Rhomboid, veinlet-like 2 (drosophila)
Rhomboid, veinlet-like 2 (Drosophila) is a protein that in humans is encoded by the RHBDL2 gene.
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Function
The protein encoded by this gene is a member of the rhomboid family of integral membrane proteins. This family contains proteins that are related to Drosophila rhomboid protein. Members of this family are found in both prokaryotes and eukaryotes and are thought to function as intramembrane serine proteases. The encoded protein is thought to release soluble growth factors by proteolytic cleavage of certain membrane-bound substrates, including ephrin B2 and ephrin B3. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## CDS exon combination :: BC137108.1, AY126343.1 [ECO:0000331] RNAseq introns :: single sample supports all introns ERS025085, ERS025087 [ECO:0000348] ##Evidence-Data-END##
References
Further reading
- Adrain, C; Strisovsky, K; Zettl, M; Hu, L; Lemberg, M. K.; Freeman, M (2011). "Mammalian EGF receptor activation by the rhomboid protease RHBDL2". EMBO Reports. 12 (5): 421–7. PMC 3090019
. PMID 21494248. doi:10.1038/embor.2011.50.
- Pascall, J. C.; Brown, K. D. (2004). "Intramembrane cleavage of ephrinB3 by the human rhomboid family protease, RHBDL2". Biochemical and Biophysical Research Communications. 317 (1): 244–52. PMID 15047175. doi:10.1016/j.bbrc.2004.03.039.
- Cheng, T. L.; Wu, Y. T.; Lin, H. Y.; Hsu, F. C.; Liu, S. K.; Chang, B. I.; Chen, W. S.; Lai, C. H.; Shi, G. Y.; Wu, H. L. (2011). "Functions of rhomboid family protease RHBDL2 and thrombomodulin in wound healing". Journal of Investigative Dermatology. 131 (12): 2486–94. PMID 21833011. doi:10.1038/jid.2011.230.
- Xu, J; Zheng, S. L.; Isaacs, S. D.; Wiley, K. E.; Wiklund, F; Sun, J; Kader, A. K.; Li, G; Purcell, L. D.; Kim, S. T.; Hsu, F. C.; Stattin, P; Hugosson, J; Adolfsson, J; Walsh, P. C.; Trent, J. M.; Duggan, D; Carpten, J; Grönberg, H; Isaacs, W. B. (2010). "Inherited genetic variant predisposes to aggressive but not indolent prostate cancer". Proceedings of the National Academy of Sciences. 107 (5): 2136–40. PMC 2836698 . PMID 20080650. doi:10.1073/pnas.0914061107.
- Urban, S; Freeman, M (2003). "Substrate specificity of rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain". Molecular Cell. 11 (6): 1425–34. PMID 12820957. doi:10.1016/s1097-2765(03)00181-3.
- Urban, S; Lee, J. R.; Freeman, M (2001). "Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases". Cell. 107 (2): 173–82. PMID 11672525. doi:10.1016/s0092-8674(01)00525-6.
- Stolk, L; Perry, J. R.; Chasman, D. I.; He, C; Mangino, M; Sulem, P; Barbalic, M; Broer, L; Byrne, E. M.; Ernst, F; Esko, T; Franceschini, N; Gudbjartsson, D. F.; Hottenga, J. J.; Kraft, P; McArdle, P. F.; Porcu, E; Shin, S. Y.; Smith, A. V.; Van Wingerden, S; Zhai, G; Zhuang, W. V.; Albrecht, E; Alizadeh, B. Z.; Aspelund, T; Bandinelli, S; Lauc, L. B.; Beckmann, J. S.; Boban, M; et al. (2012). "Meta-analyses identify 13 loci associated with age at menopause and highlight DNA repair and immune pathways". Nature Genetics. 44 (3): 260–8. PMC 3288642 . PMID 22267201. doi:10.1038/ng.1051.
- Lei, X; Li, Y. M. (2009). "The processing of human rhomboid intramembrane serine protease RHBDL2 is required for its proteolytic activity". Journal of Molecular Biology. 394 (5): 815–25. PMID 19850051. doi:10.1016/j.jmb.2009.10.025.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
