ID   CMA1_MACFA              Reviewed;         247 AA.
AC   P56435;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Chymase;
DE            EC=3.4.21.39;
DE   AltName: Full=Alpha-chymase;
DE   Flags: Precursor;
GN   Name=CMA1;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9257695; DOI=10.1016/s0014-5793(97)00752-7;
RA   Takai S., Shiota N., Kobayashi S., Matsumura E., Miyazaki M.;
RT   "Induction of chymase that forms angiotensin II in the monkey
RT   atherosclerotic aorta.";
RL   FEBS Lett. 412:86-90(1997).
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}.
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 {ECO:0000250}. Cytoplasmic granule
CC       {ECO:0000250}. Note=Mast cell granules. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; AB000823; BAA22070.1; -; mRNA.
DR   RefSeq; NP_001272121.1; NM_001285192.1.
DR   AlphaFoldDB; P56435; -.
DR   SMR; P56435; -.
DR   STRING; 9541.XP_005561049.1; -.
DR   MEROPS; S01.140; -.
DR   PRIDE; P56435; -.
DR   GeneID; 102128612; -.
DR   CTD; 1215; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   OrthoDB; 1076876at2759; -.
DR   Proteomes; UP000233100; 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; 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; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   PROPEP          20..21
FT                   /note="Activation peptide"
FT                   /id="PRO_0000027435"
FT   CHAIN           22..247
FT                   /note="Chymase"
FT                   /id="PRO_0000027436"
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;  27400 MW;  6D049B34377FC8B9 CRC64;
     MLLLPLPLLL FFLCSRAEAG EIIGGTECKP HSRPYMAYLE IVTSNGPSKS CGGFLIRRNF
     VLTAVHCAGR SITVTLGAHN ITEKEDTWQK LEVIKQFRHP KYNTSTLHHD IMLLKLKEKA
     SLTLAVGTLP FPSQFNFVPP GRMCRVAGWG RTGVLKPGSD TLQEVKLRLM DPQACSHFRY
     FDHNLQLCVG NPRKTKSAFK GDSGGPLLCA GVAQGIVSYG RLDAKPPAVF TRISHYRPWI
     NKILQAN