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BMP1_XENLA
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   03-AUG-2022, entry version 127.
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   PRIDE; P98070; -.
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; cd04281; ZnMc_BMP1_TLD; 1.
DR   Gene3D; 2.60.120.290; -; 3.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR029837; BMP-1.
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; PTHR45645:SF24; PTHR45645:SF24; 1.
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; 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
 
 
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