EC - Hepsin

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IntEnz Enzyme Nomenclature


Accepted name:
Systematic name:



This type-II membrane-associated serine peptidase has been implicated in cell growth and development [1,3]. The enzyme has been shown to activate blood coagulation factor VII by cleavage of the Arg152┼Ile153 peptide bound in BHK cells, thus indicating a possible role in the initiation of blood coagulation [2]. There is no cleavage after aromatic or aliphatic residues [1]. The occupancy of the S2 site is an absolute requirement for catalysis and a basic residue at that site is preferred to an aliphatic residue. The nature of the residue at S3 also affects hydrolysis, with Gln being much more favourable than Ala [1]. Belongs in peptidase family S1A.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Protein domains and families: PROSITE:PDOC00124
Structural data: CSA , EC2PDB


  1. Zhukov, A., Hellman, U. and Ingelman-Sundberg, M.
    Purification and characterization of hepsin from rat liver microsomes.
    Biochim. Biophys. Acta 1337: 85-95 (1997). [PMID: 9003440]
  2. Kazama, Y., Hamamoto, T., Foster, D.C. and Kisiel, W.
    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.
    J. Biol. Chem. 270: 66-72 (1995). [PMID: 7814421]
  3. Torres-Rosado, A., O'Shea, K.S., Tsuji, A., Chou, S.-H. and Kurachi, K.
    Hepsin, a putative cell-surface serine protease, is required for mammalian cell growth.
    Proc. Natl. Acad. Sci. USA 90: 7181-7185 (1993). [PMID: 8346233]

[EC created 2006]