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BMP7_CANLF
ID   BMP7_CANLF              Reviewed;         187 AA.
AC   P34819;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Bone morphogenetic protein 7;
DE            Short=BMP-7;
DE   AltName: Full=Osteogenic protein 1;
DE            Short=OP-1;
DE   Flags: Fragment;
GN   Name=BMP7;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Cocker spaniel; TISSUE=Kidney;
RX   PubMed=8503913; DOI=10.1006/bbrc.1993.1614;
RA   Ishibashi K., Sasaki S., Akiba T., Marumo F.;
RT   "Expression of bone morphogenic protein 7 mRNA in MDCK cells.";
RL   Biochem. Biophys. Res. Commun. 193:235-239(1993).
CC   -!- FUNCTION: Growth factor of the TGF-beta superfamily that plays
CC       important role in various biological processes, including
CC       embryogenesis, hematopoiesis, neurogenesis and skeletal morphogenesis.
CC       Initiates the canonical BMP signaling cascade by associating with type
CC       I receptor ACVR1 and type II receptor ACVR2A. Once all three components
CC       are bound together in a complex at the cell surface, ACVR2A
CC       phosphorylates and activates ACVR1. In turn, ACVR1 propagates signal by
CC       phosphorylating SMAD1/5/8 that travel to the nucleus and act as
CC       activators and repressors of transcription of target genes. For
CC       specific functions such as growth cone collapse in developing spinal
CC       neurons and chemotaxis of monocytes, uses also BMPR2 as type II
CC       receptor. Can also signal through non-canonical pathways such as P38
CC       MAP kinase signaling cascade that promotes brown adipocyte
CC       differentiation through activation of target genes, including members
CC       of the SOX family of transcription factors.
CC       {ECO:0000250|UniProtKB:P18075}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with SOSTDC1 (By
CC       similarity). Interacts with TWSG1 (By similarity). Interacts with FBN1
CC       (via N-terminal domain) and FBN2. Interacts with type I receptor ACVR1.
CC       Interacts with type II receptor ACVR2A. Interacts with NOG; this
CC       interaction inhibits canonical BMP signaling (By similarity). Interacts
CC       with SCUBE3 (By similarity). {ECO:0000250|UniProtKB:P18075,
CC       ECO:0000250|UniProtKB:P23359}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR   EMBL; D17697; BAA04560.1; -; mRNA.
DR   PIR; PN0496; PN0496.
DR   AlphaFoldDB; P34819; -.
DR   STRING; 9612.ENSCAFP00000017683; -.
DR   PaxDb; P34819; -.
DR   eggNOG; KOG3900; Eukaryota.
DR   InParanoid; P34819; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0070700; F:BMP receptor binding; IBA:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR   GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
DR   GO; GO:0048762; P:mesenchymal cell differentiation; ISS:UniProtKB.
DR   GO; GO:0060485; P:mesenchyme development; ISS:UniProtKB.
DR   GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
DR   GO; GO:0072125; P:negative regulation of glomerular mesangial cell proliferation; ISS:UniProtKB.
DR   GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:UniProtKB.
DR   GO; GO:0045839; P:negative regulation of mitotic nuclear division; ISS:UniProtKB.
DR   GO; GO:0042326; P:negative regulation of phosphorylation; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR   GO; GO:0090336; P:positive regulation of brown fat cell differentiation; ISS:UniProtKB.
DR   GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
DR   GO; GO:0060395; P:SMAD protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0001657; P:ureteric bud development; ISS:UniProtKB.
DR   InterPro; IPR001111; TGF-b_propeptide.
DR   InterPro; IPR015615; TGF-beta-rel.
DR   PANTHER; PTHR11848; PTHR11848; 1.
DR   Pfam; PF00688; TGFb_propeptide; 1.
PE   2: Evidence at transcript level;
KW   Chondrogenesis; Cytokine; Developmental protein; Differentiation;
KW   Disulfide bond; Glycoprotein; Growth factor; Osteogenesis;
KW   Reference proteome; Secreted.
FT   CHAIN           <1..>187
FT                   /note="Bone morphogenetic protein 7"
FT                   /id="PRO_0000051610"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT   NON_TER         187
SQ   SEQUENCE   187 AA;  21489 MW;  2188415747C61820 CRC64;
     GKHNSAPMFM LDLYNAMAVE EGGGPAGQGF SYPYKAVFST QGPPLASLQD SHFLTDADMV
     MSFVNLVEHD KEFFHPRYHH REFRFDLSKI PEGEAVTAAE FRIYKDYIRE RFDNETFRIS
     VYQVLQEHLG RESDLFLLDS RTLWASEEGW LVFDITATSN HWVVNPRHNL GLQLCVETLD
     GQSINPK
 
 
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