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Protein

Tryptase alpha/beta-1

Gene

TPSAB1

Organism
Homo sapiens (Human)
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. Isoform 2 cleaves large substrates, such as fibronectin, more efficiently than isoform 1, but seems less efficient toward small substrates (PubMed:18854315).By similarity1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei74Charge relay system1
Active sitei121Charge relay system1
Active sitei224Charge relay system1

GO - Molecular functioni

  • serine-type endopeptidase activity Source: UniProtKB
  • serine-type peptidase activity Source: ProtInc

GO - Biological processi

  • defense response Source: ProtInc
  • extracellular matrix disassembly Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.21.59. 2681.
ReactomeiR-HSA-1592389. Activation of Matrix Metalloproteinases.

Protein family/group databases

MEROPSiS01.143.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptase alpha/beta-1 (EC:3.4.21.59)
Short name:
Tryptase-1
Alternative name(s):
Tryptase I
Tryptase alpha-1
Gene namesi
Name:TPSAB1
Synonyms:TPS1, TPS2, TPSB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:12019. TPSAB1.

Subcellular locationi

  • Secreted

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

GO - Cellular componenti

  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi64499.
7177.
OpenTargetsiENSG00000172236.
PharmGKBiPA36698.

Chemistry databases

ChEMBLiCHEMBL2617.
GuidetoPHARMACOLOGYi2424.

Polymorphism and mutation databases

DMDMi18202508.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
PropeptideiPRO_000002747919 – 30Activation peptideBy similarityAdd BLAST12
ChainiPRO_000002748031 – 275Tryptase alpha/beta-1Add BLAST245

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi59 ↔ 75
Glycosylationi132N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi155 ↔ 230
Disulfide bondi188 ↔ 211
Disulfide bondi220 ↔ 248
Glycosylationi233N-linked (GlcNAc...)1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ15661.
PeptideAtlasiQ15661.
PRIDEiQ15661.

PTM databases

iPTMnetiQ15661.
PhosphoSitePlusiQ15661.

Expressioni

Tissue specificityi

Isoform 1 and isoform 2 are expressed in lung, stomach, spleen, heart and skin; in these tissues, isoform 1 is predominant. Isoform 2 is expressed in aorta, spleen, and breast tumor, with highest levels in the endothelial cells of some blood vessels surrounding the aorta, as well as those surrounding the tumor and low levels, if any, in mast cells (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000172236.
CleanExiHS_TPSAB1.
ExpressionAtlasiQ15661. baseline and differential.
GenevisibleiQ15661. HS.

Organism-specific databases

HPAiCAB016369.
CAB022175.
HPA049153.
HPA049554.

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 SERPINB6.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163332EBI-1761369,EBI-389883
PIK3R1P279862EBI-1761369,EBI-79464

Protein-protein interaction databases

BioGridi113029. 2 interactors.
IntActiQ15661. 2 interactors.
STRINGi9606.ENSP00000343577.

Chemistry databases

BindingDBiQ15661.

Structurei

Secondary structure

1275
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 36Combined sources5
Beta strandi45 – 65Combined sources21
Beta strandi68 – 71Combined sources4
Helixi73 – 76Combined sources4
Helixi83 – 85Combined sources3
Beta strandi86 – 89Combined sources4
Turni95 – 98Combined sources4
Beta strandi104 – 109Combined sources6
Turni116 – 118Combined sources3
Beta strandi123 – 129Combined sources7
Beta strandi135 – 137Combined sources3
Beta strandi155 – 160Combined sources6
Beta strandi176 – 179Combined sources4
Helixi185 – 193Combined sources9
Beta strandi196 – 198Combined sources3
Beta strandi209 – 212Combined sources4
Beta strandi215 – 218Combined sources4
Turni221 – 225Combined sources5
Beta strandi227 – 232Combined sources6
Beta strandi235 – 244Combined sources10
Beta strandi246 – 250Combined sources5
Beta strandi255 – 259Combined sources5
Helixi260 – 263Combined sources4
Helixi264 – 270Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LTOX-ray2.20A/B/C/D31-275[»]
2F9NX-ray1.60A/B/C/D31-275[»]
2F9OX-ray2.10A/B/C/D31-275[»]
2F9PX-ray2.30A/B/C/D31-275[»]
2ZEBX-ray2.50A/B/C/D31-273[»]
2ZECX-ray2.06A/B/C/D31-273[»]
4A6LX-ray2.05A/B/C/D31-275[»]
4MPUX-ray1.65A/B31-275[»]
4MPVX-ray2.31A/B31-275[»]
4MPWX-ray1.95A/B31-275[»]
4MPXX-ray2.00A/B31-275[»]
4MQAX-ray2.25A/B31-275[»]
5F03X-ray1.94A/B31-275[»]
ProteinModelPortaliQ15661.
SMRiQ15661.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15661.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 272Peptidase 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.
GeneTreeiENSGT00760000118810.
HOVERGENiHBG013304.
InParanoidiQ15661.
KOiK01340.
PhylomeDBiQ15661.
TreeFamiTF351676.

