PCOLC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BMP1-3).
TISSUE=Skin;
PubMed=8643539; DOI=10.1073/pnas.93.10.5127;
Li S.W., Sieron A.L., Fertala A., Hojima Y., Arnold W.V.,
Prockop D.J.;
"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. 93:5127-5130(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BMP1-1).
PubMed=3201241; DOI=10.1126/science.3201241;
Wozney J.M., Rosen V., Celeste A.J., Mitsock L.M., Whitters M.J.,
Kriz R.W., Hewick R.M., Wang E.A.;
"Novel regulators of bone formation: molecular clones and
activities.";
Science 242:1528-1534(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BMP1-4; BMP1-5 AND BMP1-6).
TISSUE=Placenta;
PubMed=9500680; DOI=10.1007/s001090050202;
Janitz M., Heiser V., Boettcher U., Landt O., Lauster R.;
"Three alternatively spliced variants of the gene coding for the human
bone morphogenetic protein-1.";
J. Mol. Med. 76:141-146(1998).
[4]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BMP1-3 AND BMP1-7).
TISSUE=Placenta;
PubMed=7798260;
Takahara K., Lyons G.E., Greenspan D.S.;
"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. 269:32572-32578(1994).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BMP1-5).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BMP1-3).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
DISULFIDE BOND AT 183-CYS--CYS-186.
PubMed=11283002; DOI=10.1074/jbc.M010814200;
Garrigue-Antar L., Barker C., Kadler K.E.;
"Identification of amino acid residues in bone morphogenetic protein-1
important for procollagen C-proteinase activity.";
J. Biol. Chem. 276:26237-26242(2001).
[9]
SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF
119-ARG--ARG-120.
PubMed=12637569; DOI=10.1074/jbc.M213021200;
Leighton M., Kadler K.E.;
"Paired basic/Furin-like proprotein convertase cleavage of Pro-BMP-1
in the trans-Golgi network.";
J. Biol. Chem. 278:18478-18484(2003).
[10]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[11]
X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 121-321 IN COMPLEX WITH ZINC
IONS, ZINC-BINDING SITES, COFACTOR, ACTIVE SITE, AND DISULFIDE BONDS.
PubMed=18824173; DOI=10.1016/j.jmb.2008.09.029;
Mac Sweeney A., Gil-Parrado S., Vinzenz D., Bernardi A., Hein A.,
Bodendorf U., Erbel P., Logel C., Gerhartz B.;
"Structural basis for the substrate specificity of bone morphogenetic
protein 1/tolloid-like metalloproteases.";
J. Mol. Biol. 384:228-239(2008).
[12]
VARIANT [LARGE SCALE ANALYSIS] HIS-45.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[13]
VARIANT OI13 ARG-12, CHARACTERIZATION OF VARIANT OI13 ARG-12, AND
INVOLVEMENT IN OI13.
PubMed=22482805; DOI=10.1016/j.ajhg.2012.02.026;
Asharani P.V., Keupp K., Semler O., Wang W., Li Y., Thiele H.,
Yigit G., Pohl E., Becker J., Frommolt P., Sonntag C., Altmuller J.,
Zimmermann K., Greenspan D.S., Akarsu N.A., Netzer C., Schonau E.,
Wirth R., Hammerschmidt M., Nurnberg P., Wollnik B., Carney T.J.;
"Attenuated BMP1 function compromises osteogenesis, leading to bone
fragility in humans and zebrafish.";
Am. J. Hum. Genet. 90:661-674(2012).
[14]
VARIANT OI13 LEU-249, AND CHARACTERIZATION OF VARIANT OI13 LEU-249.
PubMed=22052668; DOI=10.1002/humu.21647;
Martinez-Glez V., Valencia M., Caparros-Martin J.A., Aglan M.,
Temtamy S., Tenorio J., Pulido V., Lindert U., Rohrbach M., Eyre D.,
Giunta C., Lapunzina P., Ruiz-Perez V.L.;
"Identification of a mutation causing deficient BMP1/mTLD proteolytic
activity in autosomal recessive osteogenesis imperfecta.";
Hum. Mutat. 33:343-350(2012).
