ID   MCPT2_SHEEP             Reviewed;         246 AA.
AC   P79204;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Mast cell protease 2;
DE            Short=sMCP-2;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Bone marrow;
RA   McAleese S.M., Knox D.P., Huntley J.F., Miller H.R.P.;
RT   "Sheep mast cell proteinase-2; cDNA sequence and tissue expression.";
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Putative mast cell chymase.
CC   -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. Note=Secretory
CC       granules.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; Y08133; CAA69327.1; -; mRNA.
DR   RefSeq; NP_001116477.1; NM_001123005.1.
DR   AlphaFoldDB; P79204; -.
DR   SMR; P79204; -.
DR   STRING; 9940.ENSOARP00000004835; -.
DR   MEROPS; S01.140; -.
DR   GeneID; 101107261; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   OrthoDB; 1076876at2759; -.
DR   BRENDA; 3.4.21.39; 2668.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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..21
FT                   /note="Activation peptide"
FT                   /id="PRO_0000027469"
FT   CHAIN           22..246
FT                   /note="Mast cell protease 2"
FT                   /id="PRO_0000027470"
FT   DOMAIN          22..244
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        66
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        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        51..67
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;  27146 MW;  4C6AFE710B8431AD CRC64;
     MHRPPLPLVL LLLCCRAQAG EIIGGTESKP HSRPYMAYLE IVTSQEKQVA CGGFLIRRDF
     VLTAAHCAGR SVTVTLGAHN IQKKEDTWQR LEVIKQFPYP KYEPVGVHDI MLLKLKEKAN
     LTLAVGTLPL PPHVTFIRPG RMCQVAGWGR TGVKEPASST LQEVKLRLME PRACRHFRAF
     DHNLQLCVGN PQSTKSAFKG DSGGPLLCAG VAQGIVSYGL SSAKPPAVFT RISPYRPWID
     EVLKEN