BMP7_HUMAN
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 03-AUG-2022, entry version 224.
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.
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 [12]
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 [13]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 293-431.
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 [14] {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 [15] {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 {ECO:0000269|PubMed:12478285, ECO:0000269|PubMed:12667445,
CC ECO:0000269|PubMed:27923061, ECO:0000269|PubMed:31208997,
CC ECO:0000269|PubMed:9748228}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with SOSTDC1
CC (PubMed:15020244). Interacts with TWSG1 (By similarity). Interacts with
CC FBN1 (via N-terminal domain) and FBN2 (PubMed:18339631). Interacts with
CC type I receptor ACVR1 (PubMed:9748228). Interacts with type II receptor
CC ACVR2A (PubMed:12667445). Interacts with NOG; this interaction inhibits
CC canonical BMP signaling (PubMed:12478285). Interacts with SCUBE3
CC (PubMed:33308444). {ECO:0000250|UniProtKB:P23359,
CC ECO:0000269|PubMed:12478285, ECO:0000269|PubMed:12667445,
CC ECO:0000269|PubMed:18339631, ECO:0000269|PubMed:33308444,
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";
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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; 80.
DR DIP; DIP-5800N; -.
DR IntAct; P18075; 36.
DR MINT; P18075; -.
DR STRING; 9606.ENSP00000379204; -.
DR GlyGen; P18075; 4 sites.
DR iPTMnet; P18075; -.
DR PhosphoSitePlus; P18075; -.
DR BioMuta; BMP7; -.
DR DMDM; 115078; -.
DR EPD; P18075; -.
DR MassIVE; P18075; -.
DR MaxQB; P18075; -.
DR PaxDb; P18075; -.
DR PeptideAtlas; P18075; -.
DR PRIDE; P18075; -.
DR ProteomicsDB; 53544; -.
DR Antibodypedia; 14123; 941 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 CTD; 655; -.
DR DisGeNET; 655; -.
DR GeneCards; BMP7; -.
DR HGNC; HGNC:1074; BMP7.
DR HPA; ENSG00000101144; Tissue enhanced (brain, choroid plexus, thyroid gland).
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; HKEFRFD; -.
DR OrthoDB; 1063560at2759; -.
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; 8 hits in 1075 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 173 other tissues.
DR ExpressionAtlas; P18075; baseline and differential.
DR Genevisible; P18075; HS.
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; IBA:GO_Central.
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:BHF-UCL.
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:0060548; P:negative regulation of cell death; IDA:UniProtKB.
DR GO; GO:0072125; P:negative regulation of glomerular mesangial cell proliferation; IDA:UniProtKB.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; 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 NIK/NF-kappaB signaling; ISS:BHF-UCL.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0042326; P:negative regulation of phosphorylation; IDA:UniProtKB.
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:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
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: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:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; IDA:UniProtKB.
DR GO; GO:0060687; P:regulation of branching involved in prostate gland morphogenesis; IEA:Ensembl.
DR GO; GO:0060393; P:regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
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:0060395; P:SMAD protein signal transduction; IDA:UniProtKB.
DR GO; GO:0043401; P:steroid hormone mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0001657; P:ureteric bud development; ISS: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 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
