Transforming growth factor, beta 3

Transforming growth factor, beta 3

PDB rendering based on 1ktz.

Available structures
PDB	1KTZ, 1TGJ, 1TGK, 2PJY, 3EO1

Identifiers

TGFB3; ARVD; FLJ16571; TGF-beta3

External IDs

OMIM: 190230 MGI: 98727 HomoloGene: 2433 GeneCards: TGFB3 Gene

Gene Ontology
Molecular function	• type II transforming growth factor beta receptor binding • type II transforming growth factor beta receptor binding • protein binding • protein binding • growth factor activity • type I transforming growth factor beta receptor binding • identical protein binding • protein heterodimerization activity • transforming growth factor beta binding
Cellular component	• extracellular region • extracellular space • nucleus • cytoplasm • plasma membrane • cell surface • stored secretory granule • T-tubule • extracellular matrix • platelet alpha granule lumen • neuronal cell body
Biological process	• activation of MAPK activity • response to hypoxia • in utero embryonic development • platelet degranulation • induction of apoptosis • transforming growth factor beta receptor signaling pathway • salivary gland morphogenesis • female pregnancy • aging • blood coagulation • negative regulation of DNA replication • negative regulation of cell proliferation • positive regulation of epithelial to mesenchymal transition • positive regulation of epithelial to mesenchymal transition • positive regulation of pathway-restricted SMAD protein phosphorylation • negative regulation of macrophage cytokine production • cell growth • menstrual cycle phase • platelet activation • positive regulation of bone mineralization • negative regulation of transforming growth factor beta receptor signaling pathway • mammary gland development • response to progesterone stimulus • positive regulation of collagen biosynthetic process • response to laminar fluid shear stress • odontogenesis • negative regulation of neuron apoptosis • response to estrogen stimulus • ossification involved in bone remodeling • cell-cell junction organization • positive regulation of DNA replication • positive regulation of transcription, DNA-dependent • positive regulation of transcription, DNA-dependent • positive regulation of transcription from RNA polymerase II promoter • lung alveolus development • digestive tract development • embryonic neurocranium morphogenesis • inner ear development • positive regulation of protein secretion • positive regulation of filopodium assembly • positive regulation of cell division • palate development • face morphogenesis • frontal suture morphogenesis • positive regulation of SMAD protein import into nucleus • detection of hypoxia
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

ENSG00000119699

ENSMUSG00000021253

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 14:
76.42 – 76.45 Mb

Chr 12:
87.4 – 87.42 Mb

PubMed search

Transforming growth factor beta-3 is a protein that in humans is encoded by the TGFB3 gene.^[1]^[2]

Contents

1 Interactions
2 References
3 External links
4 Further reading

Interactions

Transforming growth factor, beta 3 has been shown to interact with TGF beta receptor 2.^[3]^[4]^[5]^[6]

References

^ Bandyopadhyay B, Fan J, Guan S, Li Y, Chen M, Woodley DT, Li W (Mar 2006). "A "traffic control" role for TGFbeta3: orchestrating dermal and epidermal cell motility during wound healing". J Cell Biol 172 (7): 1093–105. doi:10.1083/jcb.200507111. PMC 2063766. PMID 16549496. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2063766.
^ "Entrez Gene: TGFB3 transforming growth factor, beta 3". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7043.
^ De Crescenzo, Gregory; Pham Phuong L, Durocher Yves, O'Connor-McCourt Maureen D (May. 2003). "Transforming growth factor-beta (TGF-beta) binding to the extracellular domain of the type II TGF-beta receptor: receptor capture on a biosensor surface using a new coiled-coil capture system demonstrates that avidity contributes significantly to high affinity binding". J. Mol. Biol. (England) 328 (5): 1173–83. doi:10.1016/S0022-2836(03)00360-7. ISSN 0022-2836. PMID 12729750.
^ Hart, P John; Deep Shashank, Taylor Alexander B, Shu Zhanyong, Hinck Cynthia S, Hinck Andrew P (Mar. 2002). "Crystal structure of the human TbetaR2 ectodomain--TGF-beta3 complex". Nat. Struct. Biol. (United States) 9 (3): 203–8. doi:10.1038/nsb766. ISSN 1072-8368. PMID 11850637.
^ Barbara, N P; Wrana J L, Letarte M (Jan. 1999). "Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily". J. Biol. Chem. (UNITED STATES) 274 (2): 584–94. doi:10.1074/jbc.274.2.584. ISSN 0021-9258. PMID 9872992.
^ Rotzer, D; Roth M, Lutz M, Lindemann D, Sebald W, Knaus P (Feb. 2001). "Type III TGF-beta receptor-independent signalling of TGF-beta2 via TbetaRII-B, an alternatively spliced TGF-beta type II receptor". EMBO J. (England) 20 (3): 480–90. doi:10.1093/emboj/20.3.480. ISSN 0261-4189. PMC 133482. PMID 11157754. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=133482.

