TRYB1_RAT
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 03-AUG-2022, entry version 148.
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 GlyGen; P27435; 1 site.
DR PaxDb; P27435; -.
DR GeneID; 54271; -.
DR KEGG; rno:54271; -.
DR UCSC; RGD:3066; rat.
DR CTD; 7177; -.
DR RGD; 3066; Tpsab1.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; P27435; -.
DR OrthoDB; 1314811at2759; -.
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; -; 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; 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
