ID   MCPT8_RAT               Reviewed;         248 AA.
AC   P97594;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Mast cell protease 8;
DE            Short=rMCP-8;
DE            EC=3.4.21.-;
DE   AltName: Full=Mast cell protease VIII;
DE            Short=rMCP-VIII;
DE   Flags: Precursor;
GN   Name=Mcpt8;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar;
RX   PubMed=8996238; DOI=10.1084/jem.185.1.13;
RA   Lutzelschwab C., Pejler G., Aveskogh M., Hellman L.;
RT   "Secretory granule proteases in rat mast cells. Cloning of 10 different
RT   serine proteases and a carboxypeptidase A from various rat mast cell
RT   populations.";
RL   J. Exp. Med. 185:13-29(1997).
CC   -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. Note=Secretory
CC       granules.
CC   -!- TISSUE SPECIFICITY: Mast cells.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; U67911; AAB48264.1; -; mRNA.
DR   RefSeq; NP_058842.1; NM_017146.1.
DR   RefSeq; NP_067609.1; NM_021598.2.
DR   RefSeq; XP_017455369.1; XM_017599880.1.
DR   AlphaFoldDB; P97594; -.
DR   SMR; P97594; -.
DR   STRING; 10116.ENSRNOP00000027950; -.
DR   MEROPS; S01.009; -.
DR   GlyGen; P97594; 3 sites.
DR   PhosphoSitePlus; P97594; -.
DR   PaxDb; P97594; -.
DR   GeneID; 29269; -.
DR   GeneID; 54269; -.
DR   UCSC; RGD:3067; rat.
DR   CTD; 17231; -.
DR   CTD; 54269; -.
DR   RGD; 3067; Mcpt8.
DR   VEuPathDB; HostDB:ENSRNOG00000063482; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   InParanoid; P97594; -.
DR   OMA; TEDHECK; -.
DR   OrthoDB; 1076876at2759; -.
DR   PhylomeDB; P97594; -.
DR   TreeFam; TF333630; -.
DR   PRO; PR:P97594; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Bgee; ENSRNOG00000049991; Expressed in stomach and 13 other tissues.
DR   ExpressionAtlas; P97594; baseline and differential.
DR   Genevisible; P97594; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..20
FT                   /note="Activation peptide"
FT                   /id="PRO_0000027447"
FT   CHAIN           21..248
FT                   /note="Mast cell protease 8"
FT                   /id="PRO_0000027448"
FT   DOMAIN          21..243
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        108
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        201
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        142..207
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        172..186
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   248 AA;  27486 MW;  913178B7F033DD8E CRC64;
     MFLFLFFLVA ILPVNTEGGE IIWGTESKPH SRPYMASLMF YYGNSYRHYC GGFLVAKDIV
     MTAAHCNGSN IKVTLGAHNI KKQEKTQVIA VVKAKPHENY DRHSRFNDIM LLKLERKAQL
     NGAVKTIALP RSQDWVKPGQ VCTVAGWGCL ANCSLSNTLQ EVNLEVQEGQ KCEDMSRNYN
     DSIQLCVGNP SEGKATGKGD SGGPFVCDGV AQGIVSYRLC TGTLPRVFTR ISSFIPWIQK
     TMKLLQQS