ID BMP2A_XENLA Reviewed; 398 AA. AC P25703; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 27-MAR-2024, entry version 100. DE RecName: Full=Bone morphogenetic protein 2-A; DE AltName: Full=BMP-2-I; DE Flags: Precursor; GN Name=bmp2-a; 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]. RX PubMed=2054389; DOI=10.1016/0167-4781(91)90026-i; RA Plessow S., Koester M., Knoechel W.; RT "cDNA sequence of Xenopus laevis bone morphogenetic protein 2 (BMP-2)."; RL Biochim. Biophys. Acta 1089:280-282(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1510675; DOI=10.1016/s0006-291x(05)81574-8; RA Nishimatsu S., Suzuki A., Shoda A., Murakami K., Ueno N.; RT "Genes for bone morphogenetic proteins are differentially transcribed in RT early amphibian embryos."; RL Biochem. Biophys. Res. Commun. 186:1487-1495(1992). CC -!- FUNCTION: Induces cartilage and bone formation. CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:P12643}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X55031; CAA38850.1; -; mRNA. DR EMBL; X63424; CAA45018.1; -; mRNA. DR PIR; JH0687; JH0687. DR AlphaFoldDB; P25703; -. DR SMR; P25703; -. DR GlyCosmos; P25703; 3 sites, No reported glycans. DR AGR; Xenbase:XB-GENE-481833; -. DR Xenbase; XB-GENE-481833; bmp2.S. DR Proteomes; UP000186698; Genome assembly. DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW. DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW. DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW. 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 CDD; cd19390; TGF_beta_BMP2; 1. DR Gene3D; 2.60.120.970; -; 1. DR Gene3D; 2.10.90.10; Cystine-knot cytokines; 1. DR InterPro; IPR047953; BMP2_TGF_beta-like. 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:SF143; BONE MORPHOGENETIC PROTEIN 2; 1. DR PANTHER; PTHR11848; TGF-BETA FAMILY; 1. DR Pfam; PF00019; TGF_beta; 1. DR Pfam; PF00688; TGFb_propeptide; 1. DR PRINTS; PR00669; INHIBINA. DR SMART; SM00204; TGFB; 1. DR SUPFAM; SSF57501; Cystine-knot cytokines; 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..23 FT /evidence="ECO:0000255" FT PROPEP 24..284 FT /evidence="ECO:0000255" FT /id="PRO_0000033832" FT CHAIN 285..398 FT /note="Bone morphogenetic protein 2-A" FT /id="PRO_0000033833" FT CARBOHYD 137 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 202 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 340 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 298..363 FT /evidence="ECO:0000250" FT DISULFID 327..395 FT /evidence="ECO:0000250" FT DISULFID 331..397 FT /evidence="ECO:0000250" FT DISULFID 362 FT /note="Interchain" FT /evidence="ECO:0000250" FT CONFLICT 7 FT /note="S -> P (in Ref. 2; CAA45018)" FT /evidence="ECO:0000305" FT CONFLICT 16 FT /note="V -> L (in Ref. 2; CAA45018)" FT /evidence="ECO:0000305" FT CONFLICT 233 FT /note="N -> T (in Ref. 2; CAA45018)" FT /evidence="ECO:0000305" SQ SEQUENCE 398 AA; 45575 MW; 150AC64A47D2E15F CRC64; MVAGIHSLLL LLFYQVLLSG CTGLIPEEGK RKYTESGRSS PQQSQRVLNQ FELRLLSMFG LKRRPTPGKN VVIPPYMLDL YHLHLAQLAA DEGTSAMDFQ MERAASRANT VRSFHHEESM EEIPESREKT IQRFFFNLSS IPNEELVTSA ELRIFREQVQ EPFESDSSKL HRINIYDIVK PAAAASRGPV VRLLDTRLVH HNESKWESFD VTPAIARWIA HKQPNHGFVV EVNHLDNDKN VPKKHVRISR SLTPDKDNWP QIRPLLVTFS HDGKGHALHK RQKRQARHKQ RKRLKSSCRR HPLYVDFSDV GWNDWIVAPP GYHAFYCHGE CPFPLADHLN STNHAIVQTL VNSVNTNIPK ACCVPTELSA ISMLYLDENE KVVLKNYQDM VVEGCGCR //