Summary for peptidase S01.140: chymase (Homo sapiens-type)

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Structure Literature Human EST Substrates Inhibitors Pharma

 

Names
MEROPS Namechymase (Homo sapiens-type)
Other namesalpha-chymase, chymase I, CMA1 g.p. (Homo sapiens), mast cell protease 3 (Mus musculus), mMCP-3, skeletal muscle protease, skin chymotryptic proteinase, mouse chymase 3, chymase 3 (Mus musculus)
Domain architecture
MEROPS Classification
Classification Clan PA >> Subclan PA(S) >> Family S1 >> Subfamily A >> S01.140
Holotypechymase (Homo sapiens-type), Uniprot accession P23946 (peptidase unit: 22-247), MERNUM MER0000123
History Identifier created: Handbook of Proteolytic Enzymes (1998) Academic Press, London.
Activity
Catalytic typeSerine
PeplistIncluded in the Peplist with identifier PL00275
NC-IUBMBSubclass 3.4 (Peptidases) >> Sub-subclass 3.4.21 (Serine endopeptidases) >> Peptidase 3.4.21.39
EnzymologyBRENDA database
Proteolytic eventsCutDB database (23 cleavages)
Activity statushuman: active (Caughey, 2004)
mouse: active (Springman & Serafin, 1995)
PhysiologyHydrolyses extracellular matrix proteins and others after release from mast cells. Second to peptidyl-dipeptidase A, the major angiotensin II-forming enzyme (Caughey et al., 2000; Muilenburg et al., 2002). Polymorphism rs1800875 in the promoter region of the human CMA1 gene is significantly associated with atopic eczema (Weidinger et al., 2005).
Pharmaceutical relevancePossible drug target in immune-related diseases of lung. Also, there is an indication that an inhibitor can reduce post-operative adhesions (Okamoto et al., 2002). An inhibitor is reported to prevent the development of intimal hyperplasia in balloon-injured arteries (Takai et al., 2003). Results obtained in a dog model have led to the suggestion that chronic inhibition of chymase can prevent cardiac remodelling in heart failure (Matsumoto et al., 2003). The therapeutic potential of chymase inhibitors has been reviewed by Doggrell & Wanstall (2004). Takai et al., 2004 propose that chymase is also a novel target for preventing vascular diseases.
Pathways KEGGRenin-angiotensin system
Other databases TREEFAMhttp://www.treefam.org/family/TF333630
Cleavage site specificity Explanations of how to interpret the following cleavage site sequence logo and specificity matrix can be found here.
Cleavage pattern-/-/-/FYScissile bond-/edl/-/- (based on 106 cleavages)
weblogo
Specificity matrix
 
Amino acid P4 P3 P2 P1 P1' P2' P3' P4'
Gly 13 5 1 1 12 8 11 7
Pro 4 1 14 0 1 0 9 5
Ala 5 14 11 1 10 6 10 6
Val 14 18 16 0 8 4 11 8
Leu 13 7 11 8 1 17 6 10
Ile 7 4 2 0 4 0 1 2
Met 1 5 2 0 3 2 2 3
Phe 3 3 6 46 6 2 3 3
Tyr 0 0 0 43 2 1 2 0
Trp 4 1 2 7 1 1 0 2
Ser 6 13 10 0 18 10 13 10
Thr 6 4 10 0 8 2 7 7
Cys 2 2 1 0 2 0 0 0
Asn 2 1 3 0 3 2 2 4
Gln 5 8 6 0 4 3 2 0
Asp 1 3 0 0 3 17 3 3
Glu 1 7 2 0 8 21 5 6
Lys 4 3 2 0 2 0 0 0
Arg 9 2 3 0 3 0 2 5
His 0 1 0 0 1 3 8 15
Human genetics
Gene symbol Locus Megabases Ensembl Entrez gene Gene Cards OMIM
CMA1 14q11.2 ENSG00000092009 1215 CMA1 118938
Mouse genetics
Gene symbol Position Megabases Ensembl Entrez gene MGI
Mcpt3 104207 MGI:96939