ID BMP7_HUMAN Reviewed; 431 AA. AC P18075; Q9H512; Q9NTQ7; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 24-JAN-2024, entry version 232. DE RecName: Full=Bone morphogenetic protein 7; DE Short=BMP-7; DE AltName: Full=Osteogenic protein 1; DE Short=OP-1; DE AltName: INN=Eptotermin alfa; DE Flags: Precursor; GN Name=BMP7; Synonyms=OP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Placenta; RX PubMed=2357959; DOI=10.1002/j.1460-2075.1990.tb07376.x; RA Oezkaynak E., Rueger D.C., Drier E.A., Corbett C., Ridge R.J., RA Sampath T.K., Oppermann H.; RT "OP-1 cDNA encodes an osteogenic protein in the TGF-beta family."; RL EMBO J. 9:2085-2093(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2263636; DOI=10.1073/pnas.87.24.9843; RA Celeste A.J., Iannazzi J.A., Taylor R.C., Hewick R.M., Rosen V., Wang E.A., RA Wozney J.M.; RT "Identification of transforming growth factor beta family members present RT in bone-inductive protein purified from bovine bone."; RL Proc. Natl. Acad. Sci. U.S.A. 87:9843-9847(1990). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [5] RP PROTEIN SEQUENCE OF 293-302. RX PubMed=17977014; DOI=10.1016/j.pep.2007.09.016; RA Swencki-Underwood B., Mills J.K., Vennarini J., Boakye K., Luo J., RA Pomerantz S., Cunningham M.R., Farrell F.X., Naso M.F., Amegadzie B.; RT "Expression and characterization of a human BMP-7 variant with improved RT biochemical properties."; RL Protein Expr. Purif. 57:312-319(2008). RN [6] RP FUNCTION, AND INTERACTION WITH ACVR1. RX PubMed=9748228; DOI=10.1074/jbc.273.40.25628; RA Macias-Silva M., Hoodless P.A., Tang S.J., Buchwald M., Wrana J.L.; RT "Specific activation of Smad1 signaling pathways by the BMP7 type I RT receptor, ALK2."; RL J. Biol. Chem. 273:25628-25636(1998). RN [7] RP INTERACTION WITH SOSTDC1. RX PubMed=15020244; DOI=10.1016/j.bbrc.2004.02.075; RA Yanagita M., Oka M., Watabe T., Iguchi H., Niida A., Takahashi S., RA Akiyama T., Miyazono K., Yanagisawa M., Sakurai T.; RT "USAG-1: a bone morphogenetic protein antagonist abundantly expressed in RT the kidney."; RL Biochem. Biophys. Res. Commun. 316:490-500(2004). RN [8] RP INTERACTION WITH FBN1 AND FBN2. RX PubMed=18339631; DOI=10.1074/jbc.m707820200; RA Sengle G., Charbonneau N.L., Ono R.N., Sasaki T., Alvarez J., Keene D.R., RA Baechinger H.P., Sakai L.Y.; RT "Targeting of bone morphogenetic protein growth factor complexes to RT fibrillin."; RL J. Biol. Chem. 283:13874-13888(2008). RN [9] RP DEVELOPMENTAL STAGE, VARIANTS PRO-198 AND SER-321, AND ASSOCIATION WITH RP DEVELOPMENTAL EYE ANOMALIES. RX PubMed=20506283; DOI=10.1002/humu.21280; RA Wyatt A.W., Osborne R.J., Stewart H., Ragge N.K.; RT "Bone morphogenetic protein 7 (BMP7) mutations are associated with variable RT ocular, brain, ear, palate, and skeletal anomalies."; RL Hum. Mutat. 31:781-787(2010). RN [10] RP FUNCTION. RX PubMed=27923061; DOI=10.1371/journal.pgen.1006474; RA Brunmeir R., Wu J., Peng X., Kim S.Y., Julien S.G., Zhang Q., Xie W., RA Xu F.; RT "Comparative Transcriptomic and Epigenomic Analyses Reveal New Regulators RT of Murine Brown Adipogenesis."; RL PLoS Genet. 