ID   CMA1_RABIT              Reviewed;         220 AA.
AC   P85202;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Chymase;
DE            EC=3.4.21.39;
DE   AltName: Full=Alpha-chymase;
GN   Name=CMA1 {ECO:0000250|UniProtKB:P23946};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RX   PubMed=17981788; DOI=10.1074/jbc.m707157200;
RA   Kervinen J., Abad M., Crysler C., Kolpak M., Mahan A.D., Masucci J.A.,
RA   Bayoumy S., Cummings M.D., Yao X., Olson M., de Garavilla L., Kuo L.,
RA   Deckman I., Spurlino J.;
RT   "Structural basis for elastolytic substrate specificity in rodent alpha-
RT   chymases.";
RL   J. Biol. Chem. 283:427-436(2008).
CC   -!- FUNCTION: Major secreted protease of mast cells with suspected roles in
CC       vasoactive peptide generation, extracellular matrix degradation, and
CC       regulation of gland secretion. {ECO:0000250|UniProtKB:P23946}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Phe-|-Xaa > Tyr-|-Xaa > Trp-|-Xaa >
CC         Leu-|-Xaa.; EC=3.4.21.39; Evidence={ECO:0000250|UniProtKB:P23946};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P23946}.
CC       Cytoplasmic granule {ECO:0000250|UniProtKB:P23946}. Note=Mast cell
CC       granules. {ECO:0000250|UniProtKB:P23946}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   AlphaFoldDB; P85202; -.
DR   SMR; P85202; -.
DR   STRING; 9986.ENSOCUP00000020875; -.
DR   PRIDE; P85202; -.
DR   InParanoid; P85202; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Protease; Reference proteome; Secreted; Serine protease.
FT   CHAIN           1..220
FT                   /note="Chymase"
FT                   /id="PRO_0000312844"
FT   DOMAIN          2..218
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        46
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P23946"
FT   ACT_SITE        90
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P23946"
FT   ACT_SITE        177
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P23946"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..47
FT                   /evidence="ECO:0000250|UniProtKB:P23946,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        124..182
FT                   /evidence="ECO:0000250|UniProtKB:P23946,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        155..168
FT                   /evidence="ECO:0000250|UniProtKB:P23946,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   220 AA;  24710 MW;  D6E7B8C87D57156E CRC64;
     EIIGGTESKP HSRPYMAHLK IITKQGTFAY CGGFLISREF VMTAAHCKGR HITVTLGAHD
     VVKKESTWQK IDVVKQFVHP NYNSYTIRHD VMLLKLKEKA NLTLTVGTLP LLPQSNFIPP
     GRMCRAVGWG KTSVKESHSN VLQEVKLRLL DPPACQHFPD FNHNLQLCMG TVFKGDSGPL
     LCARVAQGIA SYAHKNAMPP SVFTRISYYR PWINKVLKEN