DEFA5

From Wikipedia, the free encyclopedia


Defensin, alpha 5, Paneth cell-specific
PDB rendering based on 1zmp.
Available structures: 1zmp
Identifiers
Symbol(s) DEFA5; DEF5; HD-5; MGC129728
External IDs OMIM: 600472 HomoloGene88502
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 1670 n/a
Ensembl ENSG00000164816 n/a
Uniprot Q01523 n/a
Refseq NM_021010 (mRNA)
NP_066290 (protein)
n/a (mRNA)
n/a (protein)
Location Chr 8: 6.9 - 6.9 Mb n/a
Pubmed search [1] n/a

Defensin, alpha 5, Paneth cell-specific, also known as DEFA5, is a human gene.[1]

Defensins are a family of microbicidal and cytotoxic peptides thought to be involved in host defense. They are abundant in the granules of neutrophils and also found in the epithelia of mucosal surfaces such as those of the intestine, respiratory tract, urinary tract, and vagina. Members of the defensin family are highly similar in protein sequence and distinguished by a conserved cysteine motif. Several of the alpha defensin genes appear to be clustered on chromosome 8. The protein encoded by this gene, defensin, alpha 5, is highly expressed in the secretory granules of Paneth cells of the ileum.[1]

[edit] References

[edit] Further reading

  • Jones DE, Bevins CL (1992). "Paneth cells of the human small intestine express an antimicrobial peptide gene.". J. Biol. Chem. 267 (32): 23216–25. PMID 1429669. 
  • Mallow EB, Harris A, Salzman N, et al. (1996). "Human enteric defensins. Gene structure and developmental expression.". J. Biol. Chem. 271 (8): 4038–45. PMID 8626737. 
  • Bevins CL, Jones DE, Dutra A, et al. (1996). "Human enteric defensin genes: chromosomal map position and a model for possible evolutionary relationships.". Genomics 31 (1): 95–106. doi:10.1006/geno.1996.0014. PMID 8808285. 
  • Porter EM, Liu L, Oren A, et al. (1997). "Localization of human intestinal defensin 5 in Paneth cell granules.". Infect. Immun. 65 (6): 2389–95. PMID 9169779. 
  • Quayle AJ, Porter EM, Nussbaum AA, et al. (1998). "Gene expression, immunolocalization, and secretion of human defensin-5 in human female reproductive tract.". Am. J. Pathol. 152 (5): 1247–58. PMID 9588893. 
  • Ghosh D, Porter E, Shen B, et al. (2002). "Paneth cell trypsin is the processing enzyme for human defensin-5.". Nat. Immunol. 3 (6): 583–90. doi:10.1038/ni797. PMID 12021776. 
  • 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. 
  • Salzman NH, Ghosh D, Huttner KM, et al. (2003). "Protection against enteric salmonellosis in transgenic mice expressing a human intestinal defensin.". Nature 422 (6931): 522–6. doi:10.1038/nature01520. PMID 12660734. 
  • 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. 
  • Szyk A, Wu Z, Tucker K, et al. (2007). "Crystal structures of human alpha-defensins HNP4, HD5, and HD6.". Protein Sci. 15 (12): 2749–60. doi:10.1110/ps.062336606. PMID 17088326. 
  • de Leeuw E, Burks SR, Li X, et al. (2007). "Structure-dependent functional properties of human defensin 5.". FEBS Lett. 581 (3): 515–20. doi:10.1016/j.febslet.2006.12.036. PMID 17250830.