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P50343 (TRYB2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tryptase beta-2

Short name=Tryptase-2
EC=3.4.21.59
Alternative name(s):
Mast cell protease 6
Short name=rMCP-6
Gene names
Name:Tpsb2
Synonyms:Mcp6, Mcpt6
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length274 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. Has an immunoprotective role during bacterial infection. Required to efficiently combat K.pneumoniae infection By similarity.

Catalytic activity

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

Subunit structure

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.

Subcellular location

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

Sequence similarities

Belongs to the peptidase S1 family. Tryptase subfamily.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Propeptide20 – 2910Activation peptide
PRO_0000027492
Chain30 – 274245Tryptase beta-2
PRO_0000027493

Regions

Domain30 – 271242Peptidase S1

Sites

Active site731Charge relay system By similarity
Active site1201Charge relay system By similarity
Active site2231Charge relay system By similarity

Amino acid modifications

Modified residue961Phosphotyrosine By similarity
Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation1311N-linked (GlcNAc...) Potential
Disulfide bond58 ↔ 74 By similarity
Disulfide bond154 ↔ 229 By similarity
Disulfide bond187 ↔ 210 By similarity
Disulfide bond219 ↔ 247 By similarity

Experimental info

Sequence conflict1281I → N in AAB48262. Ref.2
Sequence conflict1391I → T in AAB48262. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P50343 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: DF84D55668CA1A25

FASTA27430,508
        10         20         30         40         50         60 
MLKLLLLLAL SPLASLVHAA PCPVKQRVGI VGGREASESK WPWQVSLRFK FSFWMHFCGG 

        70         80         90        100        110        120 
SLIHPQWVLT AAHCVGLHIK SPELFRVQLR EQYLYYADQL LTVNRTVVHP HYYTVEDGAD 

       130        140        150        160        170        180 
IALLELEIPV NVSTHIHPIS LPPASETFPS GTSCWVTGWG DIDSDEPLLP PYPLKQVKVP 

       190        200        210        220        230        240 
IVENSLCDRK YHTGLYTGDD VPIVQDGMLC AGNTRSDSCQ GDSGGPLVCK VKGTWLQAGV 

       250        260        270 
VSWGEGCAEA NRPGIYTRVT YYLDWIHRYV PQRS 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D38455 mRNA. Translation: BAA07486.1.
U67909 mRNA. Translation: AAB48262.1.
PIRJC4171.
RefSeqNP_062053.2. NM_019180.2.
UniGeneRn.10183.

3D structure databases

ProteinModelPortalP50343.
SMRP50343. Positions 30-273.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000025220.

Protein family/group databases

MEROPSS01.025.

PTM databases

PhosphoSiteP50343.

Proteomic databases

PaxDbP50343.
PRIDEP50343.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29268.
KEGGrno:29268.
UCSCRGD:3065. rat.

Organism-specific databases

CTD64499.
RGD3065. Tpsb2.

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
HOVERGENHBG013304.
InParanoidP50343.
KOK01340.
PhylomeDBP50343.

Gene expression databases

GenevestigatorP50343.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio608608.

Entry information

Entry nameTRYB2_RAT
AccessionPrimary (citable) accession number: P50343
Secondary accession number(s): P97593
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 14, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries