ID   CMA1_PAPHA              Reviewed;         247 AA.
AC   P52195;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Chymase;
DE            EC=3.4.21.39;
DE   AltName: Full=Alpha-chymase;
DE   AltName: Full=Mast cell chymase;
DE   Flags: Precursor;
GN   Name=CMA1; Synonyms=CHM;
OS   Papio hamadryas (Hamadryas baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA   Liao Y., Karnik S., Husain A.;
RL   Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
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.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Phe-|-Xaa > Tyr-|-Xaa > Trp-|-Xaa >
CC         Leu-|-Xaa.; EC=3.4.21.39;
CC   -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. Note=Mast cell
CC       granules.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; U38521; AAA91160.1; -; mRNA.
DR   EMBL; U38463; AAA91159.1; -; Genomic_DNA.
DR   AlphaFoldDB; P52195; -.
DR   SMR; P52195; -.
DR   MEROPS; S01.140; -.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   PROPEP          20..21
FT                   /note="Activation peptide"
FT                   /id="PRO_0000027437"
FT   CHAIN           22..247
FT                   /note="Chymase"
FT                   /id="PRO_0000027438"
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"
FT   ACT_SITE        110
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        203
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        51..67
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        144..209
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        175..188
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   247 AA;  27339 MW;  E0EC15E0FA72FD8B CRC64;
     MLLLPLPLLL LFLCSRAEAG EIIGGTECKP HSRPYMAYLE IVTSNGPSKS CGGFLIRRNF
     VLTAAHCAGR SITVTLGAHN ITEKEDTWQE LEVIKQFRHP KYNTSTLHHD IMLLKLKEKA
     SLTLAVGTLP FPSQFNFVPP GRMCRVAGWG RTGVLKPGSD TLQEVKLRLM DPQACSHFRY
     FDHNLQLCVG NPRKTKSAFK GDSGGPLLCA GVAQGIVSYG RLDAKPPAVF TRISHYRPWI
     NKILQAN