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 24-JAN-2024, entry version 195. 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). RN [7] RP FUNCTION, AND INTERACTION WITH ERFE. RX PubMed=30097509; DOI=10.1182/blood-2018-06-857995; RA Arezes J., Foy N., McHugh K., Sawant A., Quinkert D., Terraube V., RA Brinth A., Tam M., LaVallie E.R., Taylor S., Armitage A.E., Pasricha S.R., RA Cunningham O., Lambert M., Draper S.J., Jasuja R., Drakesmith H.; RT "Erythroferrone inhibits the induction of hepcidin by BMP6."; RL Blood 132:1473-1477(2018). 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). Promotes the expression of HAMP, this is repressed by its CC interaction with ERFE (PubMed:30097509). {ECO:0000250|UniProtKB:P18075, CC ECO:0000269|PubMed:22461901, ECO:0000269|PubMed:30097509, CC ECO:0000269|PubMed:9013703}. CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with CC SOSTDC1 (PubMed:14623234). Interacts with TWSG1 (PubMed:15843411). CC Interacts with FBN1 (via N-terminal domain) and FBN2 (By similarity). CC Interacts with type I receptor ACVR1 (By similarity). Interacts with CC type II receptor ACVR2A (By similarity). Interacts with NOG; this CC interaction inhibits canonical BMP signaling (By similarity). Interacts CC with SCUBE3 (By similarity). Interacts with ERFE; the interaction CC inhibits BMP-induced transcription of HAMP (PubMed:30097509). CC {ECO:0000250|UniProtKB:P18075, ECO:0000269|PubMed:14623234, CC ECO:0000269|PubMed:15843411, ECO:0000269|PubMed:30097509}. 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 GlyCosmos; P23359; 4 sites, No reported glycans. DR GlyGen; P23359; 4 sites. DR iPTMnet; P23359; -. DR PhosphoSitePlus; P23359; -. DR PaxDb; 10090-ENSMUSP00000009143; -. DR ProteomicsDB; 281698; -. DR Antibodypedia; 14123; 1008 antibodies from 45 providers. DR DNASU; 12162; -. DR Ensembl; ENSMUST00000009143.8; ENSMUSP00000009143.8; ENSMUSG00000008999.8. DR GeneID; 12162; -. DR KEGG; mmu:12162; -. DR UCSC; uc008odb.3; mouse. DR AGR; MGI:103302; -. 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; RTIWATE; -. DR OrthoDB; 2912454at2759; -. DR PhylomeDB; P23359; -. DR TreeFam; TF316134; -. DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres. DR BioGRID-ORCS; 12162; 2 hits in 79 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 282 other cell types or tissues. 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:0008285; P:negative regulation of cell population proliferation; IMP:MGI. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:0072125; P:negative regulation of glomerular mesangial cell proliferation; 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:0060686; P:negative regulation of prostatic bud formation; IDA:MGI. 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:1900006; P:positive regulation of dendrite development; ISO:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. 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:0060391; P:positive regulation of SMAD protein signal transduction; ISO:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI. DR GO; GO:0060687; P:regulation of branching involved in prostate gland morphogenesis; IMP: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:0035239; P:tube morphogenesis; IDA:MGI. DR GO; GO:0001657; P:ureteric bud development; IMP:UniProtKB. DR CDD; cd19397; TGF_beta_BMP7; 1. DR Gene3D; 2.60.120.970; -; 1. DR Gene3D; 2.10.90.10; Cystine-knot cytokines; 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:SF135; BONE MORPHOGENETIC PROTEIN 7; 1. DR PANTHER; PTHR11848; TGF-BETA FAMILY; 1. DR Pfam; PF00019; TGF_beta; 1. DR Pfam; PF00688; TGFb_propeptide; 1. DR SMART; SM00204; TGFB; 1. DR SUPFAM; SSF57501; Cystine-knot cytokines; 1. DR PROSITE; PS00250; TGF_BETA_1; 1. DR PROSITE; PS51362; TGF_BETA_2; 1. DR Genevisible; P23359; MM. 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 //