Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P50343

- TRYB2_RAT

UniProt

P50343 - TRYB2_RAT

Protein

Tryptase beta-2

Gene

Tpsb2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.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

    1. serine-type endopeptidase activity Source: InterPro

    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

    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

    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.
    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

    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

    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:
    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: October 1, 2014
    This is version 100 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