MCPT8_MOUSE
ID MCPT8_MOUSE Reviewed; 247 AA.
AC P43430; Q9R1F1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Mast cell protease 8;
DE Short=mMCP-8;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=Mcpt8;
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].
RC STRAIN=Leaden X A1;
RX PubMed=9541598;
RX DOI=10.1002/(sici)1521-4141(199803)28:03<1022::aid-immu1022>3.0.co;2-1;
RA Lutzelschwab C., Huang M.R., Kullberg M.C., Aveskogh M., Hellman L.;
RT "Characterization of mouse mast cell protease-8, the first member of a
RT novel subfamily of mouse mast cell serine proteases, distinct from both the
RT classical chymases and tryptases.";
RL Eur. J. Immunol. 28:1022-1033(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ, and ICR X Swiss Webster; TISSUE=Liver;
RX PubMed=11398967; DOI=10.1007/s002510100316;
RA Lunderius C., Hellman L.;
RT "Characterization of the gene encoding mouse mast cell protease 8 (mMCP-8),
RT and a comparative analysis of hematopoietic serine protease genes.";
RL Immunogenetics 53:225-232(2001).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasmic granule
CC {ECO:0000250}. Note=Secretory granules. {ECO:0000250}.
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; X78545; CAA55291.1; -; mRNA.
DR EMBL; AF119362; AAD43899.1; -; Genomic_DNA.
DR EMBL; AF119363; AAD43900.1; -; Genomic_DNA.
DR CCDS; CCDS27141.1; -.
DR PIR; S45113; S45113.
DR RefSeq; NP_032598.1; NM_008572.1.
DR AlphaFoldDB; P43430; -.
DR SMR; P43430; -.
DR STRING; 10090.ENSMUSP00000015594; -.
DR MEROPS; S01.254; -.
DR GlyGen; P43430; 5 sites.
DR PhosphoSitePlus; P43430; -.
DR PaxDb; P43430; -.
DR PRIDE; P43430; -.
DR ProteomicsDB; 292198; -.
DR DNASU; 17231; -.
DR Ensembl; ENSMUST00000015594; ENSMUSP00000015594; ENSMUSG00000022157.
DR GeneID; 17231; -.
DR KEGG; mmu:17231; -.
DR UCSC; uc007ubm.2; mouse.
DR CTD; 17231; -.
DR MGI; MGI:1261780; Mcpt8.
DR VEuPathDB; HostDB:ENSMUSG00000022157; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234551; -.
DR HOGENOM; CLU_006842_1_0_1; -.
DR InParanoid; P43430; -.
DR OMA; WAVKTIT; -.
DR OrthoDB; 1076876at2759; -.
DR PhylomeDB; P43430; -.
DR TreeFam; TF333630; -.
DR BioGRID-ORCS; 17231; 1 hit in 72 CRISPR screens.
DR PRO; PR:P43430; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P43430; protein.
DR Bgee; ENSMUSG00000022157; Expressed in granulocyte and 21 other tissues.
DR ExpressionAtlas; P43430; baseline and differential.
DR Genevisible; P43430; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
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; -; 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 Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20
FT /note="Activation peptide"
FT /id="PRO_0000027457"
FT CHAIN 21..247
FT /note="Mast cell protease 8"
FT /id="PRO_0000027458"
FT DOMAIN 21..242
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 64
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 107
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 200
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 141..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 171..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 182
FT /note="I -> T (in Ref. 2; AAD43900)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 247 AA; 27122 MW; 4BB3C1D650185E29 CRC64;
MFLLLVLLVA ALPVNAEGGE IIWGTESKPH SRPYMAYIRF NDSKSVYRCG GFLVARDIVM
TAAHCNGKVI NVTLGIHNLK KKKNTQLIPV SEAIPHESFD NETLVNDIML LKLERKAQLN
SAVDTIALPK SKDWVKPGQV CTVAGWGKLA NCTLSDTLQE VNLEVQKGQK CRSMSQTYND
SIQLCVGNPS ENKATGKGDS GGPFVCNGVV QGIVSCRLCT GTLPRVFTRI SSFMPWIRKT
MKLLQQP