12:E1006474-E1006474(2016). RN [11] RP FUNCTION, AND INTERACTION WITH MOUSE 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). RN [12] RP FUNCTION. RX PubMed=31208997; DOI=10.1242/bio.042283; RA Perron J.C., Rodrigues A.A., Surubholta N., Dodd J.; RT "Chemotropic signaling by BMP7 requires selective interaction at a key RT residue in ActRIIA."; RL Biol. Open 8:0-0(2019). RN [13] RP INTERACTION WITH SCUBE3. RX PubMed=33308444; DOI=10.1016/j.ajhg.2020.11.015; RG Genomics England Research Consortium; RA Lin Y.C., Niceta M., Muto V., Vona B., Pagnamenta A.T., Maroofian R., RA Beetz C., van Duyvenvoorde H., Dentici M.L., Lauffer P., Vallian S., RA Ciolfi A., Pizzi S., Bauer P., Gruening N.M., Bellacchio E., RA Del Fattore A., Petrini S., Shaheen R., Tiosano D., Halloun R., RA Pode-Shakked B., Albayrak H.M., Isik E., Wit J.M., Dittrich M., RA Freire B.L., Bertola D.R., Jorge A.A.L., Barel O., Sabir A.H., RA Al Tenaiji A.M.J., Taji S.M., Al-Sannaa N., Al-Abdulwahed H., Digilio M.C., RA Irving M., Anikster Y., Bhavani G.S.L., Girisha K.M., Haaf T., Taylor J.C., RA Dallapiccola B., Alkuraya F.S., Yang R.B., Tartaglia M.; RT "SCUBE3 loss-of-function causes a recognizable recessive developmental RT disorder due to defective bone morphogenetic protein signaling."; RL Am. J. Hum. Genet. 108:115-133(2021). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 293-431, AND SUBUNIT. RX PubMed=8570652; DOI=10.1073/pnas.93.2.878; RA Griffith D.L., Keck P.C., Sampath T.K., Rueger D.C., Carlson W.D.; RT "Three-dimensional structure of recombinant human osteogenic protein 1: RT structural paradigm for the transforming growth factor beta superfamily."; RL Proc. Natl. Acad. Sci. U.S.A. 93:878-883(1996). RN [15] {ECO:0007744|PDB:1M4U} RP X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 293-431, GLYCOSYLATION AT RP ASN-372, INTERACTION WITH NOG, AND FUNCTION. RX PubMed=12478285; DOI=10.1038/nature01245; RA Groppe J., Greenwald J., Wiater E., Rodriguez-Leon J., Economides A.N., RA Kwiatkowski W., Affolter M., Vale W.W., Izpisua Belmonte J.C., Choe S.; RT "Structural basis of BMP signalling inhibition by the cystine knot protein RT Noggin."; RL Nature 420:636-642(2002). RN [16] {ECO:0007744|PDB:1LX5, ECO:0007744|PDB:1LXI} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 293-431, GLYCOSYLATION AT RP ASN-372, INTERACTION WITH ACVR2A, AND FUNCTION. RX PubMed=12667445; DOI=10.1016/s1097-2765(03)00094-7; RA Greenwald J., Groppe J., Gray P., Wiater E., Kwiatkowski W., Vale W., RA Choe S.; RT "The BMP7/ActRII extracellular domain complex provides new insights into RT the cooperative nature of receptor assembly."; RL Mol. Cell 11:605-617(2003). 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:31208997). Initiates the canonical BMP signaling cascade by CC associating with type I receptor ACVR1 and type II receptor ACVR2A CC (PubMed:9748228, PubMed:12667445). Once all three components are bound CC together in a complex at the cell surface, ACVR2A phosphorylates and CC activates ACVR1. In turn, ACVR1 propagates signal by phosphorylating CC SMAD1/5/8 that travel to the nucleus and act as activators and CC repressors of transcription of target genes (PubMed:12478285). For CC specific functions such as growth cone collapse in developing spinal CC neurons and chemotaxis of monocytes, uses also BMPR2 as type II CC receptor (PubMed:31208997). Can also signal through non-canonical CC pathways such as P38 MAP kinase signaling cascade that promotes brown CC adipocyte differentiation through activation