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Database: UniProt
Entry: P98070
LinkDB: P98070
Original site: P98070 
ID   BMP1_XENLA              Reviewed;         707 AA.
AC   P98070;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   18-JUL-2018, entry version 114.
DE   RecName: Full=Bone morphogenetic protein 1;
DE            Short=BMP-1;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=bmp1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Embryo;
RX   PubMed=8262384; DOI=10.1016/0378-1119(93)90103-A;
RA   Maeno M., Xue Y., Wood T.I., Ong R.C., Kung H.F.;
RT   "Cloning and expression of cDNA encoding Xenopus laevis bone
RT   morphogenetic protein-1 during early embryonic development.";
RL   Gene 134:257-261(1993).
RN   [2]
RP   FUNCTION.
RX   PubMed=10864466; DOI=10.1006/dbio.2000.9740;
RA   Blitz I.L., Shimmi O., Wuennenberg-Stapleton K., O'Connor M.B.,
RA   Cho K.W.Y.;
RT   "Is chordin a long-range- or short-range-acting factor? Roles for
RT   BMP1-related metalloproteases in chordin and BMP4 autofeedback loop
RT   regulation.";
RL   Dev. Biol. 223:120-138(2000).
RN   [3]
RP   INTERACTION WITH OLFML3.
RX   PubMed=18775317; DOI=10.1016/j.cell.2008.07.008;
RA   Inomata H., Haraguchi T., Sasai Y.;
RT   "Robust stability of the embryonic axial pattern requires a secreted
RT   scaffold for chordin degradation.";
RL   Cell 134:854-865(2008).
CC   -!- FUNCTION: Metalloprotease involved in pattern formation in
CC       gastrula and later differentiation of developing organs. Able to
CC       cleave chordin (chrd), suggesting that it may act in dorsoventral
CC       patterning during early development by regulating the chordin
CC       (chrd) activity. {ECO:0000269|PubMed:10864466,
CC       ECO:0000269|PubMed:8262384}.
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   -!- SUBUNIT: Interacts with olfml3/ont1.
CC       {ECO:0000269|PubMed:18775317}.
CC   -!- INTERACTION:
CC       B5MFE9:olfml3; NbExp=3; IntAct=EBI-1997775, EBI-1997734;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       {ECO:0000250}. Secreted, extracellular space, extracellular matrix
CC       {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Blastula, early gastrula and hatched
CC       tadpoles; little or no expression in morula and late gastrula.
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:0000250}.
DR   EMBL; L12249; AAA16313.1; -; mRNA.
DR   PIR; JC2218; JC2218.
DR   UniGene; Xl.314; -.
DR   ProteinModelPortal; P98070; -.
DR   SMR; P98070; -.
DR   IntAct; P98070; 1.
DR   MEROPS; M12.005; -.
DR   HOVERGEN; HBG004859; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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   CDD; cd00041; CUB; 3.
DR   CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR   Gene3D; 2.60.120.290; -; 3.
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; 3.
DR   PIRSF; PIRSF001199; BMP_1/tolloid-like; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00042; CUB; 3.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF49854; SSF49854; 3.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS01180; CUB; 3.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Calcium; Chondrogenesis; Cleavage on pair of basic residues; Cytokine;
KW   Developmental protein; Differentiation; Disulfide bond;
KW   EGF-like domain; Extracellular matrix; Glycoprotein; Golgi apparatus;
KW   Growth factor; Hydrolase; Metal-binding; Metalloprotease;
KW   Osteogenesis; Protease; Repeat; Secreted; Signal; Zinc.
FT   SIGNAL        1      ?       {ECO:0000255}.
FT   PROPEP        ?     83       {ECO:0000255}.
FT                                /FTId=PRO_0000028893.
FT   CHAIN        84    707       Bone morphogenetic protein 1.
FT                                /FTId=PRO_0000028894.
FT   DOMAIN       84    283       Peptidase M12A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01211}.
FT   DOMAIN      285    397       CUB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      398    509       CUB 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      510    551       EGF-like; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      554    666       CUB 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   ACT_SITE    177    177       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       176    176       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       180    180       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       186    186       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   CARBOHYD     62     62       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    105    105       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    295    295       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    326    326       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    562    562       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    126    282       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    146    168       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    148    149       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    285    311       {ECO:0000250}.
FT   DISULFID    338    360       {ECO:0000250}.
FT   DISULFID    398    424       {ECO:0000250}.
FT   DISULFID    451    473       {ECO:0000250}.
FT   DISULFID    514    526       {ECO:0000250}.
FT   DISULFID    522    535       {ECO:0000250}.
FT   DISULFID    537    550       {ECO:0000250}.
FT   DISULFID    554    580       {ECO:0000250}.
FT   DISULFID    607    629       {ECO:0000250}.
SQ   SEQUENCE   707 AA;  80674 MW;  1B6980D716DC9B8D CRC64;
     MDYSYDLEEV VEETIDYKDP CKAAAFWGDI ALDEEDLANF KIDRIVDLTK HTIHTVSGAA
     TNISRPEKGR RTRKERRRSR EKRASTSRPE RVWPDGVIPY VISGNFSGSQ RAIFRQAMRH
     WEKHTCVTFL ERTDEDSYIV FTYRPCGCCS YVGRRGGGPQ AISIGKNCDK FGIVVHELGH
     VIGFWHEHTR PDRDDHVSII RENIQPGQEY NFLKMEPEEV ESLGETYDFD SIMHYARNTF
     SRGIFLDTIL PKYDVNGVRP PIGQRTRLSS GDVAQARKLY KCPACGETLQ DSQGNFSSPG
     FPNGYSAYMH CVWRLSVTPG EKIILNFTSL DLYRSRLCWY DYIEVRDGFW KKAPLRGRFC
     GDKIPESIIS TESRLWIEFR SSSNWVGKGF QAVYEALCGG EVKKDSGHIQ SPNYPDDYRP
     NKACVWKLSV SEGFHVGISF QSFEIERHDS CAYDYLEIRD GSSETSPLVG RFCGYDKPDD
     IKSSTNQLWI KFVSDGSINK AGFSLNYFKE VDECSRPNNG GCEQRCVNTL GSYKCACDPG
     YELGQDKKSC EAACGGFLTK LNGSINSPGW PKEYPPNKNC IWQLVAPTQY RISLKFDQFE
     TEGNDVCKYD FVEVRSGLTS DSKLHGKFCG SELPAVITSQ YNNMRIEFKS DNTVSKKGFQ
     ANFFSEKKNN IQKLQQLNEV NRGQQNQAPK RVRPRMRLRT VKKTRPP
//
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