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Protein

Tryptase

Gene

Tpsab1

Organism
Rattus norvegicus (Rat)
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.

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
Complete GO annotation...

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 Componenti: 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
Complete GO annotation...

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

        10         20         30         40         50
MLKLLLLTLP LLSSLVHAAP SLAMPREGIV GGQEASGNKW PWQVSLRVND
60 70 80 90 100
TYWMHFCGGS LIHPQWVLTA AHCVGPNKAD PNKLRVQLRK QYLYYHDHLL
110 120 130 140 150
TVSQIISHPD FYIAQDGADI ALLKLTNPVN ITSNVHTVSL PPASETFPSG
160 170 180 190 200
TLCWVTGWGN INNDVSLPPP FPLEEVQVPI VENRLCDLKY HKGLNTGDNV
210 220 230 240 250
HIVRDDMLCA GNEGHDSCQG DSGGPLVCKV EDTWLQAGVV SWGEGCAQPN
260 270
RPGIYTRVTY YLDWIYRYVP KYF
Length:273
Mass (Da):30,400
Last modified:October 31, 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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
U67910 mRNA. Translation: AAB48263.1.
PIRiA23698.
S21275.
RefSeqiNP_062195.2. NM_019322.2.
UniGeneiRn.10699.

3D structure databases

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

Chemistry

BindingDBiP27435.
ChEMBLiCHEMBL3320.

Protein family/group databases

MEROPSiS01.026.

Proteomic databases

PaxDbiP27435.
PRIDEiP27435.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7177.
RGDi3066. Tpsab1.

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP27435.
KOiK01340.
PhylomeDBiP27435.

Miscellaneous databases

NextBioi610832.

Gene expression databases

GenevestigatoriP27435.

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]
ProtoNetiSearch...

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(1996) [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(1990) [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(1991) [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: July 31, 1992
Last sequence update: October 31, 1997
Last modified: March 31, 2015
This is version 118 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

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 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.