[15]
VARIANT OI13 VAL-270, AND CHARACTERIZATION OF VARIANT OI13 VAL-270.
PubMed=25402547; DOI=10.1002/humu.22731;
Cho S.Y., Asharani P.V., Kim O.H., Iida A., Miyake N., Matsumoto N.,
Nishimura G., Ki C.S., Hong G., Kim S.J., Sohn Y.B., Park S.W.,
Lee J., Kwun Y., Carney T.J., Huh R., Ikegawa S., Jin D.K.;
"Identification and in vivo functional characterization of novel
compound heterozygous BMP1 variants in osteogenesis imperfecta.";
Hum. Mutat. 36:191-195(2015).
-!- FUNCTION: Cleaves the C-terminal propeptides of procollagen I, II
and III. Induces cartilage and bone formation. May participate in
dorsoventral patterning during early development by cleaving
chordin (CHRD). Responsible for the proteolytic activation of
lysyl oxidase LOX.
-!- CATALYTIC ACTIVITY: Cleavage of the C-terminal propeptide at
Ala-|-Asp in type I and II procollagens and at Arg-|-Asp in type
III.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|PROSITE-ProRule:PRU01211,
ECO:0000269|PubMed:18824173};
Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
ProRule:PRU01211, ECO:0000269|PubMed:18824173};
-!- ACTIVITY REGULATION: Activity is increased by the procollagen C-
endopeptidase enhancer protein.
-!- SUBUNIT: Interacts with POSTN, the interaction promotes deposition
on the extracellular matrix. {ECO:0000250}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-489827, EBI-489827;
Q9H2X0:CHRD; NbExp=2; IntAct=EBI-489827, EBI-947551;
P20908:COL5A1; NbExp=2; IntAct=EBI-489827, EBI-2464511;
P07585:DCN; NbExp=2; IntAct=EBI-12509497, EBI-9663608;
O14793:MSTN; NbExp=2; IntAct=EBI-489827, EBI-8542977;
Q15113:PCOLCE; NbExp=3; IntAct=EBI-489827, EBI-8869614;
P97299:Sfrp2 (xeno); NbExp=2; IntAct=EBI-12509497, EBI-15892646;
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
{ECO:0000269|PubMed:12637569}. Secreted, extracellular space,
extracellular matrix {ECO:0000269|PubMed:12637569}. Note=Co-
localizes with POSTN in the Golgi. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=BMP1-3;
IsoId=P13497-1; Sequence=Displayed;
Name=BMP1-1;
IsoId=P13497-2; Sequence=VSP_005461, VSP_005462;
Name=BMP1-2;
IsoId=P13497-7; Sequence=Not described;
Name=BMP1-4;
IsoId=P13497-3; Sequence=VSP_005463, VSP_005464;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=BMP1-5;
IsoId=P13497-4; Sequence=VSP_005465, VSP_005466;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=BMP1-6;
IsoId=P13497-5; Sequence=VSP_005467, VSP_005468;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=BMP1-7;
IsoId=P13497-6; Sequence=VSP_005469, VSP_005470;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- 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}.
-!- DISEASE: Osteogenesis imperfecta 13 (OI13) [MIM:614856]: An
autosomal recessive form of osteogenesis imperfecta, a connective
tissue disorder characterized by low bone mass, bone fragility and
susceptibility to fractures after minimal trauma. Disease severity
ranges from very mild forms without fractures to intrauterine
fractures and perinatal lethality. Extraskeletal manifestations,
which affect a variable number of patients, are dentinogenesis
imperfecta, hearing loss, and blue sclerae. OI13 is characterized
by normal teeth, faint blue sclerae, severe growth deficiency,
borderline osteoporosis, severe bone deformity, and recurrent
fractures affecting both upper and lower limbs.
