ID   BMP3_XENLA              Reviewed;         458 AA.
AC   Q7T2X7;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Bone morphogenetic protein 3;
DE            Short=BMP-3;
DE            Short=xBMP-3;
DE   Flags: Precursor;
GN   Name=bmp3;
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], FUNCTION, INTERACTION WITH BMP-2; ADMP AND
RP   DERRIERE, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=12885561; DOI=10.1016/s0012-1606(03)00223-9;
RA   Hino J., Nishimatsu S., Nagai T., Matsuo H., Kangawa K., Nohno T.;
RT   "Coordination of BMP-3b and cerberus is required for head formation of
RT   Xenopus embryos.";
RL   Dev. Biol. 260:138-157(2003).
CC   -!- FUNCTION: Dorsalizing factor. Antagonizes mesoderm formation by
CC       ventralizing BMPs. {ECO:0000269|PubMed:12885561}.
CC   -!- SUBUNIT: Homodimer. Can form heterodimers with ADMP, BMP-2-I and/or
CC       BMP-2-II, and DERRIERE.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12885561}.
CC   -!- DEVELOPMENTAL STAGE: Tends to mark the dorsal ectodermal and mesodermal
CC       cells. Initially expressed in the embryonic ectoderm and throughout the
CC       marginal zone from the late blastula to gastrula stages. Expression is
CC       restricted to the chordal and prechordal mesoderm by the neurula
CC       stages, and to certain cells of the cephalic neural crest at the
CC       tailbud stage. {ECO:0000269|PubMed:12885561}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR   EMBL; AB059563; BAC77407.1; -; mRNA.
DR   RefSeq; NP_001084184.1; NM_001090715.1.
DR   AlphaFoldDB; Q7T2X7; -.
DR   PRIDE; Q7T2X7; -.
DR   GeneID; 399354; -.
DR   KEGG; xla:399354; -.
DR   CTD; 399354; -.
DR   Xenbase; XB-GENE-864983; bmp3.L.
DR   OrthoDB; 1002140at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 399354; Expressed in heart 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:0016015; F:morphogen activity; IEA:UniProtKB-KW.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0001649; P:osteoblast differentiation; IEA:InterPro.
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   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Cytokine; Developmental protein;
KW   Differentiation; Disulfide bond; Glycoprotein; Growth factor; Morphogen;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..348
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000033842"
FT   CHAIN           349..458
FT                   /note="Bone morphogenetic protein 3"
FT                   /id="PRO_0000033843"
FT   REGION          244..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          303..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..275
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..318
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        449
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        356..423
FT                   /evidence="ECO:0000250"
FT   DISULFID        385..455
FT                   /evidence="ECO:0000250"
FT   DISULFID        389..457
FT                   /evidence="ECO:0000250"
FT   DISULFID        422
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   458 AA;  51936 MW;  724F8C8CB1417DA6 CRC64;
     MAECRPWLVL WVGCCGCLCL ALGELLNDGL LAVGMGTGDA ARQEEAALPL GDTVSEHMLR
     LYDKYRSGGG RAKESLRYRQ ALPDGNTVRS FRAMNGDEHK KCHYMFNLTS LTSSENILSA
     TLHYYLGDLL NSSHRCPHSL FCTQHGHAKP EFTLYLTLWS FNALQNPTHV ISNFLINVSA
     SQRDHPLWQW KDITQAVRKA KEYGEAVLGF NLTIEYPNHR SIDILGLKPY ILVYANDSAI
     SEPDSVVSSL HGPHTPLALK PNRKTEKAEQ RKKRSTEILL PLQNNELPGA EYQYSVDEEG
     WEERKPYKNL QGRQNEKDKN KKKLRKGSRQ KSQTLQFDEQ TLKKARRKQW NEPRNCARRY
     LKVDFADIGW SEWIISPKSF DAYYCSGACQ FPMPKSLKPS NHATIQSIVR AVGVVPGIPE
     PCCVPEKMSS LSILFLDENK NVVLKVYPNM TVESCACR