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 24-JAN-2024, entry version 157. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; P15119; 1 site, No reported glycans. DR GlyGen; P15119; 1 site. DR iPTMnet; P15119; -. DR PhosphoSitePlus; P15119; -. DR PaxDb; 10090-ENSMUSP00000015576; -. DR ProteomicsDB; 292197; -. DR DNASU; 17225; -. DR Ensembl; ENSMUST00000015576.6; ENSMUSP00000015576.5; ENSMUSG00000022226.7. DR GeneID; 17225; -. DR KEGG; mmu:17225; -. DR UCSC; uc007ubk.1; mouse. DR AGR; MGI:96938; -. 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; 2540265at2759; -. DR PhylomeDB; P15119; -. DR TreeFam; TF333630; -. DR BioGRID-ORCS; 17225; 1 hit in 77 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 cell types or tissues. DR ExpressionAtlas; P15119; baseline and differential. 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: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; 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; P15119; MM. 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 //