ID BMP2_MOUSE Reviewed; 394 AA. AC P21274; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 24-NOV-2009, entry version 91. DE RecName: Full=Bone morphogenetic protein 2; DE Short=BMP-2; DE AltName: Full=BMP-2A; DE Flags: Precursor; GN Name=Bmp2; Synonyms=Bmp-2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=94289485; PubMed=8018727; DOI=10.1016/0167-4781(94)90017-5; RA Feng J.Q., Harris M.A., Ghosh-Choudhury N., Feng M., Mundy G.R., RA Harris S.E.; RT "Structure and sequence of mouse bone morphogenetic protein-2 gene RT (BMP-2): comparison of the structures and promoter regions of BMP-2 RT and BMP-4 genes."; RL Biochim. Biophys. Acta 1218:221-224(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-351. RX MEDLINE=90228966; PubMed=1970330; DOI=10.1016/0888-7543(90)90480-I; RA Dickinson M.E., Kobrin M.S., Silan C.M., Kingsley D.M., Justice M.J., RA Miller D.A., Ceci J.D., Lock L.F., Lee A., Buchberg A.M., RA Siracusa L.D., Lyons K.M., Derynck R., Hogan B.L.M., Copeland N.G., RA Jenkins N.A.; RT "Chromosomal localization of seven members of the murine TGF-beta RT superfamily suggests close linkage to several morphogenetic mutant RT loci."; RL Genomics 6:505-520(1990). RN [3] RP INTERACTION WITH SOSTDC1. RX MEDLINE=22984999; PubMed=14623234; DOI=10.1016/j.ydbio.2003.08.011; RA Laurikkala J., Kassai Y., Pakkasjaervi L., Thesleff I., Itoh N.; RT "Identification of a secreted BMP antagonist, ectodin, integrating RT BMP, FGF, and SHH signals from the tooth enamel knot."; RL Dev. Biol. 264:91-105(2003). RN [4] RP INTERACTION WITH GREM2. RX PubMed=15039429; DOI=10.1074/jbc.M402376200; RA Sudo S., Avsian-Kretchmer O., Wang L.S., Hsueh A.J.; RT "Protein related to DAN and cerberus is a bone morphogenetic protein RT antagonist that participates in ovarian paracrine regulation."; RL J. Biol. Chem. 279:23134-23141(2004). RN [5] RP INTERACTION WITH RGMB. RX PubMed=15671031; DOI=10.1074/jbc.M410034200; RA Samad T.A., Rebbapragada A., Bell E., Zhang Y., Sidis Y., Jeong S.-J., RA Campagna J.A., Perusini S., Fabrizio D.A., Schneyer A.L., Lin H.Y., RA Brivanlou A.H., Attisano L., Woolf C.J.; RT "DRAGON, a bone morphogenetic protein co-receptor."; RL J. Biol. Chem. 280:14122-14129(2005). RN [6] RP INTERACTION WITH RGMA. RX PubMed=15975920; DOI=10.1074/jbc.M503511200; RA Babitt J.L., Zhang Y., Samad T.A., Xia Y., Tang J., Campagna J.A., RA Schneyer A.L., Woolf C.J., Lin H.Y.; RT "Repulsive guidance molecule (RGMa), a DRAGON homologue, is a bone RT morphogenetic protein co-receptor."; RL J. Biol. Chem. 280:29820-29827(2005). RN [7] RP INTERACTION WITH RGMC. RX PubMed=16604073; DOI=10.1038/ng1777; RA Babitt J.L., Huang F.W., Wrighting D.M., Xia Y., Sidis Y., Samad T.A., RA Campagna J.A., Chung R.T., Schneyer A.L., Woolf C.J., Andrews N.C., RA Lin H.Y.; RT "Bone morphogenetic protein signaling by hemojuvelin regulates RT hepcidin expression."; RL Nat. Genet. 38:531-539(2006). RN [8] RP INTERACTION WITH RGMA. RX PubMed=17472960; DOI=10.1074/jbc.M701679200; RA Xia Y., Yu P.B., Sidis Y., Beppu H., Bloch K.D., Schneyer A.L., RA Lin H.Y.; RT "Repulsive guidance molecule RGMa alters utilization of bone RT morphogenetic protein (BMP) type II receptors by BMP2 and BMP4."; RL J. Biol. Chem. 282:18129-18140(2007). CC -!- FUNCTION: Induces cartilage and bone formation. CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with SOSTDC1, CC GREM2, RGMA, RGMB and RGMC. