BMP3_BOVIN
ID BMP3_BOVIN Reviewed; 475 AA.
AC P22444;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Bone morphogenetic protein 3;
DE Short=BMP-3;
DE AltName: Full=Osteogenin;
DE Flags: Precursor;
GN Name=BMP3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP PROTEIN SEQUENCE OF 366-387; 396-407 AND 428-445.
RC TISSUE=Bone;
RX PubMed=2547759; DOI=10.1016/s0021-9258(18)80003-5;
RA Luyten F.P., Cunningham N.S., Ma S., Muthukumaran N., Hammonds R.G.,
RA Nevins W.B., Wood W.I., Reddi A.H.;
RT "Purification and partial amino acid sequence of osteogenin, a protein
RT initiating bone differentiation.";
RL J. Biol. Chem. 264:13377-13380(1989).
CC -!- FUNCTION: Induces cartilage and bone formation.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR PIR; A32624; A32624.
DR RefSeq; NP_001179197.1; NM_001192268.1.
DR AlphaFoldDB; P22444; -.
DR SMR; P22444; -.
DR STRING; 9913.ENSBTAP00000023468; -.
DR PaxDb; P22444; -.
DR Ensembl; ENSBTAT00000023468; ENSBTAP00000023468; ENSBTAG00000017642.
DR GeneID; 539527; -.
DR KEGG; bta:539527; -.
DR CTD; 651; -.
DR VEuPathDB; HostDB:ENSBTAG00000017642; -.
DR VGNC; VGNC:26518; BMP3.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000159775; -.
DR HOGENOM; CLU_020515_10_0_1; -.
DR InParanoid; P22444; -.
DR OMA; KWDSHIR; -.
DR OrthoDB; 1002140at2759; -.
DR TreeFam; TF316134; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000017642; Expressed in lung and 62 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0070700; F:BMP receptor binding; IEA:Ensembl.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:InterPro.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
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 Chondrogenesis; Cleavage on pair of basic residues; Cytokine;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Growth factor; Osteogenesis;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..365
FT /evidence="ECO:0000269|PubMed:2547759"
FT /id="PRO_0000285573"
FT CHAIN 366..475
FT /note="Bone morphogenetic protein 3"
FT /id="PRO_0000051609"
FT REGION 68..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 373..440
FT /evidence="ECO:0000250"
FT DISULFID 402..472
FT /evidence="ECO:0000250"
FT DISULFID 406..474
FT /evidence="ECO:0000250"
FT DISULFID 439
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 373..375
FT /note="CAR -> NAA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 53501 MW; FACEF068F3F4CF4E CRC64;
MAGARGLLHL WLSCLCVSLA QGQRLRQPFP ELRVAVPADR AAGGGPESPL QPLDQVSEHM
LRLYDRYSGG RTEEARTPGN SERGSPSLRP QPLREGNTVR SFRAGAAGML ENKELHIFNL
TSLTKSENIL SATLYFYIRE LINISLSCPV SQECSHHAQR KHIQIDLSAW ILKSSGNQSQ
LLGHLSVDGG KPHRDFVSWL SKDITQLLRK AKENEEFLIG FNITTKGHQL PKKMTPSPEP
YILVYANDAA ISEPESVVSS LQGHRNFPTG AVPKLDSQSR SAPSIERRRR KRSTGVLLPL
QNNELPGAEY QYKEDEVWEE RKPYKTLQTQ PPDKSKNKKK QRKGPQQKSQ TLQFDEQTLK
KARRKQWIEP RNCARRYLKV DFADIGWSEW IISPKSFDAY YCSGACQFPM PKSLKPSNHA
TIQSIVRAVG VVPGIPEPCC VPEKMSSLSI LFFDENKNVV LKVYPNMTVE SCACR
