ID   MCPT9_MOUSE             Reviewed;         246 AA.
AC   O35164;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Mast cell protease 9;
DE            Short=mMCP-9;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=Mcpt9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=BALB/cJ;
RX   PubMed=9360993; DOI=10.1074/jbc.272.46.29158;
RA   Hunt J.E., Friend D.S., Gurish M.F., Feyfant E., Sali A., Huang C.,
RA   Ghildyal N., Stechschulte S., Austen K.F., Stevens R.L.;
RT   "Mouse mast cell protease 9, a novel member of the chromosome 14 family of
RT   serine proteases that is selectively expressed in uterine mast cells.";
RL   J. Biol. Chem. 272:29158-29166(1997).
CC   -!- TISSUE SPECIFICITY: Selectively expressed in uterine mast cells.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; AF007119; AAB65245.1; -; Genomic_DNA.
DR   EMBL; AF007120; AAB65246.1; -; mRNA.
DR   CCDS; CCDS27138.1; -.
DR   RefSeq; NP_034912.3; NM_010782.3.
DR   AlphaFoldDB; O35164; -.
DR   SMR; O35164; -.
DR   BioGRID; 201361; 1.
DR   STRING; 10090.ENSMUSP00000093476; -.
DR   BindingDB; O35164; -.
DR   ChEMBL; CHEMBL2132; -.
DR   MEROPS; S01.304; -.
DR   PaxDb; 10090-ENSMUSP00000093476; -.
DR   DNASU; 17232; -.
DR   Ensembl; ENSMUST00000095798.2; ENSMUSP00000093476.2; ENSMUSG00000071361.2.
DR   GeneID; 17232; -.
DR   KEGG; mmu:17232; -.
DR   UCSC; uc007ubj.1; mouse.
DR   AGR; MGI:1194491; -.
DR   CTD; 17232; -.
DR   MGI; MGI:1194491; Mcpt9.
DR   VEuPathDB; HostDB:ENSMUSG00000071361; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT01030000234551; -.
DR   HOGENOM; CLU_006842_1_0_1; -.
DR   InParanoid; O35164; -.
DR   OMA; QECESRY; -.
DR   OrthoDB; 4821689at2759; -.
DR   PhylomeDB; O35164; -.
DR   TreeFam; TF333630; -.
DR   BioGRID-ORCS; 17232; 2 hits in 44 CRISPR screens.
DR   PRO; PR:O35164; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; O35164; Protein.
DR   Bgee; ENSMUSG00000071361; Expressed in colon.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0008201; F:heparin binding; ISO:MGI.
DR   GO; GO:0042277; F:peptide binding; ISO:MGI.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR   GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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   PANTHER; PTHR24271:SF23; CHYMASE 2, MAST CELL-RELATED; 1.
DR   PANTHER; PTHR24271; KALLIKREIN-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
DR   Genevisible; O35164; MM.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hydrolase; Protease; Reference proteome; Serine protease;
KW   Signal; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   PROPEP          19..20
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000027459"
FT   CHAIN           21..246
FT                   /note="Mast cell protease 9"
FT                   /id="PRO_0000027460"
FT   DOMAIN          21..244
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        65
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        109
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        202
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        143..208
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        174..187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   246 AA;  26652 MW;  C3EEFC5D7B51DD01 CRC64;
     MQALLFLMAL LLPSRAGAEE IIGGVESEPH SRPYMAYVNT FSKKGYVAIC GGFLIAPQFV
     MTAAHCSGRR MTVTLGAHNV RKRECTQQKI KVEKYILPPN YNVSSKFNDI VLLKLKKQAN
     LTSAVDVVPL PGPSDFAKPG TMCWAAGWGR TGVKKSISHT LREVELKIVG EKACKIFRHY
     KDSLQICVGS STKVASVYMG DSGGPLLCAG VAHGIVSSGR GNAKPPAIFT RISPHVPWIN
     RVIKGE
//