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the TGF-beta family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L25602; AAB05665.1; -; Genomic_DNA. DR IPI; IPI00121379; -. DR PIR; A34201; A34201. DR PIR; S45355; S45355. DR UniGene; Mm.103205; -. DR SMR; P21274; 289-394. DR STRING; P21274; -. DR PRIDE; P21274; -. DR Ensembl; ENSMUST00000028836; ENSMUSP00000028836; ENSMUSG00000027358; Mus musculus. DR MGI; MGI:88177; Bmp2. DR HOGENOM; P21274; -. DR HOVERGEN; P21274; -. DR ArrayExpress; P21274; -. DR Bgee; P21274; -. DR CleanEx; MM_BMP2; -. DR Genevestigator; P21274; -. DR GermOnline; ENSMUSG00000027358; Mus musculus. DR GO; GO:0005615; C:extracellular space; IDA:MGI. DR GO; GO:0005125; F:cytokine activity; TAS:MGI. DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW. DR GO; GO:0004745; F:retinol dehydrogenase activity; IDA:MGI. DR GO; GO:0030509; P:BMP signaling pathway; IDA:MGI. DR GO; GO:0030282; P:bone mineralization; IDA:MGI. DR GO; GO:0001658; P:branching involved in ureteric bud morphoge...; IGI:MGI. DR GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW. DR GO; GO:0045165; P:cell fate commitment; IMP:MGI. DR GO; GO:0009790; P:embryonic development; IMP:MGI. DR GO; GO:0040007; P:growth; IEA:InterPro. DR GO; GO:0006954; P:inflammatory response; IEP:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell proliferation; IGI:MGI. DR GO; GO:0042475; P:odontogenesis of dentine-containing tooth; IDA:MGI. DR GO; GO:0001649; P:osteoblast differentiation; IGI:MGI. DR GO; GO:0048711; P:positive regulation of astrocyte differenti...; IDA:MGI. DR GO; GO:0010552; P:positive regulation of gene-specific transc...; IDA:MGI. DR GO; GO:0045669; P:positive regulation of osteoblast different...; IDA:MGI. DR GO; GO:0007179; P:transforming growth factor beta receptor si...; TAS:MGI. DR InterPro; IPR001839; TGFb. DR InterPro; IPR017948; TGFb_CS. DR InterPro; IPR001111; TGFb_N. DR InterPro; IPR015615; TGFbeta. DR PANTHER; PTHR11848; TGFbeta; 1. DR Pfam; PF00019; TGF_beta; 1. DR Pfam; PF00688; TGFb_propeptide; 1. DR SMART; SM00204; TGFB; 1. DR PROSITE; PS00250; TGF_BETA_1; 1. DR PROSITE; PS51362; TGF_BETA_2; 1. PE 1: Evidence at protein level; KW Chondrogenesis; Cleavage on pair of basic residues; Cytokine; KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein; KW Growth factor; Osteogenesis; Secreted; Signal. FT SIGNAL 1 19 Potential. FT PROPEP 20 280 FT /FTId=PRO_0000033826. FT CHAIN 281 394 Bone morphogenetic protein 2. FT /FTId=PRO_0000033827. FT CARBOHYD 134 134 N-linked (GlcNAc...) (Potential). FT CARBOHYD 162 162 N-linked (GlcNAc...) (Potential). FT CARBOHYD 198 198 N-linked (GlcNAc...) (Potential). FT CARBOHYD 336 336 N-linked (GlcNAc...) (Potential). FT DISULFID 294 359 By similarity. FT DISULFID 323 391 By similarity. FT DISULFID 327 393 By similarity. FT DISULFID 358 358 Interchain (By similarity). FT CONFLICT 110 110 T -> S (in Ref. 2). FT CONFLICT 113 114 QL -> HE (in Ref. 2). FT CONFLICT 271 271 G -> R (in Ref. 2). SQ SEQUENCE 394 AA; 44514 MW; FD6A0F10587EED54 CRC64; MVAGTRCLLV LLLPQVLLGG AAGLIPELGR KKFAAASSRP LSRPSEDVLS EFELRLLSMF GLKQRPTPSK DVVVPPYMLD LYRRHSGQPG APAPDHRLER AASRANTVRT FHQLEAVEEL PEMSGKTARR FFFNLSSVPS DEFLTSAELQ IFREQIQEAL GNSSFQHRIN IYEIIKPAAA NLKFPVTRLL DTRLVNQNTS QWESFDVTPA VMRWTTQGHT NHGFVVEVAH LEENPGVSKR HVRISRSLHQ DEHSWSQIRP LLVTFGHDGK GHPLHKREKR QAKHKQRKRL KSSCKRHPLY VDFSDVGWND WIVAPPGYHA FYCHGECPFP LADHLNSTNH AIVQTLVNSV NSKIPKACCV PTELSAISML YLDENEKVVL KNYQDMVVEG CGCR //