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P27435

- TRYB1_RAT

UniProt

P27435 - TRYB1_RAT

Protein

Tryptase

Gene

Tpsab1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei72 – 721Charge relay systemBy similarity
    Active sitei119 – 1191Charge relay systemBy similarity
    Active sitei222 – 2221Charge relay systemBy similarity

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS01.026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tryptase (EC:3.4.21.59)
    Alternative name(s):
    Mast cell protease 7
    Short name:
    rMCP-7
    Tryptase alpha/beta-1
    Tryptase, skin
    Gene namesi
    Name:Tpsab1
    Synonyms:Mcp7, Mcpt7, Tpsb1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3066. Tpsab1.

    Subcellular locationi

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

    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 – 1818Sequence AnalysisAdd
    BLAST
    Propeptidei19 – 2810Activation peptide2 PublicationsPRO_0000027496
    Chaini29 – 273245TryptasePRO_0000027497Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi49 – 491N-linked (GlcNAc...)Curated
    Disulfide bondi57 ↔ 73PROSITE-ProRule annotation
    Disulfide bondi153 ↔ 228PROSITE-ProRule annotation
    Disulfide bondi186 ↔ 209PROSITE-ProRule annotation
    Disulfide bondi218 ↔ 246PROSITE-ProRule annotation

    Post-translational modificationi

    Glycosylated.Curated

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiP27435.
    PRIDEiP27435.

    Expressioni

    Tissue specificityi

    Mast cells.

    Gene expression databases

    GenevestigatoriP27435.

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    3D structure databases

    ProteinModelPortaliP27435.
    SMRiP27435. Positions 29-271.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 270242Peptidase 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.
    InParanoidiP27435.
    KOiK01340.
    PhylomeDBiP27435.

    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.

    P27435-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLKLLLLTLP LLSSLVHAAP SLAMPREGIV GGQEASGNKW PWQVSLRVND    50
    TYWMHFCGGS LIHPQWVLTA AHCVGPNKAD PNKLRVQLRK QYLYYHDHLL 100
    TVSQIISHPD FYIAQDGADI ALLKLTNPVN ITSNVHTVSL PPASETFPSG 150
    TLCWVTGWGN INNDVSLPPP FPLEEVQVPI VENRLCDLKY HKGLNTGDNV 200
    HIVRDDMLCA GNEGHDSCQG DSGGPLVCKV EDTWLQAGVV SWGEGCAQPN 250
    RPGIYTRVTY YLDWIYRYVP KYF 273
    Length:273
    Mass (Da):30,400
    Last modified:November 1, 1997 - v2
    Checksum:i65A5ED4D279FB284
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti42 – 421W → V AA sequence (PubMed:1314562)Curated
    Sequence conflicti49 – 513NDT → WLP AA sequence (PubMed:1314562)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U67910 mRNA. Translation: AAB48263.1.
    PIRiA23698.
    S21275.
    RefSeqiNP_062195.2. NM_019322.2.
    UniGeneiRn.10699.

    Genome annotation databases

    GeneIDi54271.
    KEGGirno:54271.
    UCSCiRGD:3066. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U67910 mRNA. Translation: AAB48263.1 .
    PIRi A23698.
    S21275.
    RefSeqi NP_062195.2. NM_019322.2.
    UniGenei Rn.10699.

    3D structure databases

    ProteinModelPortali P27435.
    SMRi P27435. Positions 29-271.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P27435.
    ChEMBLi CHEMBL3320.

    Protein family/group databases

    MEROPSi S01.026.

    Proteomic databases

    PaxDbi P27435.
    PRIDEi P27435.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 54271.
    KEGGi rno:54271.
    UCSCi RGD:3066. rat.

    Organism-specific databases

    CTDi 7177.
    RGDi 3066. Tpsab1.

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000251820.
    HOVERGENi HBG013304.
    InParanoidi P27435.
    KOi K01340.
    PhylomeDBi P27435.

    Miscellaneous databases

    NextBioi 610832.

    Gene expression databases

    Genevestigatori P27435.

    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. "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.
    2. "Tryptase from rat skin: purification and properties."
      Braganza V.J., Simmons W.H.
      Biochemistry 30:4997-5007(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-53.
      Strain: Sprague-Dawley.
      Tissue: Skin.
    3. "Separation, purification and N-terminal sequence analysis of a novel leupeptin-sensitive serine endopeptidase present in chemically induced rat mammary tumour."
      Eto I., Grubbs C.J.
      Biochem. J. 283:209-216(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-51.
      Tissue: Mammary carcinoma.

    Entry informationi

    Entry nameiTRYB1_RAT
    AccessioniPrimary (citable) accession number: P27435
    Secondary accession number(s): P27436
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 114 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. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3