BMP7_MOUSE
ID BMP7_MOUSE Reviewed; 430 AA.
AC P23359; Q91XF7;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Bone morphogenetic protein 7;
DE Short=BMP-7;
DE AltName: Full=Osteogenic protein 1;
DE Short=OP-1;
DE Flags: Precursor;
GN Name=Bmp7; Synonyms=Bmp-7, Op1;
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 [MRNA].
RX PubMed=1715687; DOI=10.1016/0006-291x(91)91342-a;
RA Oezkaynak E., Schnegelsberg P.N.J., Oppermann H.;
RT "Murine osteogenic protein (OP-1): high levels of mRNA in kidney.";
RL Biochem. Biophys. Res. Commun. 179:116-123(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9013703; DOI=10.1006/excr.1996.3411;
RA Jena N., Martin-Seisdedos C., McCue P., Croce C.M.;
RT "BMP7 null mutation in mice: developmental defects in skeleton, kidney, and
RT eye.";
RL Exp. Cell Res. 230:28-37(1997).
RN [4]
RP INTERACTION WITH TWSG1.
RX PubMed=15843411; DOI=10.1242/dev.01822;
RA Zakin L., Reversade B., Kuroda H., Lyons K.M., De Robertis E.M.;
RT "Sirenomelia in Bmp7 and Tsg compound mutant mice: requirement for Bmp
RT signaling in the development of ventral posterior mesoderm.";
RL Development 132:2489-2499(2005).
RN [5]
RP INTERACTION WITH SOSTDC1.
RX PubMed=14623234; DOI=10.1016/j.ydbio.2003.08.011;
RA Laurikkala J., Kassai Y., Pakkasjaervi L., Thesleff I., Itoh N.;
RT "Identification of a secreted BMP antagonist, ectodin, integrating BMP,
RT FGF, and SHH signals from the tooth enamel knot.";
RL Dev. Biol. 264:91-105(2003).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22461901; DOI=10.1371/journal.pone.0034088;
RA Segklia A., Seuntjens E., Elkouris M., Tsalavos S., Stappers E.,
RA Mitsiadis T.A., Huylebroeck D., Remboutsika E., Graf D.;
RT "Bmp7 regulates the survival, proliferation, and neurogenic properties of
RT neural progenitor cells during corticogenesis in the mouse.";
RL PLoS ONE 7:e34088-e34088(2012).
CC -!- FUNCTION: Growth factor of the TGF-beta superfamily that plays
CC important role in various biological processes, including
CC embryogenesis, hematopoiesis, neurogenesis and skeletal morphogenesis
CC (PubMed:9013703, PubMed:22461901). Initiates the canonical BMP
CC signaling cascade by associating with type I receptor ACVR1 and type II
CC receptor ACVR2A. Once all three components are bound together in a
CC complex at the cell surface, ACVR2A phosphorylates and activates ACVR1.
CC In turn, ACVR1 propagates signal by phosphorylating SMAD1/5/8 that
CC travel to the nucleus and act as activators and repressors of
CC transcription of target genes. For specific functions such as growth
CC cone collapse in developing spinal neurons and chemotaxis of monocytes,
CC uses also BMPR2 as type II receptor. Can also signal through non-
CC canonical pathways such as P38 MAP kinase signaling cascade that
CC promotes brown adipocyte differentiation through activation of target
CC genes, including members of the SOX family of transcription factors (By
CC similarity). {ECO:0000250|UniProtKB:P18075,
CC ECO:0000269|PubMed:22461901, ECO:0000269|PubMed:9013703}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with SOSTDC1
CC (PubMed:14623234). Interacts with TWSG1 (PubMed:15843411). Interacts
CC with FBN1 (via N-terminal domain) and FBN2 (By similarity). Interacts
CC with type I receptor ACVR1 (By similarity). Interacts with type II
CC receptor ACVR2A (By similarity). Interacts with NOG; this interaction
CC inhibits canonical BMP signaling (By similarity). Interacts with SCUBE3
CC (By similarity). {ECO:0000250|UniProtKB:P18075,
CC ECO:0000269|PubMed:14623234, ECO:0000269|PubMed:15843411}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: nullDeltion mutant mice die shortly after birth
CC and display developmental defects in kidney, eye, skull, ribcage, and
CC hind limbs. They also show defects in the development of the axial
CC skeleton from the skull to the tail and the ossification of bones.