of target genes, including CC members of the SOX family of transcription factors (PubMed:27923061). CC Promotes the expression of HAMP, this is repressed by its interaction CC with ERFE (PubMed:30097509). {ECO:0000269|PubMed:12478285, CC ECO:0000269|PubMed:12667445, ECO:0000269|PubMed:27923061, CC ECO:0000269|PubMed:30097509, ECO:0000269|PubMed:31208997, CC ECO:0000269|PubMed:9748228}. CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:8570652). Interacts with CC SOSTDC1 (PubMed:15020244). Interacts with TWSG1 (By similarity). CC Interacts with FBN1 (via N-terminal domain) and FBN2 (PubMed:18339631). CC Interacts with type I receptor ACVR1 (PubMed:9748228). Interacts with CC type II receptor ACVR2A (PubMed:12667445). Interacts with NOG; this CC interaction inhibits canonical BMP signaling (PubMed:12478285). CC Interacts with SCUBE3 (PubMed:33308444). Interacts with ERFE; the CC interaction inhibits BMP-induced transcription of HAMP CC (PubMed:30097509). {ECO:0000250|UniProtKB:P23359, CC ECO:0000269|PubMed:12478285, ECO:0000269|PubMed:12667445, CC ECO:0000269|PubMed:18339631, ECO:0000269|PubMed:30097509, CC ECO:0000269|PubMed:33308444, ECO:0000269|PubMed:8570652, CC ECO:0000269|PubMed:9748228}. CC -!- INTERACTION: CC P18075; Q9BUH8: BEGAIN; NbExp=3; IntAct=EBI-1035195, EBI-742722; CC P18075; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-1035195, EBI-11977221; CC P18075; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-1035195, EBI-3867333; CC P18075; Q5VWX1: KHDRBS2; NbExp=3; IntAct=EBI-1035195, EBI-742808; CC P18075; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-1035195, EBI-11749135; CC P18075; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-1035195, EBI-10171774; CC P18075; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-1035195, EBI-10172052; CC P18075; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-1035195, EBI-11953334; CC P18075; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-1035195, EBI-9996449; CC P18075; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-1035195, EBI-3958099; CC P18075; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-1035195, EBI-11958364; CC P18075; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-1035195, EBI-22310682; CC P18075; P14373: TRIM27; NbExp=4; IntAct=EBI-1035195, EBI-719493; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed in the kidney and bladder. Lower levels CC seen in the brain. CC -!- DEVELOPMENTAL STAGE: Expressed in the developing eye, brain and ear CC during embryogenesis. {ECO:0000269|PubMed:20506283}. CC -!- PTM: Several N-termini starting at positions 293, 300, 315 and 316 have CC been identified by direct sequencing resulting in secretion of CC different mature forms. {ECO:0000269|PubMed:17977014}. CC -!- PHARMACEUTICAL: Available under the name Osigraft (Stryker). Its use is CC indicated in the treatment of tibial non-union of at least 9 months CC duration, secondary to trauma, in skeletally mature patients, in cases CC where autograft has failed or is unfeasible. CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Bone morphogenetic protein 7 entry; CC URL="https://en.wikipedia.org/wiki/Bone_morphogenetic_protein_7"; 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; X51801; CAA36100.1; -; mRNA. DR EMBL; M60316; AAA36738.1; -; mRNA. DR