Rhomboid, veinlet-like 2 (drosophila)

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External IDs	GeneCards: [1]
Orthologs
Species	Human	Mouse
Entrez	n/a	n/a
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UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
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Rhomboid, veinlet-like 2 (Drosophila) is a protein that in humans is encoded by the RHBDL2 gene.

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.

Further reading

• Adrain C, Strisovsky K, Zettl M, Hu L, Lemberg MK, Freeman M (May 2011). "Mammalian EGF receptor activation by the rhomboid protease RHBDL2". EMBO Reports. 12 (5): 421–7. doi:10.1038/embor.2011.50. PMC 3090019. PMID 21494248.
• Pascall JC, Brown KD (April 2004). "Intramembrane cleavage of ephrinB3 by the human rhomboid family protease, RHBDL2". Biochemical and Biophysical Research Communications. 317 (1): 244–52. doi:10.1016/j.bbrc.2004.03.039. PMID 15047175.
• Cheng TL, Wu YT, Lin HY, Hsu FC, Liu SK, Chang BI, Chen WS, Lai CH, Shi GY, Wu HL (December 2011). "Functions of rhomboid family protease RHBDL2 and thrombomodulin in wound healing". The Journal of Investigative Dermatology. 131 (12): 2486–94. doi:10.1038/jid.2011.230. PMID 21833011.
• Xu J, Zheng SL, Isaacs SD, Wiley KE, Wiklund F, Sun J, Kader AK, Li G, Purcell LD, Kim ST, Hsu FC, Stattin P, Hugosson J, Adolfsson J, Walsh PC, Trent JM, Duggan D, Carpten J, Grönberg H, Isaacs WB (February 2010). "Inherited genetic variant predisposes to aggressive but not indolent prostate cancer". Proceedings of the National Academy of Sciences of the United States of America. 107 (5): 2136–40. doi:10.1073/pnas.0914061107. PMC 2836698. PMID 20080650.
• Urban S, Freeman M (June 2003). "Substrate specificity of rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain". Molecular Cell. 11 (6): 1425–34. doi:10.1016/s1097-2765(03)00181-3. PMID 12820957.
• Urban S, Lee JR, Freeman M (October 2001). "Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases". Cell. 107 (2): 173–82. doi:10.1016/s0092-8674(01)00525-6. PMID 11672525.
• Lei X, Li YM (December 2009). "The processing of human rhomboid intramembrane serine protease RHBDL2 is required for its proteolytic activity". Journal of Molecular Biology. 394 (5): 815–25. doi:10.1016/j.jmb.2009.10.025. PMID 19850051.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.