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

 BMP1_MOUSE              Reviewed;         991 AA.
P98063; Q6NZM2;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
07-NOV-2018, entry version 163.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=8174772; DOI=10.1006/dbio.1994.1133;
Fukagawa M., Noboru S., Hogan B.L.M., Jones C.M.;
"Embryonic expression of mouse bone morphogenetic protein-1 (BMP-1),
which is related to the Drosophila dorsoventral gene tolloid and
encodes a putative astacin metalloendopeptidase.";
Dev. Biol. 163:175-183(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; 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).
[4]
FUNCTION, INTERACTION WITH POSTN, AND SUBCELLULAR LOCATION.
PubMed=20181949; DOI=10.1074/jbc.M109.088864;
Maruhashi T., Kii I., Saito M., Kudo A.;
"Interaction between periostin and BMP-1 promotes proteolytic
activation of lysyl oxidase.";
J. Biol. Chem. 285:13294-13303(2010).
-!- 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) (By similarity). Responsible for the proteolytic
activation of lysyl oxidase LOX. {ECO:0000250,
ECO:0000269|PubMed:20181949}.
-!- 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};
Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
ProRule:PRU01211};
-!- 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:0000269|PubMed:20181949}.
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
{ECO:0000269|PubMed:20181949}. Secreted, extracellular space,
extracellular matrix {ECO:0000269|PubMed:20181949}. Note=Co-
localizes with POSTN in the Golgi.
-!- TISSUE SPECIFICITY: At high levels in embryonic maternal deciduum
and floor plate region of the neural tube. Less in developing
membranous and endochondral bone, submucosa of intestine, dermis
of skin and the mesenchyme of spleen and lung.
-!- SEQUENCE CAUTION:
Sequence=AAA37306.1; Type=Frameshift; Positions=24, 61; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; L24755; AAA37306.1; ALT_FRAME; mRNA.
EMBL; AC122268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC066062; AAH66062.1; -; mRNA.
CCDS; CCDS36972.1; -.
PIR; I49540; I49540.
RefSeq; NP_033885.2; NM_009755.3.
RefSeq; XP_006518523.1; XM_006518460.3.
UniGene; Mm.27757; -.
ProteinModelPortal; P98063; -.
SMR; P98063; -.
BioGrid; 198360; 3.
IntAct; P98063; 2.
STRING; 10090.ENSMUSP00000022693; -.
MEROPS; M12.005; -.
iPTMnet; P98063; -.
PhosphoSitePlus; P98063; -.
PaxDb; P98063; -.
PeptideAtlas; P98063; -.
PRIDE; P98063; -.
Ensembl; ENSMUST00000022693; ENSMUSP00000022693; ENSMUSG00000022098.
GeneID; 12153; -.
KEGG; mmu:12153; -.
UCSC; uc007uoc.2; mouse.
CTD; 649; -.
MGI; MGI:88176; Bmp1.
eggNOG; KOG3714; Eukaryota.
eggNOG; ENOG410ZPX7; LUCA.
GeneTree; ENSGT00760000119018; -.
HOGENOM; HOG000236339; -.
HOVERGEN; HBG004859; -.
InParanoid; P98063; -.
KO; K05502; -.
OMA; KGFEASH; -.
OrthoDB; EOG091G009U; -.
TreeFam; TF314351; -.
Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
Reactome; R-MMU-2214320; Anchoring fibril formation.
Reactome; R-MMU-2243919; Crosslinking of collagen fibrils.
Reactome; R-MMU-8963896; HDL assembly.
PRO; PR:P98063; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000022098; Expressed in 280 organ(s), highest expression level in entire extraembryonic component.
CleanEx; MM_BMP1; -.
Genevisible; P98063; MM.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0031982; C:vesicle; ISO:MGI.
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; ISO:MGI.
GO; GO:0004222; F:metalloendopeptidase activity; IDA:MGI.
GO; GO:0008233; F:peptidase activity; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
GO; GO:0061036; P:positive regulation of cartilage development; ISO:MGI.
GO; GO:0006508; P:proteolysis; ISO:MGI.
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; 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.
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;
Calcium; Chondrogenesis; Cleavage on pair of basic residues;
Complete proteome; Cytokine; Developmental protein; Differentiation;
Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
Golgi apparatus; Growth factor; Hydrolase; Metal-binding;
Metalloprotease; Methylation; Osteogenesis; Protease;
Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 25 {ECO:0000255}.
PROPEP 26 125 {ECO:0000250|UniProtKB:P13497}.
/FTId=PRO_0000028891.
CHAIN 126 991 Bone morphogenetic protein 1.
/FTId=PRO_0000028892.
DOMAIN 126 325 Peptidase M12A. {ECO:0000255|PROSITE-
ProRule:PRU01211}.
DOMAIN 327 439 CUB 1. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 440 551 CUB 2. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 552 593 EGF-like 1; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 596 707 CUB 3. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 708 748 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 752 864 CUB 4. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 865 981 CUB 5. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
ACT_SITE 219 219 {ECO:0000255|PROSITE-ProRule:PRU01211}.
METAL 218 218 Zinc; via tele nitrogen; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU01211}.
METAL 222 222 Zinc; via tele nitrogen; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU01211}.
METAL 228 228 Zinc; via tele nitrogen; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU01211}.
MOD_RES 939 939 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9WVM6}.
MOD_RES 942 942 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9WVM6}.
CARBOHYD 96 96 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 147 147 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 337 337 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 368 368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 604 604 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 168 324 {ECO:0000255|PROSITE-ProRule:PRU01211}.
DISULFID 188 210 {ECO:0000255|PROSITE-ProRule:PRU01211}.
DISULFID 190 191 {ECO:0000255|PROSITE-ProRule:PRU01211}.
DISULFID 327 353 {ECO:0000250}.
DISULFID 380 402 {ECO:0000250}.
DISULFID 440 466 {ECO:0000250}.
DISULFID 493 515 {ECO:0000250}.
DISULFID 556 568 {ECO:0000250}.
DISULFID 564 577 {ECO:0000250}.
DISULFID 579 592 {ECO:0000250}.
DISULFID 596 622 {ECO:0000250}.
DISULFID 649 671 {ECO:0000250}.
DISULFID 712 723 {ECO:0000250}.
DISULFID 719 732 {ECO:0000250}.
DISULFID 734 747 {ECO:0000250}.
DISULFID 752 778 {ECO:0000250}.
DISULFID 805 827 {ECO:0000250}.
DISULFID 865 895 {ECO:0000250}.
DISULFID 922 944 {ECO:0000250}.
CONFLICT 395 397 APL -> VWV (in Ref. 1; AAA37306).
{ECO:0000305}.
CONFLICT 519 519 K -> N (in Ref. 1; AAA37306).
{ECO:0000305}.
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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