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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15661-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLNLLLLALP VLASRAYAAP APGQALQRVG IVGGQEAPRS KWPWQVSLRV
60 70 80 90 100
HGPYWMHFCG GSLIHPQWVL TAAHCVGPDV KDLAALRVQL REQHLYYQDQ
110 120 130 140 150
LLPVSRIIVH PQFYTAQIGA DIALLELEEP VNVSSHVHTV TLPPASETFP
160 170 180 190 200
PGMPCWVTGW GDVDNDERLP PPFPLKQVKV PIMENHICDA KYHLGAYTGD
210 220 230 240 250
DVRIVRDDML CAGNTRRDSC QGDSGGPLVC KVNGTWLQAG VVSWGEGCAQ
260 270
PNRPGIYTRV TYYLDWIHHY VPKKP
Length:275
Mass (Da):30,515
Last modified:November 1, 1996 - v1
Checksum:iADC48FDC51F37112
GO
Isoform 2 (identifier: Q15661-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     79-87: Missing.

Show »
Length:266
Mass (Da):29,533
Checksum:i04F79FEB4ABF517D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti129E → K in ACZ98912 (PubMed:19748655).Curated1

Polymorphismi

There are two alleles alpha and beta-I. The sequence shown is that of allele beta-I.3 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0642773N → S in allele alpha. Corresponds to variant rs371929937dbSNPEnsembl.1
Natural variantiVAR_06427815R → P.3 PublicationsCorresponds to variant rs61729112dbSNPEnsembl.1
Natural variantiVAR_01455718A → V.1 PublicationCorresponds to variant rs1800984dbSNPEnsembl.1
Natural variantiVAR_01455823G → V in allele alpha. 1 PublicationCorresponds to variant rs1141965dbSNPEnsembl.1
Natural variantiVAR_06427928R → Q in allele alpha. Corresponds to variant rs1064770dbSNPEnsembl.1
Natural variantiVAR_06428029V → A in allele alpha. Corresponds to variant rs1064771dbSNPEnsembl.1
Natural variantiVAR_06428151H → R in allele alpha. Corresponds to variant rs1060281dbSNPEnsembl.1
Natural variantiVAR_06428252G → D in allele alpha. Corresponds to variant rs17841227dbSNPEnsembl.1
Natural variantiVAR_06428353P → R in allele alpha. Corresponds to variant rs17841226dbSNPEnsembl.1
Natural variantiVAR_06428476V → L in allele alpha. Corresponds to variant rs71384640dbSNPEnsembl.1
Natural variantiVAR_01455985A → T.3 PublicationsCorresponds to variant rs1141968dbSNPEnsembl.1
Natural variantiVAR_064285115T → I in allele alpha. Corresponds to variant rs1064774dbSNPEnsembl.1
Natural variantiVAR_064286116A → I in allele alpha; requires 2 nucleotide substitutions. 1
Natural variantiVAR_064287118I → T in allele alpha. Corresponds to variant rs71376589dbSNPEnsembl.1
Natural variantiVAR_016102132N → K.2 PublicationsCorresponds to variant rs1800991dbSNPEnsembl.1
Natural variantiVAR_064288133V → I in allele alpha. Corresponds to variant rs1064779dbSNPEnsembl.1
Natural variantiVAR_051830136H → R in allele alpha. Corresponds to variant rs1064780dbSNPEnsembl.1
Natural variantiVAR_014560141T → A.1 PublicationCorresponds to variant rs1800992dbSNPEnsembl.1
Natural variantiVAR_064289141T → M in allele alpha. 1
Natural variantiVAR_014561162D → N.1 PublicationCorresponds to variant rs2234641dbSNPEnsembl.1
Natural variantiVAR_064290168R → P in allele alpha. Corresponds to variant rs1141969dbSNPEnsembl.1
Natural variantiVAR_014562170P → S.2 PublicationsCorresponds to variant rs2234904dbSNPEnsembl.1
Natural variantiVAR_064291205V → I in allele alpha. Corresponds to variant rs1060284dbSNPEnsembl.1
Natural variantiVAR_014563215T → S.3 PublicationsCorresponds to variant rs2234905dbSNPEnsembl.1
Natural variantiVAR_014564216R → Q.3 PublicationsCorresponds to variant rs2234906dbSNPEnsembl.1
Natural variantiVAR_064292221Q → K.3 PublicationsCorresponds to variant rs17841224dbSNPEnsembl.1
Natural variantiVAR_064293245G → D in allele alpha. Corresponds to variant rs1060292dbSNPEnsembl.1
Natural variantiVAR_064294263Y → N.1 PublicationCorresponds to variant rs2234646dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00537579 – 87Missing in isoform 2. Curated9

