Biology:HPN (gene)

Short description: Protein-coding gene in humans

Hepsin-SRCR
extracellular domain of human hepsin
Identifiers
Symbol	Hepsin-SRCR
Pfam	PF09272
InterPro	IPR015352
SCOP2	1p57 / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Generic protein structure example

Serine protease hepsin is an enzyme that in humans is encoded by the HPN gene.

Function

Hepsin is a cell surface serine protease.

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.

Clinical significance

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

Further reading

• "Gene targeting in hemostasis. Hepsin". Frontiers in Bioscience 6 (3): D192-200. Feb 2001. doi:10.2741/a604. PMID 11171558. 
• "Hepsin, a cell membrane-associated protease. Characterization, tissue distribution, and gene localization". The Journal of Biological Chemistry 266 (25): 16948–53. Sep 1991. doi:10.1016/S0021-9258(18)55395-3. PMID 1885621. 
• "Hepsin, a putative membrane-associated serine protease, activates human factor VII and initiates a pathway of blood coagulation on the cell surface leading to thrombin formation". The Journal of Biological Chemistry 270 (1): 66–72. Jan 1995. doi:10.1074/jbc.270.1.66. PMID 7814421. 
• "Hepsin, a putative cell-surface serine protease, is required for mammalian cell growth". Proceedings of the National Academy of Sciences of the United States of America 90 (15): 7181–5. Aug 1993. doi:10.1073/pnas.90.15.7181. PMID 8346233. Bibcode: 1993PNAS...90.7181T. 
• "Hepsin and maspin are inversely expressed in laser capture microdissectioned prostate cancer". The Journal of Urology 169 (4): 1316–9. Apr 2003. doi:10.1097/01.ju.0000050648.40164.0d. PMID 12629351. 
• "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. Sep 2003. doi:10.1016/S0969-2126(03)00148-5. PMID 12962630. 
• "Hepsin activates pro-hepatocyte growth factor and is inhibited by hepatocyte growth factor activator inhibitor-1B (HAI-1B) and HAI-2". FEBS Letters 579 (9): 1945–50. Mar 2005. doi:10.1016/j.febslet.2005.01.085. PMID 15792801. 
• "Variants in the HEPSIN gene are associated with prostate cancer in men of European origin". Human Genetics 120 (2): 187–92. Sep 2006. doi:10.1007/s00439-006-0204-3. PMID 16783571. 
• "Pro-urokinase-type plasminogen activator is a substrate for hepsin". The Journal of Biological Chemistry 281 (41): 30439–46. Oct 2006. doi:10.1074/jbc.M605440200. PMID 16908524. 
• "Clinical relevance of hepsin and hepatocyte growth factor activator inhibitor type 2 expression in renal cell carcinoma". Cancer Science 98 (4): 491–8. Apr 2007. doi:10.1111/j.1349-7006.2007.00412.x. PMID 17309599. 

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