EMBL; AL122058; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL157414; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC008584; AAH08584.1; -; mRNA. DR CCDS; CCDS13455.1; -. DR PIR; C39263; BMHU7. DR RefSeq; NP_001710.1; NM_001719.2. DR PDB; 1BMP; X-ray; 2.80 A; A=293-431. DR PDB; 1LX5; X-ray; 3.30 A; A=293-431. DR PDB; 1LXI; X-ray; 2.00 A; A=293-431. DR PDB; 1M4U; X-ray; 2.42 A; L=293-431. DR PDBsum; 1BMP; -. DR PDBsum; 1LX5; -. DR PDBsum; 1LXI; -. DR PDBsum; 1M4U; -. DR AlphaFoldDB; P18075; -. DR SMR; P18075; -. DR BioGRID; 107123; 81. DR DIP; DIP-5800N; -. DR IntAct; P18075; 36. DR MINT; P18075; -. DR STRING; 9606.ENSP00000379204; -. DR GlyCosmos; P18075; 4 sites, No reported glycans. DR GlyGen; P18075; 5 sites, 1 O-linked glycan (1 site). DR iPTMnet; P18075; -. DR PhosphoSitePlus; P18075; -. DR BioMuta; BMP7; -. DR DMDM; 115078; -. DR EPD; P18075; -. DR MassIVE; P18075; -. DR MaxQB; P18075; -. DR PaxDb; 9606-ENSP00000379204; -. DR PeptideAtlas; P18075; -. DR ProteomicsDB; 53544; -. DR Antibodypedia; 14123; 1008 antibodies from 45 providers. DR DNASU; 655; -. DR Ensembl; ENST00000395863.8; ENSP00000379204.3; ENSG00000101144.13. DR GeneID; 655; -. DR KEGG; hsa:655; -. DR MANE-Select; ENST00000395863.8; ENSP00000379204.3; NM_001719.3; NP_001710.1. DR UCSC; uc010gip.2; human. DR AGR; HGNC:1074; -. DR CTD; 655; -. DR DisGeNET; 655; -. DR GeneCards; BMP7; -. DR HGNC; HGNC:1074; BMP7. DR HPA; ENSG00000101144; Tissue enhanced (choroid plexus, thyroid gland). DR MalaCards; BMP7; -. DR MIM; 112267; gene. DR neXtProt; NX_P18075; -. DR OpenTargets; ENSG00000101144; -. DR PharmGKB; PA25384; -. DR VEuPathDB; HostDB:ENSG00000101144; -. DR eggNOG; KOG3900; Eukaryota. DR GeneTree; ENSGT00940000156490; -. DR InParanoid; P18075; -. DR OMA; RTIWATE; -. DR OrthoDB; 2912454at2759; -. DR PhylomeDB; P18075; -. DR TreeFam; TF316134; -. DR PathwayCommons; P18075; -. DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres. DR SignaLink; P18075; -. DR SIGNOR; P18075; -. DR BioGRID-ORCS; 655; 11 hits in 1153 CRISPR screens. DR ChiTaRS; BMP7; human. DR EvolutionaryTrace; P18075; -. DR GeneWiki; Bone_morphogenetic_protein_7; -. DR GenomeRNAi; 655; -. DR Pharos; P18075; Tbio. DR PRO; PR:P18075; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; P18075; Protein. DR Bgee; ENSG00000101144; Expressed in pigmented layer of retina and 175 other cell types or tissues. DR ExpressionAtlas; P18075; baseline and differential. DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0031982; C:vesicle; IEA:Ensembl. DR GO; GO:0070700; F:BMP receptor binding; IPI:BHF-UCL. 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; IEA:Ensembl. DR GO; GO:1905069; P:allantois development; ISS:BHF-UCL. DR GO; GO:0036305; P:ameloblast differentiation; IEA:Ensembl. DR GO; GO:0007411; P:axon guidance; IEA:Ensembl. DR GO; GO:0030509; P:BMP signaling pathway; IDA:UniProtKB. DR GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IEA:Ensembl. DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Ensembl. DR GO; GO:0048738; P:cardiac muscle tissue development; ISS:BHF-UCL. DR GO; GO:0060411; P:cardiac septum morphogenesis; ISS:BHF-UCL. DR GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW. DR GO; GO:0071773; P:cellular response to BMP stimulus; IMP:BHF-UCL. DR GO; GO:0071456; P:cellular response