{ECO:0000269|PubMed:22052668, ECO:0000269|PubMed:22482805,
ECO:0000269|PubMed:25402547}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
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EMBL; U50330; AAA93462.1; -; mRNA.
EMBL; M22488; AAA51833.1; -; mRNA.
EMBL; Y08723; CAA69973.1; -; mRNA.
EMBL; Y08724; CAA69974.1; -; mRNA.
EMBL; Y08725; CAA69975.1; -; mRNA.
EMBL; L35278; AAC41703.1; -; mRNA.
EMBL; L35279; AAC41710.1; -; mRNA.
EMBL; AK291620; BAF84309.1; -; mRNA.
EMBL; CH471080; EAW63698.1; -; Genomic_DNA.
EMBL; CH471080; EAW63703.1; -; Genomic_DNA.
EMBL; CH471080; EAW63704.1; -; Genomic_DNA.
EMBL; BC136679; AAI36680.1; -; mRNA.
CCDS; CCDS34856.1; -. [P13497-2]
CCDS; CCDS6026.1; -. [P13497-1]
PIR; A37278; BMHU1.
PIR; A58788; A58788.
PIR; B58788; B58788.
RefSeq; NP_001190.1; NM_001199.3. [P13497-2]
RefSeq; NP_006120.1; NM_006129.4. [P13497-1]
RefSeq; XP_011542919.1; XM_011544617.1. [P13497-4]
RefSeq; XP_016869227.1; XM_017013738.1. [P13497-5]
UniGene; Hs.1274; -.
PDB; 3EDG; X-ray; 1.27 A; A=121-321.
PDB; 3EDH; X-ray; 1.25 A; A=121-321.
PDB; 6BSL; X-ray; 1.45 A; A/B=121-321.
PDB; 6BSM; X-ray; 2.33 A; A=121-320.
PDB; 6BTN; X-ray; 2.05 A; A/B=121-321.
PDB; 6BTO; X-ray; 2.05 A; A/B=121-321.
PDB; 6BTP; X-ray; 1.93 A; A/B=121-320.
PDB; 6BTQ; X-ray; 1.75 A; A/B=121-321.
PDBsum; 3EDG; -.
PDBsum; 3EDH; -.
PDBsum; 6BSL; -.
PDBsum; 6BSM; -.
PDBsum; 6BTN; -.
PDBsum; 6BTO; -.
PDBsum; 6BTP; -.
PDBsum; 6BTQ; -.
ProteinModelPortal; P13497; -.
SMR; P13497; -.
BioGrid; 107117; 45.
DIP; DIP-33403N; -.
ELM; P13497; -.
IntAct; P13497; 14.
MINT; P13497; -.
STRING; 9606.ENSP00000305714; -.
BindingDB; P13497; -.
ChEMBL; CHEMBL3898; -.
GuidetoPHARMACOLOGY; 2333; -.
MEROPS; M12.005; -.
GlyConnect; 1045; -.
iPTMnet; P13497; -.
PhosphoSitePlus; P13497; -.
BioMuta; BMP1; -.
DMDM; 13124688; -.
EPD; P13497; -.
PaxDb; P13497; -.
PeptideAtlas; P13497; -.
PRIDE; P13497; -.
ProteomicsDB; 52914; -.
ProteomicsDB; 52915; -. [P13497-2]
ProteomicsDB; 52916; -. [P13497-3]
ProteomicsDB; 52917; -. [P13497-4]
ProteomicsDB; 52918; -. [P13497-5]
ProteomicsDB; 52919; -. [P13497-6]
Ensembl; ENST00000306349; ENSP00000306121; ENSG00000168487. [P13497-2]
Ensembl; ENST00000306385; ENSP00000305714; ENSG00000168487. [P13497-1]
Ensembl; ENST00000471755; ENSP00000428665; ENSG00000168487. [P13497-4]
Ensembl; ENST00000520970; ENSP00000428332; ENSG00000168487. [P13497-2]
Ensembl; ENST00000521385; ENSP00000430406; ENSG00000168487. [P13497-5]
GeneID; 649; -.
