GenomeNet

Database: UniProt
Entry: P98063
LinkDB: P98063
Original site: P98063 
ID   BMP1_MOUSE              Reviewed;         991 AA.
AC   P98063; Q6NZM2;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   13-FEB-2019, entry version 166.
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;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=8174772; DOI=10.1006/dbio.1994.1133;
RA   Fukagawa M., Noboru S., Hogan B.L.M., Jones C.M.;
RT   "Embryonic expression of mouse bone morphogenetic protein-1 (BMP-1),
RT   which is related to the Drosophila dorsoventral gene tolloid and
RT   encodes a putative astacin metalloendopeptidase.";
RL   Dev. Biol. 163:175-183(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; 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   [4]
RP   FUNCTION, INTERACTION WITH POSTN, AND SUBCELLULAR LOCATION.
RX   PubMed=20181949; DOI=10.1074/jbc.M109.088864;
RA   Maruhashi T., Kii I., Saito M., Kudo A.;
RT   "Interaction between periostin and BMP-1 promotes proteolytic
RT   activation of lysyl oxidase.";
RL   J. Biol. Chem. 285:13294-13303(2010).
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) (By similarity). Responsible for the proteolytic
CC       activation of lysyl oxidase LOX. {ECO:0000250,
CC       ECO:0000269|PubMed:20181949}.
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       Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU01211};
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:0000269|PubMed:20181949}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       {ECO:0000269|PubMed:20181949}. Secreted, extracellular space,
CC       extracellular matrix {ECO:0000269|PubMed:20181949}. Note=Co-
CC       localizes with POSTN in the Golgi.
CC   -!- TISSUE SPECIFICITY: At high levels in embryonic maternal deciduum
CC       and floor plate region of the neural tube. Less in developing
CC       membranous and endochondral bone, submucosa of intestine, dermis
CC       of skin and the mesenchyme of spleen and lung.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA37306.1; Type=Frameshift; Positions=24, 61; Evidence={ECO:0000305};
DR   EMBL; L24755; AAA37306.1; ALT_FRAME; mRNA.
DR   EMBL; AC122268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC066062; AAH66062.1; -; mRNA.
DR   CCDS; CCDS36972.1; -.
DR   PIR; I49540; I49540.
DR   RefSeq; NP_033885.2; NM_009755.3.
DR   RefSeq; XP_006518523.1; XM_006518460.3.
DR   UniGene; Mm.27757; -.
DR   ProteinModelPortal; P98063; -.
DR   SMR; P98063; -.
DR   BioGrid; 198360; 3.
DR   IntAct; P98063; 2.
DR   STRING; 10090.ENSMUSP00000022693; -.
DR   MEROPS; M12.005; -.
DR   iPTMnet; P98063; -.
DR   PhosphoSitePlus; P98063; -.
DR   PaxDb; P98063; -.
DR   PeptideAtlas; P98063; -.
DR   PRIDE; P98063; -.
DR   Ensembl; ENSMUST00000022693; ENSMUSP00000022693; ENSMUSG00000022098.
DR   GeneID; 12153; -.
DR   KEGG; mmu:12153; -.
DR   UCSC; uc007uoc.2; mouse.
DR   CTD; 649; -.
DR   MGI; MGI:88176; Bmp1.
DR   eggNOG; KOG3714; Eukaryota.
DR   eggNOG; ENOG410ZPX7; LUCA.
DR   GeneTree; ENSGT00940000157176; -.
DR   HOGENOM; HOG000236339; -.
DR   HOVERGEN; HBG004859; -.
DR   InParanoid; P98063; -.
DR   KO; K05502; -.
DR   OMA; KGFEASH; -.
DR   OrthoDB; 170905at2759; -.
DR   TreeFam; TF314351; -.
DR   Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-MMU-2214320; Anchoring fibril formation.
DR   Reactome; R-MMU-8963896; HDL assembly.
DR   PRO; PR:P98063; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   Bgee; ENSMUSG00000022098; Expressed in 280 organ(s), highest expression level in entire extraembryonic component.
DR   ExpressionAtlas; P98063; baseline and differential.
DR   Genevisible; P98063; MM.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031982; C:vesicle; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IDA:MGI.
DR   GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR   GO; GO:0061036; P:positive regulation of cartilage development; ISO:MGI.
DR   GO; GO:0006508; P:proteolysis; ISO:MGI.
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; 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   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   Calcium; Chondrogenesis; Cleavage on pair of basic residues;
KW   Complete proteome; Cytokine; Developmental protein; Differentiation;
KW   Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW   Golgi apparatus; Growth factor; Hydrolase; Metal-binding;
KW   Metalloprotease; Methylation; Osteogenesis; Protease;
KW   Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   PROPEP       26    125       {ECO:0000250|UniProtKB:P13497}.
