ID   TRYT_SHEEP              Reviewed;         273 AA.
AC   Q9XSM2;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Tryptase-2;
DE            EC=3.4.21.59;
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=Abomasum;
RX   PubMed=10848900; DOI=10.1046/j.1365-2222.2000.00831.x;
RA   Pemberton A.D., McAleese S.M., Huntley J.F., Collie D.D.S., Scudamore C.L.,
RA   McEuen A.R., Walls A.F., Miller H.R.P.;
RT   "cDNA sequence of two sheep mast cell tryptases and the differential
RT   expression of tryptase and sheep mast cell proteinase-1 in lung, dermis and
RT   gastrointestinal tract.";
RL   Clin. Exp. Allergy 30:818-832(2000).
CC   -!- FUNCTION: Tryptase is the major neutral protease present in mast cells
CC       and is secreted upon the coupled activation-degranulation response of
CC       this cell type.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more
CC         restricted specificity than trypsin.; EC=3.4.21.59;
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Released from the secretory
CC       granules upon mast cell activation.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Tryptase subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; Y18224; CAB41989.1; -; mRNA.
DR   RefSeq; NP_001116478.1; NM_001123006.1.
DR   AlphaFoldDB; Q9XSM2; -.
DR   SMR; Q9XSM2; -.
DR   STRING; 9940.ENSOARP00000015758; -.
DR   MEROPS; S01.118; -.
DR   PRIDE; Q9XSM2; -.
DR   GeneID; 100144429; -.
DR   KEGG; oas:100144429; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   OrthoDB; 1314811at2759; -.
DR   BRENDA; 3.4.21.59; 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:UniProtKB-EC.
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..28
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000027488"
FT   CHAIN           29..273
FT                   /note="Tryptase-2"
FT                   /id="PRO_0000027489"
FT   DOMAIN          29..270
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        72
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        119
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        222
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        57..73
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        153..228
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        186..209
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        218..246
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   273 AA;  30288 MW;  DE9BA79218C3E67D CRC64;
     MLHLLALALL LSLVSAAPAP GQALQRSGII GGKEAPGSRW PWQVSLRVRD QYWRHQCGGS
     LIHPQWVLTA AHCIGPELQE PSDFRVQLRE QHLYYQDRLL PISRVIPHPH YYMVENGADI
     ALLQLEEPVS ISRHVQPVTL PPASETFPPE SQCWVTGWGD VDNGRPLPPP YPLKQVKVPI
     VENSVCDWKY HSGLSTDYSV PIVQEDNLCA GDGGRDSCQG DSGGPLVCKV NGTWLQAGVV
     SWGDGCAKPN RPGIYTRITS YLDWIHQYVP QEP