Biology:SPPL2A
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Signal peptide peptidase-like 2A, also known as SPPL2A, is a human gene.[1]
Function
This gene is a member of the signal peptide peptidase-like protease (SPPL) family and encodes a lysosomal/late endosomal membrane protein[2] with the conserved active site motifs 'YD' and 'GxGD' in adjacent transmembrane domains (TMDs). This protein plays a role in innate and adaptive immunity by cleaving TNFα in activated dendritic cells.[3][4] A pseudogene of this gene also lies on chromosome 15.[1]
References
- ↑ 1.0 1.1 "Entrez Gene: SPPL2A signal peptide peptidase-like 2A". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84888.
- ↑ "Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail". FEBS Letters 585 (19): 2951–7. 2011. doi:10.1016/j.febslet.2011.08.043. PMID 21896273.
- ↑ "SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 production". Nat. Cell Biol. 8 (8): 843–8. 2006. doi:10.1038/ncb1440. PMID 16829952.
- ↑ "A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD aspartyl protease SPPL2b". Nat. Cell Biol. 8 (8): 894–6. 2006. doi:10.1038/ncb1450. PMID 16829951. https://escholarship.org/content/qt59c2q1jk/qt59c2q1jk.pdf?t=ntc2ir.
Further reading
- "Identification of signal peptide peptidase, a presenilin-type aspartic protease.". Science 296 (5576): 2215–8. 2002. doi:10.1126/science.1070925. PMID 12077416. Bibcode: 2002Sci...296.2215W.
- "Novel class of polytopic proteins with domains associated with putative protease activity.". Biochemistry Mosc. 67 (7): 826–35. 2002. doi:10.1023/A:1016365227942. PMID 12139484.
- "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "The human Imp3 and Imp4 proteins form a ternary complex with hMpp10, which only interacts with the U3 snoRNA in 60–80S ribonucleoprotein complexes". Nucleic Acids Res. 31 (7): 1877–87. 2003. doi:10.1093/nar/gkg300. PMID 12655004.
- "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. 2004. doi:10.1038/ng1285. PMID 14702039.
- "Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins". J. Biol. Chem. 279 (49): 50790–8. 2005. doi:10.1074/jbc.M407898200. PMID 15385547.
- "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
- "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Res. 12 (2): 117–26. 2007. doi:10.1093/dnares/12.2.117. PMID 16303743.
- "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. 2006. doi:10.1101/gr.4039406. PMID 16344560.
- "The Fas ligand intracellular domain is released by ADAM10 and SPPL2a cleavage in T-cells". Cell Death Differ. 14 (9): 1678–87. 2007. doi:10.1038/sj.cdd.4402175. PMID 17557115.
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