CC {ECO:0000269|PubMed:22461901}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X56906; CAA40222.1; -; mRNA.
DR EMBL; BC010771; AAH10771.1; -; mRNA.
DR CCDS; CCDS17136.1; -.
DR PIR; JQ1184; JQ1184.
DR RefSeq; NP_031583.2; NM_007557.3.
DR AlphaFoldDB; P23359; -.
DR SMR; P23359; -.
DR BioGRID; 198367; 3.
DR STRING; 10090.ENSMUSP00000009143; -.
DR GlyGen; P23359; 4 sites.
DR iPTMnet; P23359; -.
DR PhosphoSitePlus; P23359; -.
DR PaxDb; P23359; -.
DR PRIDE; P23359; -.
DR ProteomicsDB; 281698; -.
DR Antibodypedia; 14123; 941 antibodies from 45 providers.
DR DNASU; 12162; -.
DR Ensembl; ENSMUST00000009143; ENSMUSP00000009143; ENSMUSG00000008999.
DR GeneID; 12162; -.
DR KEGG; mmu:12162; -.
DR UCSC; uc008odb.3; mouse.
DR CTD; 655; -.
DR MGI; MGI:103302; Bmp7.
DR VEuPathDB; HostDB:ENSMUSG00000008999; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000156490; -.
DR HOGENOM; CLU_020515_4_1_1; -.
DR InParanoid; P23359; -.
DR OMA; HKEFRFD; -.
DR OrthoDB; 1063560at2759; -.
DR PhylomeDB; P23359; -.
DR TreeFam; TF316134; -.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR BioGRID-ORCS; 12162; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Bmp7; mouse.
DR PRO; PR:P23359; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P23359; protein.
DR Bgee; ENSMUSG00000008999; Expressed in molar tooth and 279 other tissues.
DR Genevisible; P23359; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA: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; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:1905069; P:allantois development; IGI:BHF-UCL.
DR GO; GO:0036305; P:ameloblast differentiation; IDA:MGI.
DR GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; IMP:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0007411; P:axon guidance; IDA:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
DR GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IMP:MGI.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IDA:MGI.
DR GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI.
DR GO; GO:0048738; P:cardiac muscle tissue development; IGI:BHF-UCL.
DR GO; GO:0060411; P:cardiac septum morphogenesis; IGI:BHF-UCL.
DR GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
DR GO; GO:0048468; P:cell development; IDA:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0071773; P:cellular response to BMP stimulus; ISO:MGI.
DR GO; GO:0060710; P:chorio-allantoic fusion; IGI:BHF-UCL.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IMP:MGI.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:MGI.
DR GO; GO:0060272; P:embryonic skeletal joint morphogenesis; IMP:MGI.
DR GO; GO:0003272; P:endocardial cushion formation; IGI:BHF-UCL.
DR GO; GO:0030855; P:epithelial cell differentiation; IMP:MGI.
DR GO; GO:0001654; P:eye development; IMP:UniProtKB.
DR GO; GO:0061384; P:heart trabecula morphogenesis; IGI:BHF-UCL.
DR GO; GO:0030902; P:hindbrain development; IGI:BHF-UCL.
DR GO; GO:0001822; P:kidney development; IMP:UniProtKB.
DR GO; GO:1901145; P:mesenchymal cell apoptotic process involved in nephron morphogenesis; IMP:MGI.
DR GO; GO:0048762; P:mesenchymal cell differentiation; ISS:UniProtKB.
DR GO; GO:0060485; P:mesenchyme development; IMP:UniProtKB.
DR GO; GO:0001707; P:mesoderm formation; IGI:MGI.
