BMP3_MOUSE
ID BMP3_MOUSE Reviewed; 468 AA.
AC Q8BHE5;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Bone morphogenetic protein 3;
DE Short=BMP-3;
DE Flags: Precursor;
GN Name=Bmp3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP PROTEIN SEQUENCE OF 260-268, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11138004; DOI=10.1038/83810;
RA Daluiski A., Engstrand T., Bahamonde M.E., Gamer L.W., Agius E.,
RA Stevenson S.L., Cox K., Rosen V., Lyons K.M.;
RT "Bone morphogenetic protein-3 is a negative regulator of bone density.";
RL Nat. Genet. 27:84-88(2001).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH ACVR2B.
RX PubMed=22074949; DOI=10.1210/me.2011-1168;
RA Kokabu S., Gamer L., Cox K., Lowery J., Tsuji K., Raz R., Economides A.,
RA Katagiri T., Rosen V.;
RT "BMP3 suppresses osteoblast differentiation of bone marrow stromal cells
RT via interaction with Acvr2b.";
RL Mol. Endocrinol. 26:87-94(2012).
CC -!- FUNCTION: Negatively regulates bone density. Antagonizes the ability of
CC certain osteogenic BMPs to induce osteoprogenitor differentitation and
CC ossification. {ECO:0000269|PubMed:11138004}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DISRUPTION PHENOTYPE: Adult mice lacking BMP3 have increased bone mass
CC (PubMed:11138004). Targeted loss of BMP3 results also in increased
CC differentiation of early osteoblasts precursors into mature osteoblasts
CC and further supports a role of BMP3 in regulating adult bone mass
CC (PubMed:22074949). {ECO:0000269|PubMed:11138004,
CC ECO:0000269|PubMed:22074949}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; AK037225; BAC29764.1; -; mRNA.
DR EMBL; AK040389; BAC30581.1; -; mRNA.
DR CCDS; CCDS19458.1; -.
DR RefSeq; NP_775580.1; NM_173404.5.
DR AlphaFoldDB; Q8BHE5; -.
DR BioGRID; 225275; 2.
DR STRING; 10090.ENSMUSP00000031278; -.
DR GlyConnect; 2159; 1 N-Linked glycan (1 site).
DR GlyGen; Q8BHE5; 5 sites, 1 N-linked glycan (1 site).
DR PhosphoSitePlus; Q8BHE5; -.
DR MaxQB; Q8BHE5; -.
DR PaxDb; Q8BHE5; -.
DR PRIDE; Q8BHE5; -.
DR ProteomicsDB; 265220; -.
DR Antibodypedia; 25010; 501 antibodies from 35 providers.
DR DNASU; 110075; -.
DR Ensembl; ENSMUST00000031278; ENSMUSP00000031278; ENSMUSG00000029335.
DR GeneID; 110075; -.
DR KEGG; mmu:110075; -.
DR UCSC; uc008ygg.1; mouse.
DR CTD; 651; -.
DR MGI; MGI:88179; Bmp3.
DR VEuPathDB; HostDB:ENSMUSG00000029335; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000159775; -.
DR HOGENOM; CLU_020515_10_1_1; -.
DR InParanoid; Q8BHE5; -.
DR PhylomeDB; Q8BHE5; -.
DR TreeFam; TF316134; -.
DR BioGRID-ORCS; 110075; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q8BHE5; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BHE5; protein.
DR Bgee; ENSMUSG00000029335; Expressed in perichondrium and 129 other tissues.
DR ExpressionAtlas; Q8BHE5; baseline and differential.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0070700; F:BMP receptor binding; ISO:MGI.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; ISO:MGI.
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:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
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; IPR015615; TGF-beta-rel.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; PTHR11848; 1.
DR Pfam; PF00019; TGF_beta; 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..358
FT /evidence="ECO:0000250"
FT /id="PRO_0000033838"
FT CHAIN 359..468
FT /note="Bone morphogenetic protein 3"
FT /id="PRO_0000033839"
FT REGION 29..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 366..433
FT /evidence="ECO:0000250"
FT DISULFID 395..465
FT /evidence="ECO:0000250"
FT DISULFID 399..467
FT /evidence="ECO:0000250"
FT DISULFID 432
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 468 AA; 52774 MW; 28E34717E15C76E4 CRC64;
MAGARGLLCL WLGYFCLNLA QGQRPNLHLP GLRETEPSDR ATGGSPSPDL RPHDKVSEHM
LWLYDRYSGS SRVQATRTPG SQLPGPQPLR GGNTVRSFRA AAAGTPQTKG LHTFNLTSLT
KSENILSATL YFYVGELVNI SLSCPEPQGC SHHTQRQHIQ IDLSAWILKS NQSQLLGHLS
VDVVRPYRDS VSWLSKDITQ LLRKAKQNEE FLIGFNITSR AHELPKRMLF FPEPYILVYA
NDAAISEPES VVSSLQRHRD FTAGTGPRLD SHVREALSVE RRKKRSTGIL LPLQNNELPG
AEYQYKEEGA WEERKPYKSL QTQPPEKSRN KKKQRKGSHQ KGQTLQFDEQ TLKKARRKQW
VEPRNCARRY LKVDFADIGW SEWIISPKSF DAFYCSGACQ FPMPKSLKPS NHATIQSIVR
AVGVVSGIPE PCCVPEKMSS LSILFFDENK NVVLKVYPNM TVDSCACR
