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   25-MAY-2022, entry version 94.
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}.
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DR   EMBL; X55031; CAA38850.1; -; mRNA.
DR   EMBL; X63424; CAA45018.1; -; mRNA.
DR   PIR; JH0687; JH0687.
DR   AlphaFoldDB; P25703; -.
DR   SMR; P25703; -.
DR   PRIDE; P25703; -.
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   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_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