ID   TRYB1_RAT               Reviewed;         273 AA.
AC   P27435; P27436;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Tryptase;
DE            EC=3.4.21.59;
DE   AltName: Full=Mast cell protease 7;
DE            Short=rMCP-7;
DE   AltName: Full=Tryptase alpha/beta-1;
DE   AltName: Full=Tryptase, skin;
DE   Flags: Precursor;
GN   Name=Tpsab1; Synonyms=Mcp7, Mcpt7, Tpsb1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RX   PubMed=8996238; DOI=10.1084/jem.185.1.13;
RA   Lutzelschwab C., Pejler G., Aveskogh M., Hellman L.;
RT   "Secretory granule proteases in rat mast cells. Cloning of 10 different
RT   serine proteases and a carboxypeptidase A from various rat mast cell
RT   populations.";
RL   J. Exp. Med. 185:13-29(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 29-53.
RC   STRAIN=Sprague-Dawley; TISSUE=Skin;
RX   PubMed=2036367; DOI=10.1021/bi00234a023;
RA   Braganza V.J., Simmons W.H.;
RT   "Tryptase from rat skin: purification and properties.";
RL   Biochemistry 30:4997-5007(1991).
RN   [3]
RP   PROTEIN SEQUENCE OF 29-51.
RC   TISSUE=Mammary carcinoma;
RX   PubMed=1314562; DOI=10.1042/bj2830209;
RA   Eto I., Grubbs C.J.;
RT   "Separation, purification and N-terminal sequence analysis of a novel
RT   leupeptin-sensitive serine endopeptidase present in chemically induced rat
RT   mammary tumour.";
RL   Biochem. J. 283:209-216(1992).
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. May play a role in innate immunity (By similarity).
CC       {ECO:0000250|UniProtKB:P21845}.
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   -!- TISSUE SPECIFICITY: Mast cells.
CC   -!- PTM: Glycosylated. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Tryptase subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; U67910; AAB48263.1; -; mRNA.
DR   PIR; A23698; A23698.
DR   PIR; S21275; S21275.
DR   RefSeq; NP_062195.2; NM_019322.2.
DR   AlphaFoldDB; P27435; -.
DR   SMR; P27435; -.
DR   STRING; 10116.ENSRNOP00000025095; -.
DR   BindingDB; P27435; -.
DR   ChEMBL; CHEMBL3320; -.
DR   MEROPS; S01.026; -.
DR   MEROPS; S01.143; -.
DR   GlyCosmos; P27435; 1 site, No reported glycans.
DR   GlyGen; P27435; 1 site.
DR   PhosphoSitePlus; P27435; -.
DR   PaxDb; 10116-ENSRNOP00000025095; -.
DR   GeneID; 54271; -.
DR   KEGG; rno:54271; -.
DR   UCSC; RGD:3066; rat.
DR   AGR; RGD:3066; -.
DR   CTD; 7177; -.
DR   RGD; 3066; Tpsab1.
DR   eggNOG; KOG3627; Eukaryota.
DR   InParanoid; P27435; -.
DR   OrthoDB; 4629979at2759; -.
DR   PhylomeDB; P27435; -.
DR   PRO; PR:P27435; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0042629; C:mast cell granule; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0008233; F:peptidase activity; ISO:RGD.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0022617; P:extracellular matrix disassembly; ISO:RGD.
DR   GO; GO:0006508; P:proteolysis; ISO:RGD.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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   PANTHER; PTHR24253; TRANSMEMBRANE PROTEASE SERINE; 1.
DR   PANTHER; PTHR24253:SF32; TRYPTASE; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 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; Glycoprotein; Hydrolase;
KW   Protease; Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..28
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:1314562,
FT                   ECO:0000269|PubMed:2036367"
FT                   /id="PRO_0000027496"
FT   CHAIN           29..273
FT                   /note="Tryptase"
FT                   /id="PRO_0000027497"
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        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
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"
FT   CONFLICT        42
FT                   /note="W -> V (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        49..51
FT                   /note="NDT -> WLP (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   273 AA;  30400 MW;  65A5ED4D279FB284 CRC64;
     MLKLLLLTLP LLSSLVHAAP SLAMPREGIV GGQEASGNKW PWQVSLRVND TYWMHFCGGS
     LIHPQWVLTA AHCVGPNKAD PNKLRVQLRK QYLYYHDHLL TVSQIISHPD FYIAQDGADI
     ALLKLTNPVN ITSNVHTVSL PPASETFPSG TLCWVTGWGN INNDVSLPPP FPLEEVQVPI
     VENRLCDLKY HKGLNTGDNV HIVRDDMLCA GNEGHDSCQG DSGGPLVCKV EDTWLQAGVV
     SWGEGCAQPN RPGIYTRVTY YLDWIYRYVP KYF
//