External links

Further reading

Kalluri R, Neilson EG (2004). "Epithelial-mesenchymal transition and its implications for fibrosis.". J. Clin. Invest. 112 (12): 1776–84. doi:10.1172/JCI20530. PMC 297008. PMID 14679171. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=297008.
Arrick BA, Lee AL, Grendell RL, Derynck R (1991). "Inhibition of translation of transforming growth factor-beta 3 mRNA by its 5' untranslated region.". Mol. Cell. Biol. 11 (9): 4306–13. PMC 361291. PMID 1875922. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=361291.
ten Dijke P, Hansen P, Iwata KK, et al. (1988). "Identification of another member of the transforming growth factor type beta gene family.". Proc. Natl. Acad. Sci. U.S.A. 85 (13): 4715–9. doi:10.1073/pnas.85.13.4715. PMC 280506. PMID 3164476. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=280506.
Derynck R, Lindquist PB, Lee A, et al. (1989). "A new type of transforming growth factor-beta, TGF-beta 3.". EMBO J. 7 (12): 3737–43. PMC 454948. PMID 3208746. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=454948.
Barton DE, Foellmer BE, Du J, et al. (1989). "Chromosomal mapping of genes for transforming growth factors beta 2 and beta 3 in man and mouse: dispersion of TGF-beta gene family.". Oncogene Res. 3 (4): 323–31. PMID 3226728.
Kaartinen V, Voncken JW, Shuler C, et al. (1996). "Abnormal lung development and cleft palate in mice lacking TGF-beta 3 indicates defects of epithelial-mesenchymal interaction.". Nat. Genet. 11 (4): 415–21. doi:10.1038/ng1295-415. PMID 7493022.
Nishida K, Sotozono C, Adachi W, et al. (1995). "Transforming growth factor-beta 1, -beta 2 and -beta 3 mRNA expression in human cornea.". Curr. Eye Res. 14 (3): 235–41. doi:10.3109/02713689509033520. PMID 7796607.
Lin HY, Moustakas A, Knaus P, et al. (1995). "The soluble exoplasmic domain of the type II transforming growth factor (TGF)-beta receptor. A heterogeneously glycosylated protein with high affinity and selectivity for TGF-beta ligands.". J. Biol. Chem. 270 (6): 2747–54. doi:10.1074/jbc.270.6.2747. PMID 7852346.
Rampazzo A, Nava A, Danieli GA, et al. (1994). "The gene for arrhythmogenic right ventricular cardiomyopathy maps to chromosome 14q23-q24.". Hum. Mol. Genet. 3 (6): 959–62. doi:10.1093/hmg/3.6.959. PMID 7951245.
Zhao Y, Chegini N, Flanders KC (1994). "Human fallopian tube expresses transforming growth factor (TGF beta) isoforms, TGF beta type I-III receptor messenger ribonucleic acid and protein, and contains [125I]TGF beta-binding sites.". J. Clin. Endocrinol. Metab. 79 (4): 1177–84. doi:10.1210/jc.79.4.1177. PMID 7962292.
Hildebrand A, Romarís M, Rasmussen LM, et al. (1994). "Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta.". Biochem. J. 302 ( Pt 2): 527–34. PMC 1137259. PMID 8093006. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1137259.
López-Casillas F, Payne HM, Andres JL, Massagué J (1994). "Betaglycan can act as a dual modulator of TGF-beta access to signaling receptors: mapping of ligand binding and GAG attachment sites.". J. Cell Biol. 124 (4): 557–68. doi:10.1083/jcb.124.4.557. PMC 2119924. PMID 8106553. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2119924.
Mittl PR, Priestle JP, Cox DA, et al. (1997). "The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: implications for receptor binding.". Protein Sci. 5 (7): 1261–71. doi:10.1002/pro.5560050705. PMC 2143453. PMID 8819159. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2143453.
Ambros RA, Kallakury BV, Malfetano JH, Mihm MC (1997). "Cytokine, cell adhesion receptor, and tumor suppressor gene expression in vulvar squamous carcinoma: correlation with prominent fibromyxoid stromal response.". Int. J. Gynecol. Pathol. 15 (4): 320–5. doi:10.1097/00004347-199610000-00004. PMID 8886879.
Djonov V, Ball RK, Graf S, et al. (1997). "Transforming growth factor-beta 3 is expressed in nondividing basal epithelial cells in normal human prostate and benign prostatic hyperplasia, and is no longer detectable in prostate carcinoma.". Prostate 31 (2): 103–9. doi:10.1002/(SICI)1097-0045(19970501)31:2<103::AID-PROS5>3.0.CO;2-O. PMID 9140123.
Jin L, Qian X, Kulig E, et al. (1997). "Transforming growth factor-beta, transforming growth factor-beta receptor II, and p27Kip1 expression in nontumorous and neoplastic human pituitaries.". Am. J. Pathol. 151 (2): 509–19. PMC 1858020. PMID 9250163. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1858020.
Lidral AC, Romitti PA, Basart AM, et al. (1998). "Association of MSX1 and TGFB3 with nonsyndromic clefting in humans.". Am. J. Hum. Genet. 63 (2): 557–68. doi:10.1086/301956. PMC 1377298. PMID 9683588. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1377298.
Barbara NP, Wrana JL, Letarte M (1999). "Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily.". J. Biol. Chem. 274 (2): 584–94. doi:10.1074/jbc.274.2.584. PMID 9872992.
Lux A, Attisano L, Marchuk DA (1999). "Assignment of transforming growth factor beta1 and beta3 and a third new ligand to the type I receptor ALK-1.". J. Biol. Chem. 274 (15): 9984–92. doi:10.1074/jbc.274.15.9984. PMID 10187774.
Mori T, Kawara S, Shinozaki M, et al. (1999). "Role and interaction of connective tissue growth factor with transforming growth factor-beta in persistent fibrosis: A mouse fibrosis model.". J. Cell. Physiol. 181 (1): 153–9. doi:10.1002/(SICI)1097-4652(199910)181:1<153::AID-JCP16>3.0.CO;2-K. PMID 10457363.

PDB gallery

1ktz: Crystal Structure of the Human TGF-beta Type II Receptor Extracellular Domain in Complex with TGF-beta3

1tgj: HUMAN TRANSFORMING GROWTH FACTOR-BETA 3, CRYSTALLIZED FROM DIOXANE

1tgk: HUMAN TRANSFORMING GROWTH FACTOR BETA 3, CRYSTALLIZED FROM PEG 4000