HM13

From Wikipedia, the free encyclopedia


Histocompatibility (minor) 13
Identifiers
Symbol(s) HM13; IMP1; H13; IMPAS; MSTP086; PSENL3; PSL3; SPP; dJ324O17.1
External IDs OMIM: 607106 MGI95886 HomoloGene7749
Orthologs
Human Mouse
Entrez 81502 14950
Ensembl ENSG00000101294 ENSMUSG00000019188
Uniprot Q8TCT9 Q3TXP0
Refseq NM_030789 (mRNA)
NP_110416 (protein)
NM_010376 (mRNA)
NP_034506 (protein)
Location Chr 20: 29.57 - 29.62 Mb Chr 2: 152.36 - 152.4 Mb
Pubmed search [1] [2]

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]

[edit] References

[edit] 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.