ID   MCPT2_MERUN             Reviewed;         247 AA.
AC   P50341;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Mast cell protease 2;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
OS   Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Gerbillinae; Meriones.
OX   NCBI_TaxID=10047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=MGS/SEA; TISSUE=Intestine;
RX   PubMed=8615790; DOI=10.1042/bj3140923;
RA   Itoh H., Murakumo Y., Tomita M., Ide H., Kobayashi T., Maruyama H.,
RA   Horii Y., Nawa Y.;
RT   "Cloning of the cDNAs for mast-cell chymases from the jejunum of Mongolian
RT   gerbils, Meriones unguiculatus, and their sequence similarities with
RT   chymases expressed in the connective-tissue mast cells of mice and rats.";
RL   Biochem. J. 314:923-929(1996).
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; D45174; BAA08122.1; -; mRNA.
DR   PIR; S64708; S64708.
DR   AlphaFoldDB; P50341; -.
DR   SMR; P50341; -.
DR   MEROPS; S01.150; -.
DR   PRIDE; P50341; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; Serine protease; Signal;
KW   Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..21
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000027465"
FT   CHAIN           22..247
FT                   /note="Mast cell protease 2"
FT                   /id="PRO_0000027466"
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   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;  27633 MW;  CA737B5CD43FBE30 CRC64;
     MHLLALHLLL FLLGSRAKAG EIIGGTECKP HSRPYMAYLE IATSKNYLST CSGFLIRRNF
     VLTAAHCSGR SITVLLGAHN KTAKEDTWQK IEVEKQFPHP KYDDYSVLHD IMLLKLKEKA
     KLTLAVGTLP LPAKFSFIPP GRVCRAVGWG KTNVNEPTSD TLQEVKMRLL EAEGCKHFTN
     FYHSSQLCVG NPKKMQNVYK GDSGGPLLCA GIAQGIASYV RRNARPPAVF TRISHYRPWI
     NKILREN