TRYB1_MOUSE
ID TRYB1_MOUSE Reviewed; 273 AA.
AC Q02844;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Tryptase;
DE EC=3.4.21.59;
DE AltName: Full=Mast cell protease 7;
DE Short=mMCP-7;
DE AltName: Full=Tryptase alpha/beta-1;
DE Flags: Precursor;
GN Name=Tpsab1; Synonyms=Mcpt7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC STRAIN=DBA/2J;
RX PubMed=1454796; DOI=10.1073/pnas.89.23.11174;
RA McNeil H.P., Reynolds D.S., Schiller V., Ghildyal N., Gurley D.S.,
RA Austen K.F., Stevens R.L.;
RT "Isolation, characterization, and transcription of the gene encoding mouse
RT mast cell protease 7.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11174-11178(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RX PubMed=8576265; DOI=10.1074/jbc.271.5.2851;
RA Hunt J.E., Stevens R.L., Austen K.F., Zhang J., Xia Z., Ghildyal N.;
RT "Natural disruption of the mouse mast cell protease 7 gene in the C57BL/6
RT mouse.";
RL J. Biol. Chem. 271:2851-2855(1996).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=The alternative splicing event is due to a G to A point
CC mutation at the exon 2/intron 2 splice site and causes loss of
CC protein expression. The alternatively spliced transcript is only
CC found in C57BL/6 mouse.;
CC Name=1;
CC IsoId=Q02844-1; Sequence=Displayed;
CC Name=2; Synonyms=Truncated;
CC IsoId=Q02844-2; Sequence=VSP_005378, VSP_005379;
CC -!- DEVELOPMENTAL STAGE: Is not expressed in mature serosal or mucosal mast
CC cells and is expressed only transiently at an early stage of in vitro
CC mast cell differentiation.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Tryptase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; L00653; AAA39992.1; -; mRNA.
DR EMBL; L00654; AAA39993.1; -; Genomic_DNA.
DR EMBL; U42405; AAA97874.1; -; mRNA.
DR EMBL; U42406; AAA97875.1; -; Genomic_DNA.
DR PIR; A47246; A47246.
DR RefSeq; NP_112464.4; NM_031187.4. [Q02844-1]
DR AlphaFoldDB; Q02844; -.
DR SMR; Q02844; -.
DR ComplexPortal; CPX-3804; Tryptase alpha/beta-1 complex.
DR STRING; 10090.ENSMUSP00000120741; -.
DR BindingDB; Q02844; -.
DR ChEMBL; CHEMBL4749; -.
DR MEROPS; S01.026; -.
DR GlyGen; Q02844; 2 sites.
DR PhosphoSitePlus; Q02844; -.
DR PaxDb; Q02844; -.
DR PRIDE; Q02844; -.
DR ProteomicsDB; 297531; -. [Q02844-1]
DR GeneID; 100503895; -.
DR KEGG; mmu:100503895; -.
DR UCSC; uc008baq.2; mouse. [Q02844-1]
DR CTD; 7177; -.
DR MGI; MGI:96943; Tpsab1.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q02844; -.
DR PhylomeDB; Q02844; -.
DR BioGRID-ORCS; 100503895; 1 hit in 51 CRISPR screens.
DR PRO; PR:Q02844; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q02844; protein.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0042629; C:mast cell granule; IDA:MGI.
DR GO; GO:1905368; C:peptidase complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0022617; P:extracellular matrix disassembly; ISO:MGI.
DR GO; GO:0030195; P:negative regulation of blood coagulation; TAS:MGI.
DR GO; GO:0006508; P:proteolysis; IDA:MGI.
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 Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Serine protease; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..28
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027494"
FT CHAIN 29..273
FT /note="Tryptase"
FT /id="PRO_0000027495"
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:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 VAR_SEQ 44..46
FT /note="VSL -> GCC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8576265"
FT /id="VSP_005378"
FT VAR_SEQ 47..273
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8576265"
FT /id="VSP_005379"
SQ SEQUENCE 273 AA; 30337 MW; 50ECB4765294205E CRC64;
MLKLLLLTLP LLSSLVHAAP GPAMTREGIV GGQEAHGNKW PWQVSLRAND TYWMHFCGGS
LIHPQWVLTA AHCVGPDVAD PNKVRVQLRK QYLYYHDHLM TVSQIITHPD FYIVQDGADI
ALLKLTNPVN ISDYVHPVPL PPASETFPSG TLCWVTGWGN IDNGVNLPPP FPLKEVQVPI
IENHLCDLKY HKGLITGDNV HIVRDDMLCA GNEGHDSCQG DSGGPLVCKV EDTWLQAGVV
SWGEGCAQPN RPGIYTRVTY YLDWIHHYVP KDF
