Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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. May play a role in innate immunity (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei72Charge relay systemBy similarity1
Active sitei119Charge relay systemBy similarity1
Active sitei222Charge relay systemBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.143.

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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3066. Tpsab1.

Subcellular locationi

  • Secreted

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3320.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
PropeptideiPRO_000002749619 – 28Activation peptide2 Publications10
ChainiPRO_000002749729 – 273TryptaseAdd BLAST245

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi49N-linked (GlcNAc...)Curated1
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.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025095.

Chemistry databases

BindingDBiP27435.

Structurei

3D structure databases

ProteinModelPortaliP27435.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini29 – 270Peptidase S1PROSITE-ProRule annotationAdd BLAST242

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

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP27435.
KOiK01340.
PhylomeDBiP27435.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[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:November 1, 1997 - v2
Checksum:i65A5ED4D279FB284
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti42W → V AA sequence (PubMed:1314562).Curated1
Sequence conflicti49 – 51NDT → WLP AA sequence (PubMed:1314562).Curated3

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025095.

Chemistry databases

BindingDBiP27435.
ChEMBLiCHEMBL3320.

Protein family/group databases

MEROPSiS01.143.

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

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP27435.
KOiK01340.
PhylomeDBiP27435.

Miscellaneous databases

PROiP27435.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[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...

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 5, 2016
This is version 130 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

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 one 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.