TRYT_MERUN
ID TRYT_MERUN Reviewed; 270 AA.
AC P50342;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Mast cell tryptase;
DE EC=3.4.21.59;
DE Flags: Precursor;
OS Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Gerbillinae; Meriones.
OX NCBI_TaxID=10047;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=MGS/SEA; TISSUE=Intestine;
RX PubMed=7639711; DOI=10.1042/bj3090921;
RA Murakumo Y., Ide H., Itoh H., Tomita M., Kobayashi T., Maruyama H.,
RA Horii Y., Nawa Y.;
RT "Cloning of the cDNA encoding mast cell tryptase of Mongolian gerbil,
RT Meriones unguiculatus, and its preferential expression in the intestinal
RT mucosa.";
RL Biochem. J. 309:921-926(1995).
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 -!- SIMILARITY: Belongs to the peptidase S1 family. Tryptase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D31789; BAA06598.1; -; mRNA.
DR PIR; S56160; S56160.
DR AlphaFoldDB; P50342; -.
DR SMR; P50342; -.
DR MEROPS; S01.026; -.
DR BRENDA; 3.4.21.59; 2421.
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; Serine protease; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..270
FT /note="Mast cell tryptase"
FT /id="PRO_0000027485"
FT DOMAIN 26..267
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 69
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 116
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 219
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..70
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 150..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 183..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 215..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 270 AA; 30167 MW; 1BE102DB86943401 CRC64;
MLKLLLLALP LFSLMHRSPL CQEWGIVGGQ EAPGNKWPWQ VSLRANETYW RHFCGGSLIH
PQWVLTAAHC VGPTIADPNK VRVQLRKQYL YYHDHLLAVS RIITHPTFYA TQNGADIALL
ELKNPVNISS HVHPVSLPPA SETFPSGTLC WVTGWGNIDN DVSLPPPFPL KEVQVPVVEN
QLCDLKYHKG VYTGDNIHIV RDDMLCAGNE GHDSCQGDSG GPLVCKVNGT WLQAGVVSWG
EGCALPNRPG IYTRVTYYLD WIHRYVPKDF
