HM13

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Histocompatibility (minor) 13
Identifiers
Symbols HM13 ; IMP1; H13; IMPAS; MSTP086; PSENL3; PSL3; SPP; dJ324O17.1
External IDs Template:OMIM5 Template:MGI HomoloGene: 7749
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Histocompatibility (minor) 13, also known as HM13, is a human gene.[1]

The protein encoded by this gene, which localizes to the endoplasmic reticulum, catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein. This activity is required to generate signal sequence-derived human lymphocyte antigen-E epitopes that are recognized by the immune system, and to process hepatitis C virus core protein. The encoded protein is an integral membrane protein with sequence motifs characteristic of the presenilin-type aspartic proteases. Multiple transcript variants encoding several different isoforms have been found for this gene.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: HM13 histocompatibility (minor) 13".

Further reading

  • Lemberg MK, Bland FA, Weihofen A; et al. (2002). "Intramembrane proteolysis of signal peptides: an essential step in the generation of HLA-E epitopes". J. Immunol. 167 (11): 6441–6. PMID 11714810.
  • Deloukas P, Matthews LH, Ashurst J; et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
  • Weihofen A, Binns K, Lemberg MK; et al. (2002). "Identification of signal peptide peptidase, a presenilin-type aspartic protease". Science. 296 (5576): 2215–8. doi:10.1126/science.1070925. PMID 12077416.
  • 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. PMID 12139484.
  • McLauchlan J, Lemberg MK, Hope G, Martoglio B (2002). "Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets". EMBO J. 21 (15): 3980–8. doi:10.1093/emboj/cdf414. PMID 12145199.
  • Lemberg MK, Martoglio B (2002). "Requirements for signal peptide peptidase-catalyzed intramembrane proteolysis". Mol. Cell. 10 (4): 735–44. PMID 12419218.
  • 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. doi:10.1073/pnas.242603899. PMID 12477932.
  • Urny J, Hermans-Borgmeyer I, Gercken G, Schaller HC (2004). "Expression of the presenilin-like signal peptide peptidase (SPP) in mouse adult brain and during development". Gene Expr. Patterns. 3 (5): 685–91. PMID 12972007.
  • Lehner B, Semple JI, Brown SE; et al. (2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics. 83 (1): 153–67. PMID 14667819.
  • Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Nyborg AC, Kornilova AY, Jansen K; et al. (2004). "Signal peptide peptidase forms a homodimer that is labeled by an active site-directed gamma-secretase inhibitor". J. Biol. Chem. 279 (15): 15153–60. doi:10.1074/jbc.M309305200. PMID 14704149.
  • Moliaka YK, Grigorenko A, Madera D, Rogaev EI (2004). "Impas 1 possesses endoproteolytic activity against multipass membrane protein substrate cleaving the presenilin 1 holoprotein". FEBS Lett. 557 (1–3): 185–92. PMID 14741365.
  • Soares MR, Bisch PM, Campos de Carvalho AC; et al. (2004). "Correlation between conformation and antibody binding: NMR structure of cross-reactive peptides from T. cruzi, human and L. braziliensis". FEBS Lett. 560 (1–3): 134–40. doi:10.1016/S0014-5793(04)00088-2. PMID 14988012.
  • 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. 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. PMID 15489334.
  • Otsuki T, Ota T, Nishikawa T; et al. (2007). "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. doi:10.1093/dnares/12.2.117. PMID 16303743.
  • Urny J, Hermans-Borgmeyer I, Schaller HC (2006). "Cell-surface expression of a new splice variant of the mouse signal peptide peptidase". Biochim. Biophys. Acta. 1759 (3–4): 159–65. doi:10.1016/j.bbaexp.2006.02.007. PMID 16730383.
  • Loureiro J, Lilley BN, Spooner E; et al. (2006). "Signal peptide peptidase is required for dislocation from the endoplasmic reticulum". Nature. 441 (7095): 894–7. doi:10.1038/nature04830. PMID 16738546.
  • Sato T, Nyborg AC, Iwata N; et al. (2006). "Signal peptide peptidase: biochemical properties and modulation by nonsteroidal antiinflammatory drugs". Biochemistry. 45 (28): 8649–56. doi:10.1021/bi060597g. PMID 16834339.

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