MCPTX_MOUSE
ID MCPTX_MOUSE Reviewed; 246 AA.
AC Q00356;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Mast cell protease-like protein;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=Mcptl;
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].
RX PubMed=1988455; DOI=10.1016/s0021-9258(18)52383-8;
RA Serafin W.E., Sullivan T.P., Conder G.A., Ebrahimi A., Marcham P.,
RA Johnson S.S., Austen K.F., Reynolds D.S.;
RT "Cloning of the cDNA and gene for mouse mast cell protease 4. Demonstration
RT of its late transcription in mast cell subclasses and analysis of its
RT homology to subclass-specific neutral proteases of the mouse and rat.";
RL J. Biol. Chem. 266:1934-1941(1991).
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; M57401; AAA39990.1; -; Genomic_DNA.
DR PIR; A38678; A38678.
DR AlphaFoldDB; Q00356; -.
DR SMR; Q00356; -.
DR BioGRID; 201362; 1.
DR MEROPS; S01.304; -.
DR PRIDE; Q00356; -.
DR MGI; MGI:102792; Mcptl.
DR InParanoid; Q00356; -.
DR PRO; PR:Q00356; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q00356; protein.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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 3: Inferred from homology;
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_0000027461"
FT CHAIN 21..246
FT /note="Mast cell protease-like protein"
FT /id="PRO_0000027462"
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; 26775 MW; 304BA25BC2B2B2AD CRC64;
MQALLFLMAL LLPSGAGAEE IIGGVESEPH SRPYMAYVNT FRRKGYVAIC GGFLITPQFV
MTAAHCRGRR MTVTLGAHNV RKRECTQQKI KVEKYILPPN YNVSSKFNDI VLLKLKKQAN
LTSAVDVVPL PGPSDFAKPG TMCWAAGWGR TGVKKIISHT LREVELKIVG EKACKIFRHY
KDSLQICVGS STKVASVYMG DSGGPLLCAG VAHGIVSSGR GNAKPPAIFT RISPHVPWIN
RVIKGK
