TRYB2_RAT
ID TRYB2_RAT Reviewed; 274 AA.
AC P50343; P97593;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Tryptase beta-2;
DE Short=Tryptase-2;
DE EC=3.4.21.59;
DE AltName: Full=Mast cell protease 6;
DE Short=rMCP-6;
DE Flags: Precursor;
GN Name=Tpsb2; Synonyms=Mcp6, Mcpt6;
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 TISSUE=Peritoneal mast cell;
RX PubMed=8537314; DOI=10.1093/oxfordjournals.jbchem.a124880;
RA Ide H., Itoh H., Tomita M., Murakumo Y., Kobayashi T., Maruyama H.,
RA Osada Y., Nawa Y.;
RT "cDNA sequencing and expression of rat mast cell tryptase.";
RL J. Biochem. 118:210-215(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Peritoneal mast cell;
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).
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. Plays a role in innate immunity. {ECO:0000250,
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. The active tetramer is converted to inactive
CC monomers at neutral and acidic pH in the absence of heparin. Low
CC concentrations of inactive monomers become active monomers at pH 6.0 in
CC the presence of heparin. When the concentration of active monomers is
CC higher, they convert to active monomers and then to active tetramers.
CC These monomers are active and functionally distinct from the tetrameric
CC enzyme. In contrast to the hidden active sites in the tetrameric form,
CC the active site of the monomeric form is accessible for macromolecular
CC proteins and inhibitors eg: fibrinogen which is a substrate for the
CC monomeric but not for the tetrameric form. The monomeric form forms a
CC complex with SERPINB6.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Released from the
CC secretory granules upon mast cell activation. {ECO:0000250}.
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; D38455; BAA07486.1; -; mRNA.
DR EMBL; U67909; AAB48262.1; -; mRNA.
DR PIR; JC4171; JC4171.
DR RefSeq; NP_062053.2; NM_019180.2.
DR AlphaFoldDB; P50343; -.
DR SMR; P50343; -.
DR STRING; 10116.ENSRNOP00000025220; -.
DR MEROPS; S01.025; -.
DR GlyGen; P50343; 2 sites.
DR PhosphoSitePlus; P50343; -.
DR PaxDb; P50343; -.
DR GeneID; 29268; -.
DR KEGG; rno:29268; -.
DR UCSC; RGD:3065; rat.
DR CTD; 64499; -.
DR RGD; 3065; Tpsb2.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; P50343; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P50343; -.
DR Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases.
DR PRO; PR:P50343; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0008201; F:heparin 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: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; Phosphoprotein; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..29
FT /note="Activation peptide"
FT /id="PRO_0000027492"
FT CHAIN 30..274
FT /note="Tryptase beta-2"
FT /id="PRO_0000027493"
FT DOMAIN 30..271
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 73
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 120
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 223
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 96
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P21845"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 154..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 187..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 219..247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 128
FT /note="I -> N (in Ref. 2; AAB48262)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="I -> T (in Ref. 2; AAB48262)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 274 AA; 30508 MW; DF84D55668CA1A25 CRC64;
MLKLLLLLAL SPLASLVHAA PCPVKQRVGI VGGREASESK WPWQVSLRFK FSFWMHFCGG
SLIHPQWVLT AAHCVGLHIK SPELFRVQLR EQYLYYADQL LTVNRTVVHP HYYTVEDGAD
IALLELEIPV NVSTHIHPIS LPPASETFPS GTSCWVTGWG DIDSDEPLLP PYPLKQVKVP
IVENSLCDRK YHTGLYTGDD VPIVQDGMLC AGNTRSDSCQ GDSGGPLVCK VKGTWLQAGV
VSWGEGCAEA NRPGIYTRVT YYLDWIHRYV PQRS
