ID   CMA1_CAVPO              Reviewed;         247 AA.
AC   A7WPL7; P85201;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Chymase;
DE            EC=3.4.21.39;
DE   AltName: Full=Alpha-chymase;
DE   Flags: Precursor;
GN   Name=CMA1 {ECO:0000312|EMBL:CAO99144.1};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1] {ECO:0000312|EMBL:CAO99144.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart {ECO:0000312|EMBL:CAO99144.1};
RA   Beauchamp J.C., Caughey G.H., Fingerle J., Schliemann K.;
RT   "Guinea pig chymase is leucine-specific: a novel example of functional
RT   plasticity in the chymase/granzyme family of immune cell serine
RT   peptidases.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 22-247.
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   EMBL; AM851020; CAO99144.1; -; mRNA.
DR   RefSeq; NP_001166403.1; NM_001172932.1.
DR   AlphaFoldDB; A7WPL7; -.
DR   SMR; A7WPL7; -.
DR   STRING; 10141.ENSCPOP00000011161; -.
DR   MEROPS; S01.140; -.
DR   GeneID; 100135503; -.
DR   KEGG; cpoc:100135503; -.
DR   CTD; 1215; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   InParanoid; A7WPL7; -.
DR   OrthoDB; 1076876at2759; -.
DR   BRENDA; 3.4.21.39; 1225.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
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   InterPro; IPR033116; TRYPSIN_SER.
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.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Protease; Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..21
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:17981788"
FT                   /id="PRO_0000312843"
FT   CHAIN           22..247
FT                   /note="Chymase"
FT                   /evidence="ECO:0000269|PubMed:17981788"
FT                   /id="PRO_5000271615"
FT   DOMAIN          22..245
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        66
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P23946"
FT   ACT_SITE        110
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P23946"
FT   ACT_SITE        203
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P23946"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        51..67
FT                   /evidence="ECO:0000250|UniProtKB:P23946,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        144..209
FT                   /evidence="ECO:0000250|UniProtKB:P23946,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        175..188
FT                   /evidence="ECO:0000250|UniProtKB:P23946,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        52
FT                   /note="G -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   247 AA;  27666 MW;  988E69EBAD6AF589 CRC64;
     MCLLSLPLLL FLQYTRAKAG EVIGGTECKP HSRPYMAYLE IVSSEGYEKD CGGFLIRRNF
     VLTAAHCAGR SLTVNLGVHN KKMKEDTWQR LKVIKQFLHP NYNSSVLLHD IMLLKLEKKA
     NLTLAVGTLP LPPECNFLTS GRMCRAAGWG RTNVEEPASD TLQEVKLRLM DPQACKHFPN
     FNHNLQLCVG NPRKRKSVFK GDSGGPLLCA GIAQGIVSYA HRNAKPPVVF TRISHYRPWI
     NKILKAN