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Protein

Tryptase beta-2

Gene

Tpsb2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei73 – 731Charge relay systemBy similarity
Active sitei120 – 1201Charge relay systemBy similarity
Active sitei223 – 2231Charge relay systemBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3065. Tpsb2.

Subcellular locationi

  • Secreted By similarity

  • Note: Released from the secretory granules upon mast cell activation.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Propeptidei20 – 2910Activation peptidePRO_0000027492
Chaini30 – 274245Tryptase beta-2PRO_0000027493Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi58 ↔ 74PROSITE-ProRule annotation
Modified residuei96 – 961PhosphotyrosineBy similarity
Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi131 – 1311N-linked (GlcNAc...)Sequence Analysis
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

PhosphoSiteiP50343.

Expressioni

Gene expression databases

GenevisibleiP50343. RN.

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. Positions 30-273.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 271242Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family. Tryptase subfamily.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP50343.
KOiK01340.
PhylomeDBiP50343.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti128 – 1281I → N in AAB48262 (PubMed:8996238).Curated
Sequence conflicti139 – 1391I → T in AAB48262 (PubMed:8996238).Curated

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP50343.
SMRiP50343. Positions 30-273.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025220.

Protein family/group databases

MEROPSiS01.025.

PTM databases

PhosphoSiteiP50343.

Proteomic databases

PaxDbiP50343.
PRIDEiP50343.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29268.
KEGGirno:29268.
UCSCiRGD:3065. rat.

Organism-specific databases

CTDi64499.
RGDi3065. Tpsb2.

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP50343.
KOiK01340.
PhylomeDBiP50343.

Miscellaneous databases

NextBioi608608.
PROiP50343.

Gene expression databases

GenevisibleiP50343. RN.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "cDNA sequencing and expression of rat mast cell tryptase."
    Ide H., Itoh H., Tomita M., Murakumo Y., Kobayashi T., Maruyama H., Osada Y., Nawa Y.
    J. Biochem. 118:210-215(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Peritoneal mast cell.
  2. "Secretory granule proteases in rat mast cells. Cloning of 10 different serine proteases and a carboxypeptidase A from various rat mast cell populations."
    Lutzelschwab C., Pejler G., Aveskogh M., Hellman L.
    J. Exp. Med. 185:13-29(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Peritoneal mast cell.

Entry informationi

Entry nameiTRYB2_RAT
AccessioniPrimary (citable) accession number: P50343
Secondary accession number(s): P97593
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.