ID   BMP3_RAT                Reviewed;         468 AA.
AC   P49002;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 134.
DE   RecName: Full=Bone morphogenetic protein 3;
DE            Short=BMP-3;
DE   Flags: Precursor;
GN   Name=Bmp3; Synonyms=Bmp-3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Calvaria;
RX   PubMed=8605043; DOI=10.1006/bbrc.1996.0289;
RA   Takao M., Hino J., Takeshita N., Konno Y., Nishizawa T., Matsuo H.,
RA   Kangawa K.;
RT   "Identification of rat bone morphogenetic protein-3b (BMP-3b), a new member
RT   of BMP-3.";
RL   Biochem. Biophys. Res. Commun. 219:656-662(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 109-468.
RC   TISSUE=Calvaria;
RX   PubMed=7880444; DOI=10.1089/dna.1995.14.235;
RA   Chen D., Feng J.Q., Feng M., Harris M.A., Mahy P., Mundy G.R., Harris S.E.;
RT   "Sequence and expression of bone morphogenetic protein 3 mRNA in prolonged
RT   cultures of fetal rat calvarial osteoblasts and in rat prostate
RT   adenocarcinoma PA III cells.";
RL   DNA Cell Biol. 14:235-239(1995).
RN   [3]
RP   INDUCTION.
RX   PubMed=12689682; DOI=10.1016/s8756-3282(03)00029-2;
RA   Wang F.-S., Yang K.D., Kuo Y.-R., Wang C.-J., Sheen-Chen S.-M.,
RA   Huang H.-C., Chen Y.-J.;
RT   "Temporal and spatial expression of bone morphogenetic proteins in
RT   extracorporeal shock wave-promoted healing of segmental defect.";
RL   Bone 32:387-396(2003).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=27130896; DOI=10.1016/j.brainres.2016.04.057;
RA   Yamashita K., Mikawa S., Sato K.;
RT   "BMP3 expression in the adult rat CNS.";
RL   Brain Res. 1643:35-50(2016).
CC   -!- FUNCTION: Negatively regulates bone density. Antagonizes the ability of
CC       certain osteogenic BMPs to induce osteoprogenitor differentitation and
CC       ossification (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in embryonic calvaria and femur, and in
CC       adult aorta, costa, femur, kidney, lung, ovary, spleen and trachea
CC       (PubMed:8605043). Widely expressed throughout the adult central nervous
CC       system, including most neurons and their axons (PubMed:27130896).
CC       {ECO:0000269|PubMed:27130896, ECO:0000269|PubMed:8605043}.
CC   -!- INDUCTION: Expression increases in mesenchymal cells at fracture sites
CC       during healing. Also highly expressed in chondrocytes and osteoblasts
CC       at newly formed cartilage and bone. {ECO:0000269|PubMed:12689682}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR   EMBL; D63860; BAA09922.1; -; mRNA.
DR   EMBL; S77492; AAB33725.1; -; mRNA.
DR   PIR; I53032; I53032.
DR   RefSeq; NP_058801.1; NM_017105.1.
DR   AlphaFoldDB; P49002; -.
DR   SMR; P49002; -.
DR   STRING; 10116.ENSRNOP00000032031; -.
DR   GlyGen; P49002; 5 sites.
DR   PaxDb; P49002; -.
DR   GeneID; 25667; -.
DR   KEGG; rno:25667; -.
DR   UCSC; RGD:2212; rat.
DR   CTD; 651; -.
DR   RGD; 2212; Bmp3.
DR   eggNOG; KOG3900; Eukaryota.
DR   InParanoid; P49002; -.
DR   OrthoDB; 1002140at2759; -.
DR   PhylomeDB; P49002; -.
DR   PRO; PR:P49002; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0031982; C:vesicle; IDA:RGD.
DR   GO; GO:0070700; F:BMP receptor binding; ISO:RGD.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0008083; F:growth factor activity; IDA:RGD.
DR   GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
DR   GO; GO:0001649; P:osteoblast differentiation; IEA:InterPro.
DR   GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR017197; BMP3/BMP3B.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR001839; TGF-b_C.
DR   InterPro; IPR001111; TGF-b_propeptide.
DR   InterPro; IPR015615; TGF-beta-rel.
DR   InterPro; IPR017948; TGFb_CS.
DR   PANTHER; PTHR11848; PTHR11848; 1.
DR   Pfam; PF00019; TGF_beta; 1.
DR   Pfam; PF00688; TGFb_propeptide; 1.
DR   PIRSF; PIRSF037403; BMP3/GDF10; 1.
DR   SMART; SM00204; TGFB; 1.
DR   SUPFAM; SSF57501; SSF57501; 1.
DR   PROSITE; PS00250; TGF_BETA_1; 1.
DR   PROSITE; PS51362; TGF_BETA_2; 1.
PE   2: Evidence at transcript level;
KW   Chondrogenesis; Cleavage on pair of basic residues; Cytokine;
KW   Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW   Growth factor; Osteogenesis; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..358
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000033840"
FT   CHAIN           359..468
FT                   /note="Bone morphogenetic protein 3"
FT                   /id="PRO_0000033841"
FT   REGION          27..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          316..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        459
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        366..433
FT                   /evidence="ECO:0000250"
FT   DISULFID        395..465
FT                   /evidence="ECO:0000250"
FT   DISULFID        399..467
FT                   /evidence="ECO:0000250"
FT   DISULFID        432
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   468 AA;  52675 MW;  05315D4954DC3CA1 CRC64;
     MAGARGLLCL WLGCFCLNLA QGQRPNLHLP GLRGTESSDR MTGGGPSPDL RPHDKVSEHM
     LWLYDRYSGS NRAQATRTPG SQLPGPQPLR GGNTVRSFRA AAAGTLQRKG LHTFNLTSLT
     KSENILSATL YFYIGELVNT SVNCPESQGC SHDSQRQHIQ IDLSAWTLQS NQSQLLGHLS
     VDTAKPYRDS MSWLSKDITQ LLRKAKQDEE FLIGFNITSR AHELPKRMLL FPEPYILVYA
     NDAAICEPES VVSSLQRHRD FTAGTVPRLD SHVREALSVE RRKKRSTGIL LPLQNNELPG
     AEYQYKEAGV WEERKPYKSL QTQPPEKSRS KKKQRKGPHQ KGQTLQFDEQ TLKKARRKQW
     IEPRNCARRY LKVDFADIGW SEWIISPKSF DAYYCSGACQ FPMPKSLKPS NHATIQSIVR
     AVGVVSGIPE PCCVPEKMSS LSILFFDENK NVVLKVYPNM TVDSCACR