KEGG; hsa:649; -.
UCSC; uc003xbb.4; human. [P13497-1]
CTD; 649; -.
DisGeNET; 649; -.
EuPathDB; HostDB:ENSG00000168487.17; -.
GeneCards; BMP1; -.
HGNC; HGNC:1067; BMP1.
HPA; HPA014572; -.
MalaCards; BMP1; -.
MIM; 112264; gene.
MIM; 614856; phenotype.
neXtProt; NX_P13497; -.
OpenTargets; ENSG00000168487; -.
Orphanet; 314029; High bone mass osteogenesis imperfecta.
Orphanet; 216812; Osteogenesis imperfecta type 3.
PharmGKB; PA25377; -.
eggNOG; KOG3714; Eukaryota.
eggNOG; ENOG410ZPX7; LUCA.
GeneTree; ENSGT00760000119018; -.
HOVERGEN; HBG004859; -.
InParanoid; P13497; -.
KO; K05502; -.
OMA; KGFEASH; -.
OrthoDB; EOG091G009U; -.
PhylomeDB; P13497; -.
TreeFam; TF314351; -.
BRENDA; 3.4.24.19; 2681.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
Reactome; R-HSA-2214320; Anchoring fibril formation.
Reactome; R-HSA-2243919; Crosslinking of collagen fibrils.
Reactome; R-HSA-8963896; HDL assembly.
ChiTaRS; BMP1; human.
EvolutionaryTrace; P13497; -.
GeneWiki; Bone_morphogenetic_protein_1; -.
GenomeRNAi; 649; -.
PMAP-CutDB; P13497; -.
PRO; PR:P13497; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000168487; Expressed in 197 organ(s), highest expression level in placenta.
CleanEx; HS_BMP1; -.
ExpressionAtlas; P13497; baseline and differential.
Genevisible; P13497; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0031982; C:vesicle; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004222; F:metalloendopeptidase activity; TAS:Reactome.
GO; GO:0008237; F:metallopeptidase activity; NAS:UniProtKB.
GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0001502; P:cartilage condensation; TAS:ProtInc.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0034380; P:high-density lipoprotein particle assembly; TAS:Reactome.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
GO; GO:0061036; P:positive regulation of cartilage development; IDA:MGI.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
CDD; cd00041; CUB; 5.
CDD; cd04281; ZnMc_BMP1_TLD; 1.
Gene3D; 2.60.120.290; -; 5.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR015446; BMP_1/tolloid-like.
InterPro; IPR000859; CUB_dom.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001506; Peptidase_M12A.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR035914; Sperma_CUB_dom_sf.
InterPro; IPR034036; ZnMP_TLD/BMP1.
Pfam; PF01400; Astacin; 1.
Pfam; PF00431; CUB; 5.
Pfam; PF07645; EGF_CA; 1.
PIRSF; PIRSF001199; BMP_1/tolloid-like; 1.
PRINTS; PR00480; ASTACIN.
SMART; SM00042; CUB; 5.
SMART; SM00181; EGF; 2.
SMART; SM00179; EGF_CA; 2.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF49854; SSF49854; 5.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS51864; ASTACIN; 1.
PROSITE; PS00010; ASX_HYDROXYL; 2.
PROSITE; PS01180; CUB; 5.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS50026; EGF_3; 2.
PROSITE; PS01187; EGF_CA; 2.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Chondrogenesis;
Cleavage on pair of basic residues; Complete proteome; Cytokine;
Developmental protein; Differentiation; Disease mutation;
Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
Golgi apparatus; Growth factor; Hydrolase; Metal-binding;
Metalloprotease; Methylation; Osteogenesis; Osteogenesis imperfecta;
Polymorphism; Protease; Reference proteome; Repeat; Secreted; Signal;
Zinc; Zymogen.
SIGNAL 1 22 {ECO:0000255}.
PROPEP 23 120 {ECO:0000269|PubMed:12637569}.
