MCP4 (MCPT4) Active Protein

Function: Has chymotrypsin-like activity. Hydrolyzes the amide bonds of synthetic substrates having Tyr and Phe residues at the P1 position. Preferentially hydrolyzes the 'Tyr-4-|-Ile-5' bond of angiotensin I and the 'Phe-20-|-Ala-21' bond of amyloid beta-protein, and is less active towards the 'Phe-8-|-His-9' bond of angiotensin I and the 'Phe-4-|-Ala-5' and 'Tyr-10-|-Glu-11' bonds of amyloid beta-protein. Involved in thrombin regulation and fibronectin processing. Ref.4 Ref.7

Enzyme regulation: Completely inhibited by serine protease inhibitors such as chymostatin, diisopropylfluorophosphate and phenylmethylsulfonyl fluoride, but not by p-tosyl-L-phenylalanine chloromethyl ketone, p-tosyl-L-lysine chloromethyl ketone, pepstatin, E-64, EDTA or o-phenanthroline. Also inhibited by lima bean trypsin inhibitor, soy bean trypsin inhibitor and human plasma alpha1-antichymotrysin.

Subunit structure: Monomer. Ref.4

Tissue specificity: Submucosal mast cells. In femoral muscle, detected in myocytes but not in mast cells. Ref.4

Disruption phenotype: Mice display an impaired ability to inactivate thrombin or degrade fibronectin in peritoneal cells. Ref.7

Sequence similarities: Belongs to the peptidase S1 family. Granzyme subfamily.Contains 1 peptidase S1 domain.

Biophysicochemical propertiespH dependence:Optimum pH is 9 at high salt concentrations.

Mass spectrometry: Molecular mass is 25187 Da from positions 21 - 246. Determined by MALDI. Ref.4

Sequence caution: The sequence BAB18732.1 differs from that shown. Reason: Erroneous initiation.