SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P50343

- TRYB2_RAT

UniProt

P50343 - TRYB2_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Tryptase beta-2

Gene
Tpsb2, Mcp6, Mcpt6
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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. Has an immunoprotective role during bacterial infection. Required to efficiently combat K.pneumoniae infection 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 system By similarity
Active sitei120 – 1201Charge relay system By similarity
Active sitei223 – 2231Charge relay system By similarity

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro
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: 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

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi58 ↔ 74 By similarity
Modified residuei96 – 961Phosphotyrosine By similarity
Glycosylationi104 – 1041N-linked (GlcNAc...) Reviewed prediction
Glycosylationi131 – 1311N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi154 ↔ 229 By similarity
Disulfide bondi187 ↔ 210 By similarity
Disulfide bondi219 ↔ 247 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

PaxDbiP50343.
PRIDEiP50343.

PTM databases

PhosphoSiteiP50343.

Expressioni

Gene expression databases

GenevestigatoriP50343.

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 271242Peptidase S1Add
BLAST

Sequence similaritiesi

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

MLKLLLLLAL SPLASLVHAA PCPVKQRVGI VGGREASESK WPWQVSLRFK    50
FSFWMHFCGG SLIHPQWVLT AAHCVGLHIK SPELFRVQLR EQYLYYADQL 100
LTVNRTVVHP HYYTVEDGAD IALLELEIPV NVSTHIHPIS LPPASETFPS 150
GTSCWVTGWG DIDSDEPLLP PYPLKQVKVP IVENSLCDRK YHTGLYTGDD 200
VPIVQDGMLC AGNTRSDSCQ GDSGGPLVCK VKGTWLQAGV VSWGEGCAEA 250
NRPGIYTRVT YYLDWIHRYV PQRS 274
Length:274
Mass (Da):30,508
Last modified:October 1, 1996 - v1
Checksum:iDF84D55668CA1A25
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti128 – 1281I → N in AAB48262. 1 Publication
Sequence conflicti139 – 1391I → T in AAB48262. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
D38455 mRNA. Translation: BAA07486.1 .
U67909 mRNA. Translation: AAB48262.1 .
PIRi JC4171.
RefSeqi NP_062053.2. NM_019180.2.
UniGenei Rn.10183.

3D structure databases

ProteinModelPortali P50343.
SMRi P50343. Positions 30-273.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000025220.

Protein family/group databases

MEROPSi S01.025.

PTM databases

PhosphoSitei P50343.

Proteomic databases

PaxDbi P50343.
PRIDEi P50343.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 29268.
KEGGi rno:29268.
UCSCi RGD:3065. rat.

Organism-specific databases

CTDi 64499.
RGDi 3065. Tpsb2.

Phylogenomic databases

eggNOGi COG5640.
HOGENOMi HOG000251820.
HOVERGENi HBG013304.
InParanoidi P50343.
KOi K01340.
PhylomeDBi P50343.

Miscellaneous databases

NextBioi 608608.

Gene expression databases

Genevestigatori P50343.

Family and domain databases

InterProi IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: May 14, 2014
This is version 99 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