Rhomboid, veinlet-like 2 (drosophila)

Rhomboid, veinlet-like 2 (Drosophila) is a protein that in humans is encoded by the RHBDL2 gene.[5]

RHBDL2
Identifiers
Aliases	RHBDL2, RRP2, rhomboid like 2
External IDs	OMIM: 608962 MGI: 3608413 HomoloGene: 49508 GeneCards: RHBDL2
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p34.3 Start 38,885,807 bp[1] End 38,941,830 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4|4 D2.2 Start 123,787,874 bp[2] End 123,829,904 bp[2]
Gene ontology Molecular function • peptidase activity • serine-type peptidase activity • serine-type endopeptidase activity • hydrolase activity Cellular component • integral component of membrane • cell membrane • membrane Biological process • protein processing • proteolysis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	54933	230726
Ensembl	ENSG00000158315	ENSMUSG00000043333
UniProt	Q9NX52	A2AGA4
RefSeq (mRNA)	NM_017821 NM_001304746	NM_183163 NM_001356445
RefSeq (protein)	NP_001291675 NP_060291	NP_898986 NP_001343374
Location (UCSC)	Chr 1: 38.89 – 38.94 Mb	Chr 4: 123.79 – 123.83 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.

References

1. GRCh38: Ensembl release 89: ENSG00000158315 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000043333 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: Rhomboid, veinlet-like 2 (Drosophila)".

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.