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Tryptase (EC 3.4.21.59) (Mast cell protease 7) (rMCP-7) (Tryptase alpha/beta-1) (Tryptase, skin)

 TRYB1_RAT               Reviewed;         273 AA.
P27435; P27436;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
23-MAY-2018, entry version 135.
RecName: Full=Tryptase;
EC=3.4.21.59;
AltName: Full=Mast cell protease 7;
Short=rMCP-7;
AltName: Full=Tryptase alpha/beta-1;
AltName: Full=Tryptase, skin;
Flags: Precursor;
Name=Tpsab1; Synonyms=Mcp7, Mcpt7, Tpsb1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
PubMed=8996238; DOI=10.1084/jem.185.1.13;
Lutzelschwab C., Pejler G., Aveskogh M., Hellman L.;
"Secretory granule proteases in rat mast cells. Cloning of 10
different serine proteases and a carboxypeptidase A from various rat
mast cell populations.";
J. Exp. Med. 185:13-29(1997).
[2]
PROTEIN SEQUENCE OF 29-53.
STRAIN=Sprague-Dawley; TISSUE=Skin;
PubMed=2036367; DOI=10.1021/bi00234a023;
Braganza V.J., Simmons W.H.;
"Tryptase from rat skin: purification and properties.";
Biochemistry 30:4997-5007(1991).
[3]
PROTEIN SEQUENCE OF 29-51.
TISSUE=Mammary carcinoma;
PubMed=1314562; DOI=10.1042/bj2830209;
Eto I., Grubbs C.J.;
"Separation, purification and N-terminal sequence analysis of a novel
leupeptin-sensitive serine endopeptidase present in chemically induced
rat mammary tumour.";
Biochem. J. 283:209-216(1992).
-!- FUNCTION: Tryptase is the major neutral protease present in mast
cells and is secreted upon the coupled activation-degranulation
response of this cell type. May play a role in innate immunity (By
similarity). {ECO:0000250|UniProtKB:P21845}.
-!- CATALYTIC ACTIVITY: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa,
but with more restricted specificity than trypsin.
-!- SUBUNIT: Homotetramer.
-!- SUBCELLULAR LOCATION: Secreted. Note=Released from the secretory
granules upon mast cell activation.
-!- TISSUE SPECIFICITY: Mast cells.
-!- PTM: Glycosylated. {ECO:0000305}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Tryptase
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; U67910; AAB48263.1; -; mRNA.
PIR; A23698; A23698.
PIR; S21275; S21275.
RefSeq; NP_062195.2; NM_019322.2.
UniGene; Rn.10699; -.
ProteinModelPortal; P27435; -.
SMR; P27435; -.
STRING; 10116.ENSRNOP00000025095; -.
BindingDB; P27435; -.
ChEMBL; CHEMBL3320; -.
MEROPS; S01.143; -.
PaxDb; P27435; -.
PRIDE; P27435; -.
GeneID; 54271; -.
KEGG; rno:54271; -.
UCSC; RGD:3066; rat.
CTD; 7177; -.
RGD; 3066; Tpsab1.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; P27435; -.
KO; K01340; -.
PhylomeDB; P27435; -.
PRO; PR:P27435; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Hydrolase; Protease; Reference proteome; Secreted;
Serine protease; Signal; Zymogen.
SIGNAL 1 18 {ECO:0000255}.
PROPEP 19 28 Activation peptide.
{ECO:0000269|PubMed:1314562,
ECO:0000269|PubMed:2036367}.
/FTId=PRO_0000027496.
CHAIN 29 273 Tryptase.
/FTId=PRO_0000027497.
DOMAIN 29 270 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 72 72 Charge relay system. {ECO:0000250}.
ACT_SITE 119 119 Charge relay system. {ECO:0000250}.
ACT_SITE 222 222 Charge relay system. {ECO:0000250}.
CARBOHYD 49 49 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
DISULFID 57 73 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 153 228 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 186 209 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 218 246 {ECO:0000255|PROSITE-ProRule:PRU00274}.
CONFLICT 42 42 W -> V (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 49 51 NDT -> WLP (in Ref. 3; AA sequence).
{ECO:0000305}.
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


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