ID   TRYT_PIG                Reviewed;         275 AA.
AC   Q9N2D1;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Tryptase;
DE            EC=3.4.21.59;
DE   Flags: Precursor;
GN   Name=MCT7;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   PubMed=10824103; DOI=10.1046/j.1432-1327.2000.01346.x;
RA   Chen Y., Shiota M., Ohuchi M., Towatari T., Tashiro J., Murakami M.,
RA   Yano M., Yang B., Kido H.;
RT   "Mast cell tryptase from pig lungs triggers infection by pneumotropic
RT   Sendai and influenza A viruses. Purification and characterization.";
RL   Eur. J. Biochem. 267:3189-3197(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; AB038652; BAA93614.1; -; mRNA.
DR   RefSeq; NP_999356.1; NM_214191.1.
DR   AlphaFoldDB; Q9N2D1; -.
DR   SMR; Q9N2D1; -.
DR   STRING; 9823.ENSSSCP00000026057; -.
DR   MEROPS; S01.118; -.
DR   PaxDb; Q9N2D1; -.
DR   PeptideAtlas; Q9N2D1; -.
DR   Ensembl; ENSSSCT00035025182; ENSSSCP00035009520; ENSSSCG00035019421.
DR   Ensembl; ENSSSCT00050107753; ENSSSCP00050047710; ENSSSCG00050078183.
DR   GeneID; 397389; -.
DR   KEGG; ssc:397389; -.
DR   CTD; 397389; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   InParanoid; Q9N2D1; -.
DR   OMA; ASWVENC; -.
DR   OrthoDB; 1314811at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
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   2: Evidence at transcript level;
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_0000027486"
FT   CHAIN           31..275
FT                   /note="Tryptase"
FT                   /id="PRO_0000027487"
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   CARBOHYD        233
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;  30439 MW;  ACC582647FCCB973 CRC64;
     MLNLLVLALP LLVSLVHTAP APGQALERAG IVGGKEAPGH KWPWQVSLRC LDQYWKHFCG
     GSLIHPQWVL TAAHCFGPEK ADPLYIRVQL GEQHLYYQDR LLLVSRIIVH PNYYDEVNGA
     DIALLELEDP VNLSSHVQPV TLPPASETFP KGTRCWVTGW GDVHSGWPLP PPYPLKQVRV
     PIVENSECDM QYHLGLSTGD NIPIVRDDML CAGSEGHDSC QGDSGGPLVC RVNGTWLQAG
     VVSWGEGCAL PNRPGIYTRV THYLDWIHQC IPRES