Serine protease hepsin is an enzyme that in humans is encoded by the HPN gene.[5][6]

Function

Hepsin is a cell surface serine protease.[6]

Hepson contains a peptidase S1 domain and an SRCR domain. The SRCR domain is located in the extracellular part of the protein, it is formed primarily by three elements of regular secondary structure: a 12-residue alpha helix, a twisted five-stranded antiparallel beta sheet, and a second, two-stranded, antiparallel sheet. The two beta-sheets lie at roughly right angles to each other, with the helix nestled between the two, adopting an SRCR fold. The exact function of this domain has not been identified, though it probably may serve to orient the protease domain or place it in the vicinity of its substrate.[7]

Clinical significance

Hepsin expression is unregulated in prostate cancer and correlates with disease progression.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000105707Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000001249Ensembl, 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. ^ Leytus SP, Loeb KR, Hagen FS, Kurachi K, Davie EW (Feb 1988). "A novel trypsin-like serine protease (hepsin) with a putative transmembrane domain expressed by human liver and hepatoma cells". Biochemistry. 27 (3): 1067–74. doi:10.1021/bi00403a032. PMID 2835076.
  6. ^ a b "Entrez Gene: HPN hepsin (transmembrane protease, serine 1)".
  7. ^ Somoza JR, Ho JD, Luong C, Ghate M, Sprengeler PA, Mortara K, Shrader WD, Sperandio D, Chan H, McGrath ME, Katz BA (Sep 2003). "The structure of the extracellular region of human hepsin reveals a serine protease domain and a novel scavenger receptor cysteine-rich (SRCR) domain". Structure. 11 (9): 1123–31. doi:10.1016/S0969-2126(03)00148-5. PMID 12962630.
  8. ^ Wu Q, Parry G (2007). "Hepsin and prostate cancer". Frontiers in Bioscience. 12 (12): 5052–9. doi:10.2741/2447. PMID 17569629.

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR015352
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