to hypoxia; ISS:BHF-UCL. DR GO; GO:0060710; P:chorio-allantoic fusion; ISS:BHF-UCL. DR GO; GO:0016358; P:dendrite development; TAS:BHF-UCL. DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IEA:Ensembl. DR GO; GO:0030326; P:embryonic limb morphogenesis; IEA:Ensembl. DR GO; GO:0009880; P:embryonic pattern specification; IEA:Ensembl. DR GO; GO:0060272; P:embryonic skeletal joint morphogenesis; IEA:Ensembl. DR GO; GO:0003272; P:endocardial cushion formation; ISS:BHF-UCL. DR GO; GO:0001837; P:epithelial to mesenchymal transition; TAS:HGNC-UCL. DR GO; GO:0061384; P:heart trabecula morphogenesis; ISS:BHF-UCL. DR GO; GO:0030902; P:hindbrain development; ISS:BHF-UCL. DR GO; GO:1901145; P:mesenchymal cell apoptotic process involved in nephron morphogenesis; IEA:Ensembl. DR GO; GO:0048762; P:mesenchymal cell differentiation; IDA:UniProtKB. DR GO; GO:0060485; P:mesenchyme development; ISS:UniProtKB. DR GO; GO:0001707; P:mesoderm formation; IEA:Ensembl. DR GO; GO:0001823; P:mesonephros development; IEP:UniProtKB. DR GO; GO:0072136; P:metanephric mesenchymal cell proliferation involved in metanephros development; IEA:Ensembl. DR GO; GO:0072133; P:metanephric mesenchyme morphogenesis; IEA:Ensembl. DR GO; GO:0001656; P:metanephros development; IEP:UniProtKB. DR GO; GO:0070487; P:monocyte aggregation; IDA:UniProtKB. DR GO; GO:0045786; P:negative regulation of cell cycle; IDA:HGNC-UCL. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0072125; P:negative regulation of glomerular mesangial cell proliferation; IDA:UniProtKB. DR GO; GO:0072040; P:negative regulation of mesenchymal cell apoptotic process involved in nephron morphogenesis; IEA:Ensembl. DR GO; GO:0045839; P:negative regulation of mitotic nuclear division; IDA:UniProtKB. DR GO; GO:0050768; P:negative regulation of neurogenesis; IEA:Ensembl. DR GO; GO:0045665; P:negative regulation of neuron differentiation; IDA:MGI. DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:BHF-UCL. DR GO; GO:1901223; P:negative regulation of non-canonical NF-kappaB signal transduction; ISS:BHF-UCL. DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IEA:Ensembl. DR GO; GO:0060686; P:negative regulation of prostatic bud formation; IEA:Ensembl. DR GO; GO:0010664; P:negative regulation of striated muscle cell apoptotic process; ISS:BHF-UCL. DR GO; GO:0072134; P:nephrogenic mesenchyme morphogenesis; IEA:Ensembl. DR GO; GO:0021502; P:neural fold elevation formation; ISS:BHF-UCL. DR GO; GO:0048812; P:neuron projection morphogenesis; IDA:MGI. DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl. DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW. DR GO; GO:0003344; P:pericardium morphogenesis; ISS:BHF-UCL. DR GO; GO:0060037; P:pharyngeal system development; ISS:BHF-UCL. DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0030501; P:positive regulation of bone mineralization; IDA:BHF-UCL. DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IMP:UniProtKB. DR GO; GO:1905312; P:positive regulation of cardiac neural crest cell migration involved in outflow tract morphogenesis; IEA:Ensembl. DR GO; GO:1900006; P:positive regulation of dendrite development; IDA:BHF-UCL. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IEA:Ensembl. DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL. DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IDA:UniProtKB. DR GO; GO:1900106; P:positive regulation of hyaluranon cable assembly; IDA:UniProtKB. DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl. DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:BHF-UCL. DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0060687; P:regulation of branching involved in prostate gland morphogenesis; IEA:Ensembl. DR GO; GO:0042325; P:regulation of phosphorylation; IEA:Ensembl. DR GO; GO:2000121; P:regulation of removal of superoxide radicals; ISS:BHF-UCL. 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:0001501; P:skeletal system development; TAS:ProtInc. DR GO; GO:0001657; P:ureteric bud development; ISS: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; P18075; HS. PE 1: Evidence at protein level; KW 3D-structure; Chondrogenesis; Cytokine; Developmental protein; KW Differentiation; Direct protein sequencing; Disulfide bond; Glycoprotein; KW Growth factor; Osteogenesis; Pharmaceutical; Reference proteome; Secreted; KW Signal. FT SIGNAL 1..29 FT /evidence="ECO:0000255" FT PROPEP 30..292 FT /evidence="ECO:0000269|PubMed:17977014" FT /id="PRO_0000033876" FT CHAIN 293..431 FT /note="Bone morphogenetic protein 7" FT /id="PRO_0000033877" FT REGION 291..311 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 187 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 302 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 321 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 372 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12478285, FT ECO:0000269|PubMed:12667445" FT DISULFID 330..396 FT DISULFID 359..428 FT DISULFID 363..430 FT DISULFID 395 FT /note="Interchain" FT VARIANT 198 FT /note="L -> P (found in a patient with unilateral FT microphthalmia, optic disk and chorioretinal coloboma, mild FT learning difficulties; dbSNP:rs376798352)" FT /evidence="ECO:0000269|PubMed:20506283" FT /id="VAR_064058" FT VARIANT 321 FT /note="N -> S (in dbSNP:rs61733438)" FT /evidence="ECO:0000269|PubMed:20506283" FT /id="VAR_064059" FT STRAND 329..333 FT /evidence="ECO:0007829|PDB:1LXI" FT STRAND 336..338 FT /evidence="ECO:0007829|PDB:1LXI" FT HELIX 339..342 FT /evidence="ECO:0007829|PDB:1LXI" FT TURN 345..347 FT /evidence="ECO:0007829|PDB:1LXI" FT STRAND 348..350 FT /evidence="ECO:0007829|PDB:1LXI" FT STRAND 352..355 FT /evidence="ECO:0007829|PDB:1LXI" FT STRAND 358..362 FT /evidence="ECO:0007829|PDB:1LXI" FT STRAND 365..368 FT /evidence="ECO:0007829|PDB:1M4U" FT HELIX 369..371 FT /evidence="ECO:0007829|PDB:1LXI" FT HELIX 375..386 FT /evidence="ECO:0007829|PDB:1LXI" FT TURN 388..390 FT /evidence="ECO:0007829|PDB:1LXI" FT STRAND 396..409 FT /evidence="ECO:0007829|PDB:1LXI" FT HELIX 411..413 FT /evidence="ECO:0007829|PDB:1BMP" FT STRAND 415..430 FT /evidence="ECO:0007829|PDB:1LXI" SQ SEQUENCE 431 AA; 49313 MW; 47A05E45C6815F8A CRC64; MHVRSLRAAA PHSFVALWAP LFLLRSALAD FSLDNEVHSS FIHRRLRSQE RREMQREILS ILGLPHRPRP HLQGKHNSAP MFMLDLYNAM AVEEGGGPGG QGFSYPYKAV FSTQGPPLAS LQDSHFLTDA DMVMSFVNLV EHDKEFFHPR YHHREFRFDL SKIPEGEAVT AAEFRIYKDY IRERFDNETF RISVYQVLQE HLGRESDLFL LDSRTLWASE EGWLVFDITA TSNHWVVNPR HNLGLQLSVE TLDGQSINPK LAGLIGRHGP QNKQPFMVAF FKATEVHFRS IRSTGSKQRS QNRSKTPKNQ EALRMANVAE NSSSDQRQAC KKHELYVSFR DLGWQDWIIA PEGYAAYYCE GECAFPLNSY MNATNHAIVQ TLVHFINPET VPKPCCAPTQ LNAISVLYFD DSSNVILKKY RNMVVRACGC H //