Matriptase |
---|
Identifiers |
---|
EC no. | 3.4.21.109 |
---|
CAS no. | 241475-96-7 |
---|
Databases |
---|
IntEnz | IntEnz view |
---|
BRENDA | BRENDA entry |
---|
ExPASy | NiceZyme view |
---|
KEGG | KEGG entry |
---|
MetaCyc | metabolic pathway |
---|
PRIAM | profile |
---|
PDB structures | RCSB PDB PDBe PDBsum |
---|
Search |
---|
PMC | articles |
---|
PubMed | articles |
---|
NCBI | proteins |
---|
|
Peptidase S1A, matripase |
---|
Identifiers |
---|
Symbol | S1A |
---|
InterPro | IPR017051 |
---|
Membranome | 1287 |
---|
Matriptases (EC 3.4.21.109) are an enzyme family.[1][2] 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.
Human matriptases
- ST14, also known as matriptase
- TMPRSS6, also known as matriptase 2
References
- ^ Lee SL, Dickson RB, Lin CY (November 2000). "Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease". The Journal of Biological Chemistry. 275 (47): 36720–5. doi:10.1074/jbc.M007802200. PMID 10962009.
- ^ Lin CY, Anders J, Johnson M, Sang QA, Dickson RB (June 1999). "Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity". The Journal of Biological Chemistry. 274 (26): 18231–6. doi:10.1074/jbc.274.26.18231. PMID 10373424.
External links
|
---|
Activity | |
---|
Regulation | |
---|
Classification | |
---|
Kinetics | |
---|
Types | |
---|
Portal:
Biology