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 27-MAR-2024, entry version 132.
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; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; 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 morphogenetic
RT 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., Cho K.W.Y.;
RT "Is chordin a long-range- or short-range-acting factor? Roles for BMP1-
RT 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 gastrula and
CC later differentiation of developing organs. Able to cleave chordin
CC (chrd), suggesting that it may act in dorsoventral patterning during
CC early development by regulating the chordin (chrd) activity.
CC {ECO:0000269|PubMed:10864466, 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. {ECO:0000269|PubMed:18775317}.
CC -!- INTERACTION:
CC P98070; 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 tadpoles;
CC little or no expression in morula and late gastrula.
CC -!- PTM: Proteolytically activated in the trans-Golgi network by furin-
CC like/paired basic proprotein convertases, cleavage is not required for
CC secretion. {ECO:0000250}.
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DR EMBL; L12249; AAA16313.1; -; mRNA.
DR PIR; JC2218; JC2218.
DR AlphaFoldDB; P98070; -.
DR SMR; P98070; -.
DR IntAct; P98070; 1.
DR MEROPS; M12.005; -.
DR GlyCosmos; P98070; 5 sites, No reported glycans.
DR AGR; Xenbase:XB-GENE-479195; -.
DR Xenbase; XB-GENE-479195; bmp1.S.
DR BRENDA; 3.4.24.19; 6725.
DR Proteomes; UP000186698; Genome assembly.
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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 3.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 3.
DR InterPro; IPR015446; BMP_1/tolloid-like.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
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 PANTHER; PTHR24251:SF42; BONE MORPHOGENETIC PROTEIN 1; 1.
DR PANTHER; PTHR24251; OVOCHYMASE-RELATED; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 3.
DR Pfam; PF14670; FXa_inhibition; 1.
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; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 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; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Golgi apparatus; Growth factor;
KW Hydrolase; Metal-binding; Metalloprotease; Osteogenesis; Protease;
KW Reference proteome; Repeat; Secreted; Signal; Zinc.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT PROPEP ?..83
FT /evidence="ECO:0000255"
FT /id="PRO_0000028893"
FT CHAIN 84..707
FT /note="Bone morphogenetic protein 1"
FT /id="PRO_0000028894"
FT DOMAIN 84..283
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 285..397
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 398..509
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 510..551
FT /note="EGF-like; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 554..666
FT /note="CUB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT REGION 57..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..707
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 126..282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 146..168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 148..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 285..311
FT /evidence="ECO:0000250"
FT DISULFID 338..360
FT /evidence="ECO:0000250"
FT DISULFID 398..424
FT /evidence="ECO:0000250"
FT DISULFID 451..473
FT /evidence="ECO:0000250"
FT DISULFID 514..526
FT /evidence="ECO:0000250"
FT DISULFID 522..535
FT /evidence="ECO:0000250"
FT DISULFID 537..550
FT /evidence="ECO:0000250"
FT DISULFID 554..580
FT /evidence="ECO:0000250"
FT DISULFID 607..629
FT /evidence="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
//
