MCPT2_MOUSE
ID MCPT2_MOUSE Reviewed; 244 AA.
AC P15119;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Mast cell protease 2;
DE Short=mMCP-2;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=Mcpt2;
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 [MRNA].
RX PubMed=1688433; DOI=10.1016/s0021-9258(19)40247-0;
RA Serafin W.E., Reynolds D.S., Rogelj S., Lane W.S., Conder G.A.,
RA Johnson S.S., Austen K.F., Stevens R.L.;
RT "Identification and molecular cloning of a novel mouse mucosal mast cell
RT serine protease.";
RL J. Biol. Chem. 265:423-429(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Hematopoietic;
RX PubMed=8098710; DOI=10.1016/s0021-9258(18)82134-2;
RA Gurish M.F., Nadeau J.H., Johnson K.R., McNeil H.P., Grattan K.M.,
RA Austen K.F., Stevens R.L.;
RT "A closely linked complex of mouse mast cell-specific chymase genes on
RT chromosome 14.";
RL J. Biol. Chem. 268:11372-11379(1993).
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; J05177; AAA39972.1; -; mRNA.
DR EMBL; L08486; AAA74555.1; -; Genomic_DNA.
DR CCDS; CCDS27139.1; -.
DR PIR; A34910; A34910.
DR PIR; A46721; A46721.
DR RefSeq; NP_032597.1; NM_008571.1.
DR AlphaFoldDB; P15119; -.
DR SMR; P15119; -.
DR STRING; 10090.ENSMUSP00000015576; -.
DR MEROPS; S01.003; -.
DR GlyGen; P15119; 1 site.
DR iPTMnet; P15119; -.
DR PhosphoSitePlus; P15119; -.
DR PaxDb; P15119; -.
DR PRIDE; P15119; -.
DR ProteomicsDB; 292197; -.
DR DNASU; 17225; -.
DR Ensembl; ENSMUST00000015576; ENSMUSP00000015576; ENSMUSG00000022226.
DR GeneID; 17225; -.
DR KEGG; mmu:17225; -.
DR UCSC; uc007ubk.1; mouse.
DR CTD; 17225; -.
DR MGI; MGI:96938; Mcpt2.
DR VEuPathDB; HostDB:ENSMUSG00000022226; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234551; -.
DR HOGENOM; CLU_006842_1_0_1; -.
DR InParanoid; P15119; -.
DR OMA; NGSKERC; -.
DR OrthoDB; 434182at33208; -.
DR PhylomeDB; P15119; -.
DR TreeFam; TF333630; -.
DR BioGRID-ORCS; 17225; 1 hit in 72 CRISPR screens.
DR PRO; PR:P15119; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P15119; protein.
DR Bgee; ENSMUSG00000022226; Expressed in mucous cell of stomach and 31 other tissues.
DR ExpressionAtlas; P15119; baseline and differential.
DR Genevisible; P15119; MM.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..18
FT PROPEP 19..20
FT /note="Activation peptide"
FT /id="PRO_0000027451"
FT CHAIN 21..244
FT /note="Mast cell protease 2"
FT /id="PRO_0000027452"
FT DOMAIN 21..242
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 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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"
FT CONFLICT 67
FT /note="N -> R (in Ref. 1; AAA39972)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="Y -> N (in Ref. 1; AAA39972)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="S -> N (in Ref. 1; AAA39972)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="S -> L (in Ref. 1; AAA39972)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="S -> G (in Ref. 1; AAA39972)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 244 AA; 26732 MW; 132E248B6E2339CC CRC64;
MQALLFLMAL LLPSGAGAEE IIGGVEAKPH SRPYMAYLKF TTKNGSKERC GGFLIAPQFV
MTAAHCNGSE ISVILGAHNI NKNEPTQQII KTEKTFVHPK FQYLSGFYDI MLLKLQKKAE
LNSDVDVISL PSSSDFIKPG KMCWTAGWGK TGKNNPLSVT LREVELRIMD QEACKDHSDY
DYQLQVCAGS PTTSKSIGQG DSGGPLVCDS VAHGIASSYE AKAPAVFTRI SYYLPWIYKV
LKSK
