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Protein

Tryptase beta-2

Gene

Tpsb2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei75 – 751Charge relay systemBy similarity
Active sitei122 – 1221Charge relay systemBy similarity
Active sitei225 – 2251Charge relay systemBy similarity

GO - Molecular functioni

  • heparin binding Source: MGI
  • peptidase activity Source: MGI
  • serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  • inflammatory response Source: MGI
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:
mMCP-6
Gene namesi
Name:Tpsb2
Synonyms:Mcpt6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:96942. Tpsb2.

Subcellular locationi

  • Secreted By similarity

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

GO - Cellular componenti

  • extracellular region Source: MGI
  • extracellular space Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

Mutant mice do not exhibit any visible phenotype when maintained in pathogen-free facilities. However, after peritoneal inoculation of Klebsiella pneumoniae, they cannot efficiently fight the infection and show increased lethality.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Propeptidei22 – 3110Activation peptide1 PublicationPRO_0000027490
Chaini32 – 276245Tryptase beta-2PRO_0000027491Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi60 ↔ 76PROSITE-ProRule annotation
Modified residuei98 – 981PhosphotyrosineCombined sources
Glycosylationi133 – 1331N-linked (GlcNAc...)Sequence analysis
Disulfide bondi156 ↔ 231PROSITE-ProRule annotation
Disulfide bondi189 ↔ 212PROSITE-ProRule annotation
Disulfide bondi221 ↔ 249PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

MaxQBiP21845.
PaxDbiP21845.
PRIDEiP21845.

PTM databases

iPTMnetiP21845.
PhosphoSiteiP21845.

Expressioni

Tissue specificityi

During embryogenesis, detected primarily in skin.1 Publication

Developmental stagei

Not detected at early embryonic stages but is abundantly expressed in later stages with a peak at E17.5-E18.5.1 Publication

Gene expression databases

CleanExiMM_TPSB2.

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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000063499.

Structurei

3D structure databases

ProteinModelPortaliP21845.
SMRiP21845. Positions 32-273.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 273242Peptidase 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

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP21845.
PhylomeDBiP21845.

Family and domain databases

InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: P21845-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLKRRLLLLW ALSLLASLVY SAPRPANQRV GIVGGHEASE SKWPWQVSLR
60 70 80 90 100
FKLNYWIHFC GGSLIHPQWV LTAAHCVGPH IKSPQLFRVQ LREQYLYYGD
110 120 130 140 150
QLLSLNRIVV HPHYYTAEGG ADVALLELEV PVNVSTHIHP ISLPPASETF
160 170 180 190 200
PPGTSCWVTG WGDIDNDEPL PPPYPLKQVK VPIVENSLCD RKYHTGLYTG
210 220 230 240 250
DDFPIVHDGM LCAGNTRRDS CQGDSGGPLV CKVKGTWLQA GVVSWGEGCA
260 270
QPNKPGIYTR VTYYLDWIHR YVPEHS
Length:276
Mass (Da):30,927
Last modified:August 1, 1991 - v2
Checksum:i525B2C9A04A72200
GO
Isoform Short (identifier: P21845-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     223-230: GDSGGPLV → PFCIGDDI
     231-276: Missing.

Note: Probably non functional.
Show »
Length:230
Mass (Da):25,829
Checksum:i503F4E4477EA7073
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei223 – 2308GDSGGPLV → PFCIGDDI in isoform Short. 1 PublicationVSP_005376
Alternative sequencei231 – 27646Missing in isoform Short. 1 PublicationVSP_005377Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57626 mRNA. Translation: AAA39988.1.
M57625 mRNA. Translation: AAA39987.1.
L31853 mRNA. Translation: AAA39725.1.
X78542 mRNA. Translation: CAA55288.1.
BC024374 mRNA. Translation: AAH24374.1.
CCDSiCCDS28517.1. [P21845-1]
PIRiA38654.
I48685.
UniGeneiMm.7409.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57626 mRNA. Translation: AAA39988.1.
M57625 mRNA. Translation: AAA39987.1.
L31853 mRNA. Translation: AAA39725.1.
X78542 mRNA. Translation: CAA55288.1.
BC024374 mRNA. Translation: AAH24374.1.
CCDSiCCDS28517.1. [P21845-1]
PIRiA38654.
I48685.
UniGeneiMm.7409.

3D structure databases

ProteinModelPortaliP21845.
SMRiP21845. Positions 32-273.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000063499.

Protein family/group databases

MEROPSiS01.025.

PTM databases

iPTMnetiP21845.
PhosphoSiteiP21845.

Proteomic databases

MaxQBiP21845.
PaxDbiP21845.
PRIDEiP21845.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:96942. Tpsb2.

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP21845.
PhylomeDBiP21845.

Miscellaneous databases

PROiP21845.
SOURCEiSearch...

Gene expression databases

CleanExiMM_TPSB2.

Family and domain databases

InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[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

« Hide 'large scale' publications
  1. "Cloning of the cDNA and gene of mouse mast cell protease-6. Transcription by progenitor mast cells and mast cells of the connective tissue subclass."
    Reynolds D.S., Gurley D.S., Austen K.F., Serafin W.E.
    J. Biol. Chem. 266:3847-3853(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Expression of a mast cell tryptase in the human monocytic cell lines U-937 and Mono Mac 6."
    Huang R., Abrink M., Gobl A.E., Nilsson G., Aveskogh M., Larsson L.G., Nilsson K., Hellman L.
    Scand. J. Immunol. 38:359-367(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Leaden X A1.
  3. "Genes for mast-cell serine protease and their molecular evolution."
    Huang R., Hellman L.T.
    Immunogenetics 40:397-414(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
    Strain: Leaden X A1.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
    Strain: FVB/N.
    Tissue: Colon.
  5. "Different mouse mast cell populations express various combinations of at least six distinct mast cell serine proteases."
    Reynolds D.S., Stevens R.L., Lane W.S., Carr M.H., Austen K.F., Serafin W.E.
    Proc. Natl. Acad. Sci. U.S.A. 87:3230-3234(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 32-54.
  6. "The mast cell-restricted tryptase mMCP-6 has a critical immunoprotective role in bacterial infections."
    Thakurdas S.M., Melicoff E., Sansores-Garcia L., Moreira D.C., Petrova Y., Stevens R.L., Adachi R.
    J. Biol. Chem. 282:20809-20815(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  8. "The expression pattern of three mast cell specific proteases during mouse development."
    Abraham D., Oster H., Huber M., Leitges M.
    Mol. Immunol. 44:732-740(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiTRYB2_MOUSE
AccessioniPrimary (citable) accession number: P21845
Secondary accession number(s): Q61962
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: August 1, 1991
Last modified: May 11, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.