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BMP2_TETNG
ID   BMP2_TETNG              Reviewed;         420 AA.
AC   Q804S2; Q4SCZ1;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Bone morphogenetic protein 2;
DE            Short=BMP-2;
DE   Flags: Precursor;
GN   Name=bmp2; ORFNames=GSTENG00020275001;
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Laize V., Pombinho A.R., Cancela M.L.;
RT   "Identification of Tetraodon nigroviridis bone morphogenetic protein 2
RT   (BMP-2) by comparative genomics.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
CC   -!- FUNCTION: Induces cartilage and bone formation. {ECO:0000250}.
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; AF542093; AAO33820.1; -; Genomic_DNA.
DR   EMBL; CAAE01014646; CAG01491.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q804S2; -.
DR   SMR; Q804S2; -.
DR   STRING; 99883.ENSTNIP00000013645; -.
DR   Ensembl; ENSTNIT00000013839; ENSTNIP00000013645; ENSTNIG00000010727.
DR   KEGG; tng:GSTEN00020275G001; -.
DR   GeneTree; ENSGT00940000155666; -.
DR   HOGENOM; CLU_020515_4_2_1; -.
DR   InParanoid; Q804S2; -.
DR   OMA; WTSGKGH; -.
DR   TreeFam; TF351789; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
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:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR   GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
DR   GO; GO:0045168; P:cell-cell signaling involved in cell fate commitment; IEA:Ensembl.
DR   GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR   GO; GO:0048264; P:determination of ventral identity; IEA:Ensembl.
DR   GO; GO:0060030; P:dorsal convergence; IEA:Ensembl.
DR   GO; GO:0009950; P:dorsal/ventral axis specification; IEA:Ensembl.
DR   GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR   GO; GO:0090008; P:hypoblast development; IEA:Ensembl.
DR   GO; GO:0001889; P:liver development; IEA:Ensembl.
DR   GO; GO:0021703; P:locus ceruleus development; IEA:Ensembl.
DR   GO; GO:0001710; P:mesodermal cell fate commitment; IEA:Ensembl.
DR   GO; GO:0042664; P:negative regulation of endodermal cell fate specification; IEA:Ensembl.
DR   GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
DR   GO; GO:0030903; P:notochord development; IEA:Ensembl.
DR   GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR   GO; GO:0061131; P:pancreas field specification; IEA:Ensembl.
DR   GO; GO:0030513; P:positive regulation of BMP signaling pathway; IEA:Ensembl.
DR   GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
DR   GO; GO:0060876; P:semicircular canal formation; IEA:Ensembl.
DR   GO; GO:0055015; P:ventricular cardiac muscle cell development; IEA:Ensembl.
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   3: Inferred from homology;
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..303
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000042925"
FT   CHAIN           304..420
FT                   /note="Bone morphogenetic protein 2"
FT                   /id="PRO_0000042926"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        172
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        320..385
FT                   /evidence="ECO:0000250"
FT   DISULFID        349..417
FT                   /evidence="ECO:0000250"
FT   DISULFID        353..419
FT                   /evidence="ECO:0000250"
FT   DISULFID        384
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        254
FT                   /note="Q -> H (in Ref. 1; AAO33820)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        259
FT                   /note="K -> N (in Ref. 1; AAO33820)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        290
FT                   /note="D -> N (in Ref. 1; AAO33820)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        301
FT                   /note="E -> D (in Ref. 1; AAO33820)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        363
FT                   /note="S -> F (in Ref. 1; AAO33820)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        378
FT                   /note="S -> L (in Ref. 1; AAO33820)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        385
FT                   /note="C -> W (in Ref. 1; AAO33820)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        409
FT                   /note="Y -> F (in Ref. 1; AAO33820)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   420 AA;  47625 MW;  A72B05DDE6D3E6F7 CRC64;
     MVAVVRSLMV LLLAQVLLEG ATGLIPEVGR RRYSESGKQS PQQSEGFLNE FELRLLNMFG
     LKRRPTPSKQ AVVPQYMVDL YRMHSANGDH SAKRPKSMGR HAERAASKAN TIRSFHHEES
     MEALARLKGK TTQQFYFNLT SIPKEELITS AELRIYRDQV MGAASTNNSS TNSSTSDKAH
     AGGFHRINIY EIFGVPQGRE PLARLLDTRL VQDSLTRWES FDVSSAVFQW TSGKGHNHGF
     MIEVLHPEEG EVEQERADKH SRHVRVSRSL HQDRDSWPQA RPLLVTYGHD GRGDSVLHTR
     EKRQAALRKQ RRKHQHKASC KRHALYVDFS DVGWNEWIVA PPGYHAFYCQ GECPFPLADH
     LNSTNHAIVQ TLVNSVNSNI PRACCVPTDL SPISLLYLDE YEKVILKNYQ DMVVEGCGCR
 
 
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