DR GO; GO:0072136; P:metanephric mesenchymal cell proliferation involved in metanephros development; IGI:UniProtKB.
DR GO; GO:0072133; P:metanephric mesenchyme morphogenesis; IGI:UniProtKB.
DR GO; GO:0070487; P:monocyte aggregation; ISO:MGI.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0072125; P:negative regulation of glomerular mesangial cell proliferation; ISS:UniProtKB.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:UniProtKB.
DR GO; GO:0072040; P:negative regulation of mesenchymal cell apoptotic process involved in nephron morphogenesis; IMP:MGI.
DR GO; GO:0045839; P:negative regulation of mitotic nuclear division; ISS:UniProtKB.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IDA:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IGI:MGI.
DR GO; GO:0042326; P:negative regulation of phosphorylation; ISS:UniProtKB.
DR GO; GO:0060686; P:negative regulation of prostatic bud formation; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0072134; P:nephrogenic mesenchyme morphogenesis; IGI:UniProtKB.
DR GO; GO:0021502; P:neural fold elevation formation; IGI:BHF-UCL.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:MGI.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IDA:MGI.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR GO; GO:0003344; P:pericardium morphogenesis; IGI:BHF-UCL.
DR GO; GO:0060037; P:pharyngeal system development; IGI:BHF-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISO:MGI.
DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; ISS:UniProtKB.
DR GO; GO:1905312; P:positive regulation of cardiac neural crest cell migration involved in outflow tract morphogenesis; IGI:BHF-UCL.
DR GO; GO:0010942; P:positive regulation of cell death; IGI:UniProtKB.
DR GO; GO:1900006; P:positive regulation of dendrite development; ISO:MGI.
DR GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IDA:MGI.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IGI:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:1900106; P:positive regulation of hyaluranon cable assembly; ISO:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:MGI.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:MGI.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
DR GO; GO:0060687; P:regulation of branching involved in prostate gland morphogenesis; IMP:MGI.
DR GO; GO:0060393; P:regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
DR GO; GO:0042325; P:regulation of phosphorylation; ISO:MGI.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:MGI.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISS:UniProtKB.
DR GO; GO:0043401; P:steroid hormone mediated signaling pathway; ISO:MGI.
DR GO; GO:0035239; P:tube morphogenesis; IDA:MGI.
DR GO; GO:0001657; P:ureteric bud development; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Chondrogenesis; Cytokine; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Growth factor; Osteogenesis;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..291
FT /evidence="ECO:0000250"
FT /id="PRO_0000033878"
FT CHAIN 292..430
FT /note="Bone morphogenetic protein 7"
FT /id="PRO_0000033879"
FT REGION 290..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 329..395
FT /evidence="ECO:0000250"
FT DISULFID 358..427
FT /evidence="ECO:0000250"
FT DISULFID 362..429
FT /evidence="ECO:0000250"
FT DISULFID 394
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 167
FT /note="A -> R (in Ref. 1; CAA40222)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 49199 MW; 464F36D5D2E54041 CRC64;
MHVRSLRAAA PHSFVALWAP LFLLRSALAD FSLDNEVHSS FIHRRLRSQE RREMQREILS
ILGLPHRPRP HLQGKHNSAP MFMLDLYNAM AVEESGPDGQ GFSYPYKAVF STQGPPLASL
QDSHFLTDAD MVMSFVNLVE HDKEFFHPRY HHREFRFDLS KIPEGEAVTA AEFRIYKDYI
RERFDNETFQ ITVYQVLQEH SGRESDLFLL DSRTIWASEE GWLVFDITAT SNHWVVNPRH
NLGLQLSVET LDGQSINPKL AGLIGRHGPQ NKQPFMVAFF KATEVHLRSI RSTGGKQRSQ
NRSKTPKNQE ALRMASVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG
ECAFPLNSYM NATNHAIVQT LVHFINPDTV PKPCCAPTQL NAISVLYFDD SSNVILKKYR
NMVVRACGCH