/FTId=PRO_0000028889.
CHAIN 121 986 Bone morphogenetic protein 1.
/FTId=PRO_0000028890.
DOMAIN 121 320 Peptidase M12A. {ECO:0000255|PROSITE-
ProRule:PRU01211}.
DOMAIN 322 434 CUB 1. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 435 546 CUB 2. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 547 588 EGF-like 1; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 591 703 CUB 3. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 704 743 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 747 859 CUB 4. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 860 976 CUB 5. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
ACT_SITE 214 214 {ECO:0000255|PROSITE-ProRule:PRU01211,
ECO:0000269|PubMed:18824173}.
METAL 213 213 Zinc; via tele nitrogen; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU01211,
ECO:0000269|PubMed:18824173}.
METAL 217 217 Zinc; via tele nitrogen; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU01211,
ECO:0000269|PubMed:18824173}.
METAL 223 223 Zinc; via tele nitrogen; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU01211,
ECO:0000269|PubMed:18824173}.
MOD_RES 934 934 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9WVM6}.
MOD_RES 937 937 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9WVM6}.
CARBOHYD 91 91 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 142 142 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 332 332 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 363 363 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 599 599 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 163 319 {ECO:0000255|PROSITE-ProRule:PRU01211,
ECO:0000269|PubMed:18824173}.
DISULFID 183 205 {ECO:0000255|PROSITE-ProRule:PRU01211,
ECO:0000269|PubMed:18824173}.
DISULFID 185 186 {ECO:0000255|PROSITE-ProRule:PRU01211,
ECO:0000269|PubMed:18824173}.
DISULFID 322 348 {ECO:0000250}.
DISULFID 375 397 {ECO:0000250}.
DISULFID 435 461 {ECO:0000250}.
DISULFID 488 510 {ECO:0000250}.
DISULFID 551 563 {ECO:0000250}.
DISULFID 559 572 {ECO:0000250}.
DISULFID 574 587 {ECO:0000250}.
DISULFID 591 617 {ECO:0000250}.
DISULFID 644 666 {ECO:0000250}.
DISULFID 707 718 {ECO:0000250}.
DISULFID 714 727 {ECO:0000250}.
DISULFID 729 742 {ECO:0000250}.
DISULFID 747 773 {ECO:0000250}.
DISULFID 800 822 {ECO:0000250}.
DISULFID 860 890 {ECO:0000250}.
DISULFID 917 939 {ECO:0000250}.
VAR_SEQ 245 302 QEYNFLKMEPQEVESLGETYDFDSIMHYARNTFSRGIFLDT
IVPKYEVNGVKPPIGQR -> VLHSSLLLLSCGSRNGASFP
CSLESSTHQALCWTGLFLRPSPFPRLPLAAPRTLRAGV
(in isoform BMP1-4).
{ECO:0000303|PubMed:9500680}.
/FTId=VSP_005463.
VAR_SEQ 303 986 Missing (in isoform BMP1-4).
{ECO:0000303|PubMed:9500680}.
/FTId=VSP_005464.
VAR_SEQ 589 622 AACGGFLTKLNGSITSPGWPKEYPPNKNCIWQLV -> GCY
DLQVGKPLLWDRHCFRLSTHGPEMLGTALRG (in
isoform BMP1-5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:9500680}.
/FTId=VSP_005465.
VAR_SEQ 623 986 Missing (in isoform BMP1-5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:9500680}.
/FTId=VSP_005466.
VAR_SEQ 703 823 DKDECSKDNGGCQQDCVNTFGSYECQCRSGFVLHDNKHDCK
EAGCDHKVTSTSGTITSPNWPDKYPSKKECTWAISSTPGHR
VKLTFMEMDIESQPECAYDHLEVFDGRDAKAPVLGRFCG
-> VLEGAGDRHSHLSGLELLLCPHALVDTVPAPPSALHGD
THAHTHTHVHTHCPIAQETCRGPPLGASRLSPQGPGHLTLA
PQEGSYLDFWDTHRGDPKPRRRRKSLKTFSLTPATFRGIWA
L (in isoform BMP1-7). {ECO:0000305}.
