MCPT1_MOUSE
ID MCPT1_MOUSE Reviewed; 246 AA.
AC P11034;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Mast cell protease 1;
DE Short=mMCP-1;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=Mcpt1;
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.
RX PubMed=1517575;
RA Ghildyal N., McNeil H.P., Stechschulte S., Austen K.F., Silberstein D.,
RA Gurish M.F., Somerville L.L., Stevens R.L.;
RT "IL-10 induces transcription of the gene for mouse mast cell protease-1, a
RT serine protease preferentially expressed in mucosal mast cells of
RT Trichinella spiralis-infected mice.";
RL J. Immunol. 149:2123-2129(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=2060576; DOI=10.1002/eji.1830210706;
RA Huang R., Blom T., Hellman L.;
RT "Cloning and structural analysis of MMCP-1, MMCP-4 and MMCP-5, three mouse
RT mast cell-specific serine proteases.";
RL Eur. J. Immunol. 21:1611-1621(1991).
RN [3]
RP PROTEIN SEQUENCE OF 21-246.
RX PubMed=2706264; DOI=10.1021/bi00427a054;
RA le Trong H., Newlands G.F.J., Miller H.R.P., Charbonneau H., Neurath H.,
RA Woodbury R.G.;
RT "Amino acid sequence of a mouse mucosal mast cell protease.";
RL Biochemistry 28:391-395(1989).
RN [4]
RP PROTEIN SEQUENCE OF 21-49.
RX PubMed=8363563; DOI=10.1042/bj2940127;
RA Newlands G.F.J., Knox D.P., Pirie-Shepherd S.R., Miller H.R.P.;
RT "Biochemical and immunological characterization of multiple glycoforms of
RT mouse mast cell protease 1: comparison with an isolated murine serosal mast
RT cell protease (MMCP-4).";
RL Biochem. J. 294:127-135(1993).
CC -!- FUNCTION: Has a chymotrypsin-like activity.
CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. Note=Secretory
CC granules.
CC -!- TISSUE SPECIFICITY: Mucosal mast cells.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; S44609; AAB23194.1; -; mRNA.
DR EMBL; X68803; CAA48703.1; -; Genomic_DNA.
DR CCDS; CCDS27137.1; -.
DR PIR; A46504; A46504.
DR RefSeq; NP_032596.1; NM_008570.1.
DR AlphaFoldDB; P11034; -.
DR SMR; P11034; -.
DR STRING; 10090.ENSMUSP00000022836; -.
DR MEROPS; S01.458; -.
DR GlyGen; P11034; 1 site.
DR CPTAC; non-CPTAC-3473; -.
DR PaxDb; P11034; -.
DR PeptideAtlas; P11034; -.
DR PRIDE; P11034; -.
DR ProteomicsDB; 292196; -.
DR DNASU; 17224; -.
DR Ensembl; ENSMUST00000022836; ENSMUSP00000022836; ENSMUSG00000022227.
DR GeneID; 17224; -.
DR KEGG; mmu:17224; -.
DR UCSC; uc007ubi.1; mouse.
DR CTD; 17224; -.
DR MGI; MGI:96937; Mcpt1.
DR VEuPathDB; HostDB:ENSMUSG00000022227; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234551; -.
DR HOGENOM; CLU_006842_1_0_1; -.
DR InParanoid; P11034; -.
DR OMA; WGKTGVR; -.
DR OrthoDB; 1076876at2759; -.
DR PhylomeDB; P11034; -.
DR TreeFam; TF333630; -.
DR BioGRID-ORCS; 17224; 1 hit in 71 CRISPR screens.
DR PRO; PR:P11034; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P11034; protein.
DR Bgee; ENSMUSG00000022227; Expressed in skin of snout and 64 other tissues.
DR ExpressionAtlas; P11034; baseline and differential.
DR Genevisible; P11034; MM.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:MGI.
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..18
FT PROPEP 19..20
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:2706264,
FT ECO:0000269|PubMed:8363563"
FT /id="PRO_0000027449"
FT CHAIN 21..246
FT /note="Mast cell protease 1"
FT /id="PRO_0000027450"
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 CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
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; 27013 MW; 26E112E8C580154B CRC64;
MQALLFLMAL LLPSGAGAEE IIGGVEARPH SRPYMAHLKI ITDRGSEDRC GGFLIAPQFV
LTAAHCKGRE ITVTLGAHDV SKSESTQQRI KVEKQIIHKN YNVSFNLYDI MLLKLEEKAE
LTPTVDVIPL PGPSDFIDPG KMCWTAGWGK TGEKEPTSET LREVELRIMD KEACKMYKHY
DYNFQVCVGS STKLKTAYMG DSGGPLLCAG VAHGIVSYGD SHGKPPAVFT RISAYVPWIK
TVINGK
