SPPL2B
| SPPL2B | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | SPPL2B, IMP-4, IMP4, PSH4, PSL1, signal peptide peptidase like 2B | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 608239; MGI: 1920468; GeneCards: SPPL2B | |||||||||||||||||||||||||||||||||||||||||||||||||||||
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Signal peptide peptidase-like 2B, also known as SPPL2B, is a human gene.[5]
Gene
Multiple transcript variants encoding different isoforms have been found for this gene.[5]
Subcellular distribution
This enzyme localizes to endosomes, lysosomes, and the plasma membrane.
Structure
This gene is a member of the signal peptide peptidase-like protease (SPPL) family with the conserved active site motifs 'YD' and 'GxGD' in adjacent transmembrane domains (TMDs).
Function
This protein plays a role in innate and adaptive immunity by cleaving TNFα in activated dendritic cells.[6][7] SPPL2b also modulates APP cleavage and Aβ production.[8]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000005206 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000035206 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ a b "Entrez Gene: SPPL2B signal peptide peptidase-like 2B".
- ^ Friedmann E, Hauben E, Maylandt K, Schleeger S, Vreugde S, Lichtenthaler SF, et al. (August 2006). "SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 production". Nature Cell Biology. 8 (8): 843–848. doi:10.1038/ncb1440. PMID 16829952. S2CID 129089.
- ^ Fluhrer R, Grammer G, Israel L, Condron MM, Haffner C, Friedmann E, et al. (August 2006). "A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD aspartyl protease SPPL2b". Nature Cell Biology. 8 (8): 894–896. doi:10.1038/ncb1450. PMID 16829951. S2CID 23712486.
- ^ Maccioni R, Travisan C, Badman J, Zerial S, Wagener A, Andrade-Talavera Y, et al. (April 2024). "Signal peptide peptidase-like 2b modulates the amyloidogenic pathway and exhibits an Aβ-dependent expression in Alzheimer's disease". Progress in Neurobiology. 235 102585. doi:10.1016/j.pneurobio.2024.102585. PMID 38367747.
Further reading
- Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
- Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O (April 2000). "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 7 (2): 143–150. doi:10.1093/dnares/7.2.143. PMID 10819331.
- Weihofen A, Binns K, Lemberg MK, Ashman K, Martoglio B (June 2002). "Identification of signal peptide peptidase, a presenilin-type aspartic protease". Science. 296 (5576). New York, N.Y.: 2215–2218. Bibcode:2002Sci...296.2215W. doi:10.1126/science.1070925. PMID 12077416. S2CID 45633906.
- Grigorenko AP, Moliaka YK, Korovaitseva GI, Rogaev EI (2003). "Novel class of polytopic proteins with domains associated with putative protease activity". Biochemistry. Biokhimiia. 67 (7). Mosc: 826–835. doi:10.1023/A:1016365227942. PMID 12139484. S2CID 11785597.
- Friedmann E, Lemberg MK, Weihofen A, Dev KK, Dengler U, Rovelli G, et al. (December 2004). "Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins". The Journal of Biological Chemistry. 279 (49): 50790–50798. doi:10.1074/jbc.M407898200. hdl:2262/89311. PMID 15385547.
- Krawitz P, Haffner C, Fluhrer R, Steiner H, Schmid B, Haass C (November 2005). "Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenilin homologues SPPL2b and SPPL3". The Journal of Biological Chemistry. 280 (47): 39515–39523. doi:10.1074/jbc.M501645200. PMID 15998642.
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