/FTId=VSP_005469.
VAR_SEQ 703 730 DKDECSKDNGGCQQDCVNTFGSYECQCR -> EKRPALQPP
RGRPHQLKFRVQKRNRTPQ (in isoform BMP1-1).
{ECO:0000303|PubMed:3201241}.
/FTId=VSP_005461.
VAR_SEQ 703 717 DKDECSKDNGGCQQD -> GGELFGLLGHPPRRP (in
isoform BMP1-6).
{ECO:0000303|PubMed:9500680}.
/FTId=VSP_005467.
VAR_SEQ 718 986 Missing (in isoform BMP1-6).
{ECO:0000303|PubMed:9500680}.
/FTId=VSP_005468.
VAR_SEQ 731 986 Missing (in isoform BMP1-1).
{ECO:0000303|PubMed:3201241}.
/FTId=VSP_005462.
VAR_SEQ 824 986 Missing (in isoform BMP1-7).
{ECO:0000305}.
/FTId=VSP_005470.
VARIANT 12 12 G -> R (in OI13; the mutation leads to
severely reduced post-translational N-
glycosylation of the protein and impairs
protein secretion; leads to both reduced
secretion and subsequent reduced
processing of the substrates CHRD and
COL1A1; dbSNP:rs318240762).
{ECO:0000269|PubMed:22482805}.
/FTId=VAR_069096.
VARIANT 45 45 D -> H (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036141.
VARIANT 249 249 F -> L (in OI13; leads to a protein with
deficient procollagen I C-terminal
propeptide proteolytic activity;
dbSNP:rs398122891).
{ECO:0000269|PubMed:22052668}.
/FTId=VAR_067224.
VARIANT 270 270 M -> V (in OI13; partial loss of
activity; dbSNP:rs786205219).
{ECO:0000269|PubMed:25402547}.
/FTId=VAR_072248.
VARIANT 719 719 V -> I (in dbSNP:rs11996036).
/FTId=VAR_051584.
MUTAGEN 119 120 RR->AA: Doesn't abolish secretion.
{ECO:0000269|PubMed:12637569}.
CONFLICT 748 748 D -> N (in Ref. 4; AAC41710).
{ECO:0000305}.
CONFLICT 934 934 R -> S (in Ref. 4; AAC41710).
{ECO:0000305}.
STRAND 122 124 {ECO:0000244|PDB:6BTP}.
HELIX 126 128 {ECO:0000244|PDB:3EDH}.
HELIX 131 133 {ECO:0000244|PDB:3EDH}.
STRAND 134 139 {ECO:0000244|PDB:3EDH}.
HELIX 145 161 {ECO:0000244|PDB:3EDH}.
STRAND 165 168 {ECO:0000244|PDB:3EDH}.
STRAND 173 180 {ECO:0000244|PDB:3EDH}.
STRAND 183 185 {ECO:0000244|PDB:6BSL}.
STRAND 194 201 {ECO:0000244|PDB:3EDH}.
HELIX 203 205 {ECO:0000244|PDB:3EDH}.
HELIX 208 219 {ECO:0000244|PDB:3EDH}.
HELIX 224 226 {ECO:0000244|PDB:3EDH}.
HELIX 230 232 {ECO:0000244|PDB:3EDH}.
STRAND 234 236 {ECO:0000244|PDB:3EDH}.
HELIX 238 240 {ECO:0000244|PDB:3EDH}.
HELIX 246 249 {ECO:0000244|PDB:3EDH}.
HELIX 254 256 {ECO:0000244|PDB:3EDH}.
TURN 274 277 {ECO:0000244|PDB:3EDH}.
STRAND 278 280 {ECO:0000244|PDB:3EDH}.
STRAND 285 290 {ECO:0000244|PDB:3EDH}.
HELIX 307 316 {ECO:0000244|PDB:3EDH}.
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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