ID   TRYT_CANLF              Reviewed;         275 AA.
AC   P15944;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Tryptase;
DE            EC=3.4.21.59;
DE   Flags: Precursor;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2504277; DOI=10.1021/bi00436a004;
RA   Vanderslice P., Craik C.S., Nadel J.A., Caughey G.H.;
RT   "Molecular cloning of dog mast cell tryptase and a related protease:
RT   structural evidence of a unique mode of serine protease activation.";
RL   Biochemistry 28:4148-4155(1989).
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.
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; M24664; AAA30854.1; -; Genomic_DNA.
DR   PIR; A32410; A32410.
DR   RefSeq; NP_001091024.1; NM_001097555.1.
DR   AlphaFoldDB; P15944; -.
DR   SMR; P15944; -.
DR   STRING; 9612.ENSCAFP00000041549; -.
DR   BindingDB; P15944; -.
DR   ChEMBL; CHEMBL4700; -.
DR   MEROPS; S01.118; -.
DR   PaxDb; P15944; -.
DR   PRIDE; P15944; -.
DR   Ensembl; ENSCAFT00000047008; ENSCAFP00000041549; ENSCAFG00000031939.
DR   Ensembl; ENSCAFT00030028446; ENSCAFP00030024818; ENSCAFG00030015380.
DR   Ensembl; ENSCAFT00040004828; ENSCAFP00040004145; ENSCAFG00040002521.
DR   Ensembl; ENSCAFT00845040586; ENSCAFP00845031769; ENSCAFG00845022862.
DR   GeneID; 100049001; -.
DR   KEGG; cfa:100049001; -.
DR   VEuPathDB; HostDB:ENSCAFG00845022862; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000162207; -.
DR   HOGENOM; CLU_006842_0_4_1; -.
DR   InParanoid; P15944; -.
DR   OMA; RIIRDDM; -.
DR   OrthoDB; 1314811at2759; -.
DR   TreeFam; TF351676; -.
DR   BRENDA; 3.4.21.59; 1153.
DR   Reactome; R-CFA-1592389; Activation of Matrix Metalloproteinases.
DR   PRO; PR:P15944; -.
DR   Proteomes; UP000002254; Chromosome 6.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..30
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000027473"
FT   CHAIN           31..275
FT                   /note="Tryptase"
FT                   /id="PRO_0000027474"
FT   DOMAIN          31..272
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        74
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        121
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        224
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        59..75
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        155..230
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        188..211
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        220..248
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   275 AA;  30088 MW;  C3B869251F248D5B CRC64;
     MPSPLVLALA LLGSLVPVSP APGQALQRVG IVGGREAPGS KWPWQVSLRL KGQYWRHICG
     GSLIHPQWVL TAAHCVGPNV VCPEEIRVQL REQHLYYQDH LLPVNRIVMH PNYYTPENGA
     DIALLELEDP VNVSAHVQPV TLPPALQTFP TGTPCWVTGW GDVHSGTPLP PPFPLKQVKV
     PIVENSMCDV QYHLGLSTGD GVRIVREDML CAGNSKSDSC QGDSGGPLVC RVRGVWLQAG
     VVSWGEGCAQ PNRPGIYTRV AYYLDWIHQY VPKEP