SPPL2B

Protein-coding gene in the species Homo sapiens
SPPL2B
Identifiers
AliasesSPPL2B, IMP-4, IMP4, PSH4, PSL1, signal peptide peptidase like 2B
External IDsOMIM: 608239; MGI: 1920468; HomoloGene: 10605; GeneCards: SPPL2B; OMA:SPPL2B - orthologs
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for SPPL2B
Genomic location for SPPL2B
Band19p13.3Start2,328,615 bp[1]
End2,355,095 bp[1]
Gene location (Mouse)
Chromosome 10 (mouse)
Chr.Chromosome 10 (mouse)[2]
Chromosome 10 (mouse)
Genomic location for SPPL2B
Genomic location for SPPL2B
Band10|10 C1Start80,691,109 bp[2]
End80,704,542 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right uterine tube

  • anterior pituitary

  • left testis

  • right testis

  • right hemisphere of cerebellum

  • transverse colon

  • right lobe of thyroid gland

  • body of pancreas

  • left lobe of thyroid gland

  • mucosa of transverse colon
Top expressed in
  • spermatocyte

  • fetal liver hematopoietic progenitor cell

  • spermatid

  • motor neuron

  • saccule

  • neural layer of retina

  • otic vesicle

  • otic placode

  • external carotid artery

  • Rostral migratory stream
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • protein homodimerization activity
  • aspartic-type endopeptidase activity
  • peptidase activity
  • protein binding
  • hydrolase activity
  • aspartic endopeptidase activity, intramembrane cleaving
Cellular component
  • integral component of membrane
  • endosome
  • centrosome
  • Golgi apparatus
  • membrane
  • integral component of cytoplasmic side of endoplasmic reticulum membrane
  • Golgi membrane
  • nucleoplasm
  • lysosomal membrane
  • actin cytoskeleton
  • Golgi-associated vesicle membrane
  • lysosome
  • integral component of lumenal side of endoplasmic reticulum membrane
  • endosome membrane
  • plasma membrane
Biological process
  • membrane protein proteolysis
  • proteolysis
  • membrane protein ectodomain proteolysis
  • membrane protein intracellular domain proteolysis
  • regulation of immune response
  • regulation of tumor necrosis factor-mediated signaling pathway
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

56928

73218

Ensembl

ENSG00000005206

ENSMUSG00000035206

UniProt

Q8TCT7

Q3TD49

RefSeq (mRNA)

NM_001077238
NM_152988

NM_175195
NM_001358803
NM_001358804

RefSeq (protein)

NP_001070706
NP_694533

NP_780404
NP_001345732
NP_001345733

Location (UCSC)Chr 19: 2.33 – 2.36 MbChr 10: 80.69 – 80.7 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Signal peptide peptidase-like 2B, also known as SPPL2B, is a human gene.[5]

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). This enzyme localizes to endosomes, lysosomes, and the plasma membrane. 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] Multiple transcript variants encoding different isoforms have been found for this gene.[5]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000005206 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000035206 – 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. ^ a b "Entrez Gene: SPPL2B signal peptide peptidase-like 2B".
  6. ^ Friedmann E, Hauben E, Maylandt K, et al. (2006). "SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 production". Nat. Cell Biol. 8 (8): 843–8. doi:10.1038/ncb1440. PMID 16829952. S2CID 129089.
  7. ^ Fluhrer R, Grammer G, Israel L, et al. (2006). "A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD aspartyl protease SPPL2b". Nat. Cell Biol. 8 (8): 894–6. doi:10.1038/ncb1450. PMID 16829951. S2CID 23712486.
  8. ^ Maccioni, Riccardo; Travisan, Caterina; Badman, Jack; Zerial, Stefania; Wagener, Annika; Andrade-Talavera, Yuniesky; Picciau, Federico; Grassi, Caterina; Chen, Gefei; Lemoine, Laetitia; Fisahn, André; Jiang, Richeng; Fluhrer, Regina; Mentrup, Torben; Schröder, Bernd (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.

Further reading

  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Nagase T, Kikuno R, Ishikawa K, et al. (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 Res. 7 (2): 143–50. doi:10.1093/dnares/7.2.143. PMID 10819331.
  • Weihofen A, Binns K, Lemberg MK, et al. (2002). "Identification of signal peptide peptidase, a presenilin-type aspartic protease". Science. 296 (5576): 2215–8. 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 Mosc. 67 (7): 826–35. doi:10.1023/A:1016365227942. PMID 12139484. S2CID 11785597.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Grimwood J, Gordon LA, Olsen A, et al. (2004). "The DNA sequence and biology of human chromosome 19" (PDF). Nature. 428 (6982): 529–35. Bibcode:2004Natur.428..529G. doi:10.1038/nature02399. PMID 15057824. S2CID 4420825.
  • Friedmann E, Lemberg MK, Weihofen A, et al. (2005). "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. doi:10.1074/jbc.M407898200. hdl:2262/89311. PMID 15385547.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Krawitz P, Haffner C, Fluhrer R, et al. (2006). "Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenilin homologues SPPL2b and SPPL3". J. Biol. Chem. 280 (47): 39515–23. doi:10.1074/jbc.M501645200. PMID 15998642.
  • Fluhrer R, Grammer G, Israel L, et al. (2006). "A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD aspartyl protease SPPL2b" (PDF). Nat. Cell Biol. 8 (8): 894–6. doi:10.1038/ncb1450. PMID 16829951. S2CID 23712486.
  • Friedmann E, Hauben E, Maylandt K, et al. (2006). "SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 production". Nat. Cell Biol. 8 (8): 843–8. doi:10.1038/ncb1440. PMID 16829952. S2CID 129089.


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