:Matriptase

{{Infobox enzyme

| Name = Matriptase

| EC_number = 3.4.21.109

| CAS_number = 241475-96-7

| GO_code =

| image =

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}}

{{Infobox protein family

| Symbol = S1A

| Name = Peptidase S1A, matripase

| image =

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| Pfam=

| InterPro= IPR017051

| SMART=

| Prosite =

| SCOP =

| TCDB =

| OPM family=

| OPM protein=

| PDB=

| Membranome family = 1287

}}

Matriptases ({{EC number|3.4.21.109}}) are an enzyme family.{{cite journal | vauthors = Lee SL, Dickson RB, Lin CY | title = Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease | journal = The Journal of Biological Chemistry | volume = 275 | issue = 47 | pages = 36720–5 | date = November 2000 | pmid = 10962009 | doi = 10.1074/jbc.M007802200 | doi-access = free }}{{cite journal | vauthors = Lin CY, Anders J, Johnson M, Sang QA, Dickson RB | title = Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity | journal = The Journal of Biological Chemistry | volume = 274 | issue = 26 | pages = 18231–6 | date = June 1999 | pmid = 10373424 | doi = 10.1074/jbc.274.26.18231 | doi-access = free }} This enzyme 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

This trypsin-like integral-membrane serine peptidase has been implicated in breast cancer invasion and metastasis. It belongs to proteases of PA superfamily.