Reaction: Cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position
Other name(s): serine protease 14; membrane-type serine protease 1; MT-SP1; prostamin; serine protease TADG-15; tumor-associated differentially-expressed gene 15 protein; ST14; breast cancer 80 kDa protease; epithin; serine endopeptidase SNC19; matriptase-1; matriptase-2; matriptase-3; TMPRSS6 (gene name)
Comments: This trypsin-like integral-membrane serine peptidase has been implicated in breast cancer invasion and metastasis [1,2]. The enzyme can activate hepatocyte growth factor/scattering factor (HGF/SF) by cleavage of the two-chain forms at an Arg residue to give active α- and β-HGF, but It does not activate plasminogen, which shares high homology with HGF [1]. The enzyme can also activate urokinase plasminogen activator (uPA), which initiates the matrix-degrading peptidase cascade [1,2]. Hemojuvelin has been shown to be a physiological substrate for matriptase-2 [5]. Belongs in peptidase family S1A.
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, MetaCyc, PDB, CAS registry number: 241475-96-7
References:
1. Lee, S.L., Dickson, R.B. and Lin, C.Y. Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease. J. Biol. Chem. 275 (2000) 36720-36725. [PMID: 10962009]
2. Lin, C.Y., Anders, J., Johnson, M., Sang, Q.A. and Dickson, R.B. Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity. J. Biol. Chem. 274 (1999) 18231-18236. [PMID: 10373424]
3. Ramsay, A.J., Reid, J.C., Velasco, G., Quigley, J.P. and Hooper, J.D. The type II transmembrane serine protease matriptase-2 – identification, structural features, enzymology, expression pattern and potential roles. Front. Biosci. 13 (2008) 569-579. [PMID: 17981570]
4. Kojima, K., Tsuzuki, S., Fushiki, T. and Inouye, K. The activity of a type II transmembrane serine protease, matriptase, is dependent solely on the catalytic domain. Biosci. Biotechnol. Biochem. 73 (2009) 454-456. [PMID: 19202271]
5. Wysocka, M., Gruba, N., Miecznikowska, A., Popow-Stellmaszyk, J., Gutschow, M., Stirnberg, M., Furtmann, N., Bajorath, J., Lesner, A. and Rolka, K. Substrate specificity of human matriptase-2. Biochimie 97 (2014) 121-127. [PMID: 24161741]