ID   BMP2B_XENLA             Reviewed;         398 AA.
AC   P30884;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Bone morphogenetic protein 2-B;
DE   AltName: Full=BMP-2-II;
DE   Flags: Precursor;
GN   Name=bmp2-b;
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].
RC   TISSUE=Oocyte;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11677055; DOI=10.1016/s0925-4773(01)00506-8;
RA   Knoechel S., Dillinger K., Koester M., Knoechel W.;
RT   "Structure and expression of Xenopus tropicalis BMP-2 and BMP-4 genes.";
RL   Mech. Dev. 109:79-82(2001).
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}.
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DR   EMBL; X63425; CAA45019.1; -; mRNA.
DR   EMBL; AJ315159; CAC44177.1; -; Genomic_DNA.
DR   PIR; JH0688; JH0688.
DR   RefSeq; NP_001095136.1; NM_001101666.1.
DR   AlphaFoldDB; P30884; -.
DR   SMR; P30884; -.
DR   GeneID; 397873; -.
DR   KEGG; xla:397873; -.
DR   CTD; 397873; -.
DR   Xenbase; XB-GENE-6252323; bmp2.L.
DR   OrthoDB; 962484at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 397873; Expressed in blastula and 13 other tissues.
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   Gene3D; 2.10.90.10; -; 1.
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   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..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..284
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000033834"
FT   CHAIN           285..398
FT                   /note="Bone morphogenetic protein 2-B"
FT                   /id="PRO_0000033835"
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        237
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"
SQ   SEQUENCE   398 AA;  45616 MW;  60E41FA2C8E603DC CRC64;
     MVAGIHSLLL LQFYQILLSG CTGLVPEEGK RKYSESTRSS PQQSQQVLDQ FELRLLNMFG
     LKRRPTPGKN VVIPPYMLDL YHLHSAQLAD DQGSSEVDYH MERAASRANT VRSFHHEESM
     EEIPESGEKT IQRFFFNLSS IPDEELVTSS ELRIFREQVQ EPFKTDGSKL HRINIYDIVK
     PAAAASRGPV VRLLDTRLIH HNESKWESFD VTPAITRWIA HKQPNHGFVV EVTHLDNDTN
     VPKRHVRISR SLTLDKGHWP RIRPLLVTFS HDGKGHALHK RQKRQARHKQ RKRLKSSCRR
     HPLYVDFSDV GWNDWIVAPP GYHAFYCHGE CPFPLADHLN STNHAIVQTL VNSVNTNIPK
     ACCVPTELSA ISMLYLDENE KVVLKNYQDM VVEGCGCR