ID   MCT1A_SHEEP             Reviewed;         245 AA.
AC   P80931;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Mast cell protease 1A;
DE            Short=sMCP-1A;
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], AND PROTEIN SEQUENCE OF 176-185.
RC   TISSUE=Mast cell;
RX   PubMed=9677343; DOI=10.1042/bj3330801;
RA   McAleese S.M., Pemberton A.D., McGrath M.E., Huntley J.F., Miller H.R.P.;
RT   "Sheep mast-cell proteinases-1 and -3: cDNA cloning, primary structure and
RT   molecular modelling of the enzymes and further studies on substrate
RT   specificity.";
RL   Biochem. J. 333:801-809(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 20-44.
RA   Miller H.R.P., Huntley J.F., Newlands G.F.J.;
RL   (In) Caughey G.H. (eds.);
RL   Mast cell proteases in immunology and biology, pp.203-235, Marcel Dekker,
RL   New York (1995).
RN   [3]
RP   PROTEIN SEQUENCE OF 20-29.
RC   TISSUE=Gastric mucosa;
RX   PubMed=9032451; DOI=10.1042/bj3210665;
RA   Pemberton A.D., Huntley J.F., Miller H.R.P.;
RT   "Sheep mast cell proteinase-1: characterization as a member of a new class
RT   of dual-specific ruminant chymases.";
RL   Biochem. J. 321:665-670(1997).
CC   -!- FUNCTION: Has a chymotrypsin-like and trypsin-like activity.
CC   -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. Note=Secretory
CC       granules.
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; Y14654; CAA74984.1; -; mRNA.
DR   RefSeq; NP_001009472.1; NM_001009472.1.
DR   AlphaFoldDB; P80931; -.
DR   SMR; P80931; -.
DR   MEROPS; S01.142; -.
DR   PRIDE; P80931; -.
DR   GeneID; 443546; -.
DR   KEGG; oas:443546; -.
DR   CTD; 443546; -.
DR   OrthoDB; 1076876at2759; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..19
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:9032451, ECO:0000269|Ref.2"
FT                   /id="PRO_0000027467"
FT   CHAIN           20..245
FT                   /note="Mast cell protease 1A"
FT                   /id="PRO_0000027468"
FT   DOMAIN          20..243
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        63
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        201
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        48..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        141..207
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        172..186
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        20
FT                   /note="I -> F (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   245 AA;  26877 MW;  C362CF3367FFF180 CRC64;
     MVLFLLLVAL LSPAGEAGKI IGGHEAKPHS RPYMAFLQIK ISGKSYRCGG FLVHEDFVLT
     AAHCLGSSIS VTLGAHNIVD RERTQQVIQV RRAIPHPHYN DKTLANDIML LQLTRKAEMS
     DAVSPINLPR SLEKVKPGMM CSVAGWGQLG VNMPSADKLQ EVNLEVQSEE ECIARFKNYI
     PITQICAGDS TKRKNSFSGD SGGPLVCNGV AQGIVSYGKD DGTTPDVYTR ISSFLSWIQR
     TMRRY