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Protein

Tryptase beta-2

Gene

Tpsb2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. Plays a role in innate immunity.By similarity

Catalytic activityi

Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more restricted specificity than trypsin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei73Charge relay systemBy similarity1
Active sitei120Charge relay systemBy similarity1
Active sitei223Charge relay systemBy similarity1

GO - Molecular functioni

Keywordsi

Molecular functionHydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.025

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptase beta-2 (EC:3.4.21.59)
Short name:
Tryptase-2
Alternative name(s):
Mast cell protease 6
Short name:
rMCP-6
Gene namesi
Name:Tpsb2
Synonyms:Mcp6, Mcpt6
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3065 Tpsb2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
PropeptideiPRO_000002749220 – 29Activation peptide10
ChainiPRO_000002749330 – 274Tryptase beta-2Add BLAST245

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi58 ↔ 74PROSITE-ProRule annotation
Modified residuei96PhosphotyrosineBy similarity1
Glycosylationi104N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi131N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi154 ↔ 229PROSITE-ProRule annotation
Disulfide bondi187 ↔ 210PROSITE-ProRule annotation
Disulfide bondi219 ↔ 247PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

PaxDbiP50343
PRIDEiP50343

PTM databases

PhosphoSitePlusiP50343

Interactioni

Subunit structurei

Homotetramer. The active tetramer is converted to inactive monomers at neutral and acidic pH in the absence of heparin. Low concentrations of inactive monomers become active monomers at pH 6.0 in the presence of heparin. When the concentration of active monomers is higher, they convert to active monomers and then to active tetramers. These monomers are active and functionally distinct from the tetrameric enzyme. In contrast to the hidden active sites in the tetrameric form, the active site of the monomeric form is accessible for macromolecular proteins and inhibitors eg: fibrinogen which is a substrate for the monomeric but not for the tetrameric form. The monomeric form forms a complex with SERPINB6.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025220

Structurei

3D structure databases

ProteinModelPortaliP50343
SMRiP50343
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 271Peptidase S1PROSITE-ProRule annotationAdd BLAST242

Sequence similaritiesi

Belongs to the peptidase S1 family. Tryptase subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3627 Eukaryota
COG5640 LUCA
HOGENOMiHOG000251820
HOVERGENiHBG013304
InParanoidiP50343
KOiK01340
PhylomeDBiP50343

Family and domain databases

CDDicd00190 Tryp_SPc, 1 hit
InterProiView protein in InterPro
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF00089 Trypsin, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
SMARTiView protein in SMART
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
PROSITEiView protein in PROSITE
PS50240 TRYPSIN_DOM, 1 hit
PS00134 TRYPSIN_HIS, 1 hit
PS00135 TRYPSIN_SER, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P50343-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKLLLLLAL SPLASLVHAA PCPVKQRVGI VGGREASESK WPWQVSLRFK
60 70 80 90 100
FSFWMHFCGG SLIHPQWVLT AAHCVGLHIK SPELFRVQLR EQYLYYADQL
110 120 130 140 150
LTVNRTVVHP HYYTVEDGAD IALLELEIPV NVSTHIHPIS LPPASETFPS
160 170 180 190 200
GTSCWVTGWG DIDSDEPLLP PYPLKQVKVP IVENSLCDRK YHTGLYTGDD
210 220 230 240 250
VPIVQDGMLC AGNTRSDSCQ GDSGGPLVCK VKGTWLQAGV VSWGEGCAEA
260 270
NRPGIYTRVT YYLDWIHRYV PQRS
Length:274
Mass (Da):30,508
Last modified:October 1, 1996 - v1
Checksum:iDF84D55668CA1A25
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti128I → N in AAB48262 (PubMed:8996238).Curated1
Sequence conflicti139I → T in AAB48262 (PubMed:8996238).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38455 mRNA Translation: BAA07486.1
U67909 mRNA Translation: AAB48262.1
PIRiJC4171
RefSeqiNP_062053.2, NM_019180.2
UniGeneiRn.10183

Genome annotation databases

GeneIDi29268
KEGGirno:29268
UCSCiRGD:3065 rat

Similar proteinsi

Entry informationi

Entry nameiTRYB2_RAT
AccessioniPrimary (citable) accession number: P50343
Secondary accession number(s): P97593
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 23, 2018
This is version 120 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health