FT                                /FTId=PRO_0000028891.
FT   CHAIN       126    991       Bone morphogenetic protein 1.
FT                                /FTId=PRO_0000028892.
FT   DOMAIN      126    325       Peptidase M12A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01211}.
FT   DOMAIN      327    439       CUB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      440    551       CUB 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      552    593       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      596    707       CUB 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      708    748       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      752    864       CUB 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      865    981       CUB 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   ACT_SITE    219    219       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       218    218       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       222    222       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       228    228       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   MOD_RES     939    939       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:Q9WVM6}.
FT   MOD_RES     942    942       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:Q9WVM6}.
FT   CARBOHYD     96     96       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    147    147       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    337    337       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    368    368       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    604    604       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    168    324       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    188    210       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    190    191       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    327    353       {ECO:0000250}.
FT   DISULFID    380    402       {ECO:0000250}.
FT   DISULFID    440    466       {ECO:0000250}.
FT   DISULFID    493    515       {ECO:0000250}.
FT   DISULFID    556    568       {ECO:0000250}.
FT   DISULFID    564    577       {ECO:0000250}.
FT   DISULFID    579    592       {ECO:0000250}.
FT   DISULFID    596    622       {ECO:0000250}.
FT   DISULFID    649    671       {ECO:0000250}.
FT   DISULFID    712    723       {ECO:0000250}.
FT   DISULFID    719    732       {ECO:0000250}.
FT   DISULFID    734    747       {ECO:0000250}.
FT   DISULFID    752    778       {ECO:0000250}.
FT   DISULFID    805    827       {ECO:0000250}.
FT   DISULFID    865    895       {ECO:0000250}.
FT   DISULFID    922    944       {ECO:0000250}.
FT   CONFLICT    395    397       APL -> VWV (in Ref. 1; AAA37306).
FT                                {ECO:0000305}.
FT   CONFLICT    519    519       K -> N (in Ref. 1; AAA37306).
FT                                {ECO:0000305}.
SQ   SEQUENCE   991 AA;  111666 MW;  F838441CF1DA9F1A CRC64;
     MPGVARPPLP LLSLPLLLLL LLLPRAGRPL DLADYTYDLG EEDAPELLNY KDPCKAAAFL
     GDIALDEEDL RAFQVQQAAV LRQQTARRPS IKAAGNSSAL GGQGTSGQPQ RESRGRWRGR
     PRSRRAATSR PERVWPDGVI PFVIGGNFTG SQRAVFRQAM RHWEKHTCVT FLERTDEDSY
     IVFTYRPCGC CSYVGRRGGG PQAISIGKNC DKFGIVVHEL GHVIGFWHEH TRPDRDRHVS
     IVRENIQPGQ EYNFLKMEVQ EVESLGETYD FDSIMHYARN TFSRGIFLDT IVPKYEVNGV
     KPSIGQRTRL SKGDIAQARK LYKCPACGET LQDSTGNFSS PEYPNGYSAH MHCVWRISVT
     PGEKIILNFT SMDLYRSRLC WYDYVEVRDG FWRKAPLRGR FCGGKLPEPI VSTDSRLWVE
     FRSSSNWVGK GFFAVYEAIC GGDVKKDNGH IQSPNYPDDY RPSKVCIWRI QVSEGFHVGL
     TFQSFEIERH DSCAYDYLEV RDGHSESSNL IGRYCGYEKP DDIKSTSSRL WLKFVSDGSI
     NKAGFAVNFF KEVDECSRPN RGGCEQRCLN TLGSYKCSCD PGYELAPDKR RCEAACGGFL
     TKLNGSITSP GWPKEYPPNK NCIWQLVAPT QYRISLQFDF FETEGNDVCK YDFVEVRSGL
     TADSKLHGKF CGSEKPEVIT SQYNNMRVEF KSDNTVSKKG FKAHFFSDKD ECSKDNGGCQ
     QDCVNTFGSY ECQCRSGFVL HDNKHDCKEA GCEHKVTSTS GTITSPNWPD KYPSKKECTW
     AISSTPGHRV KLTFVEMDIE SQPECAYDHL EVFDGRDAKA PVLGRFCGSK KPEPVLATGN
     RMFLRFYSDN SVQRKGFQAS HSTECGGQVR ADVKTKDLYS HAQFGDNNYP GGVDCEWVIV
     AEEGYGVELV FQTFEVEEET DCGYDYIELF DGYDSTAPRL GRYCGSGPPE EVYSAGDSVL
     VKFHSDDTIS KKGFHLRYTS TKFQDTLHSR K
//
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