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30038 mRNA. Translation: AAA86934.1.
M33494 Genomic DNA. Translation: AAC83172.1.
M33491 mRNA. Translation: AAA36778.1.
AF098328 Genomic DNA. Translation: AAD17846.1.
AF099144 Genomic DNA. Translation: AAD17860.1.
AF206665 mRNA. Translation: AAG35695.1.
AF206666 mRNA. Translation: AAG35696.1.
AF206667 mRNA. Translation: AAG35697.1.
FJ931116 Genomic DNA. Translation: ACZ98910.1.
FJ931118 mRNA. Translation: ACZ98912.1.
AC120498 Genomic DNA. No translation available.
BC074974 mRNA. Translation: AAH74974.1.
CCDSiCCDS10431.1. [Q15661-1]
PIRiA35863.
A45754.
C35863.
RefSeqiNP_003285.2. NM_003294.3. [Q15661-1]
UniGeneiHs.405479.
Hs.592982.

Genome annotation databases

EnsembliENST00000338844; ENSP00000343577; ENSG00000172236. [Q15661-1]
GeneIDi7177.
KEGGihsa:7177.
UCSCiuc002ckz.4. human. [Q15661-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30038 mRNA. Translation: AAA86934.1.
M33494 Genomic DNA. Translation: AAC83172.1.
M33491 mRNA. Translation: AAA36778.1.
AF098328 Genomic DNA. Translation: AAD17846.1.
AF099144 Genomic DNA. Translation: AAD17860.1.
AF206665 mRNA. Translation: AAG35695.1.
AF206666 mRNA. Translation: AAG35696.1.
AF206667 mRNA. Translation: AAG35697.1.
FJ931116 Genomic DNA. Translation: ACZ98910.1.
FJ931118 mRNA. Translation: ACZ98912.1.
AC120498 Genomic DNA. No translation available.
BC074974 mRNA. Translation: AAH74974.1.
CCDSiCCDS10431.1. [Q15661-1]
PIRiA35863.
A45754.
C35863.
RefSeqiNP_003285.2. NM_003294.3. [Q15661-1]
UniGeneiHs.405479.
Hs.592982.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LTOX-ray2.20A/B/C/D31-275[»]
2F9NX-ray1.60A/B/C/D31-275[»]
2F9OX-ray2.10A/B/C/D31-275[»]
2F9PX-ray2.30A/B/C/D31-275[»]
2ZEBX-ray2.50A/B/C/D31-273[»]
2ZECX-ray2.06A/B/C/D31-273[»]
4A6LX-ray2.05A/B/C/D31-275[»]
4MPUX-ray1.65A/B31-275[»]
4MPVX-ray2.31A/B31-275[»]
4MPWX-ray1.95A/B31-275[»]
4MPXX-ray2.00A/B31-275[»]
4MQAX-ray2.25A/B31-275[»]
5F03X-ray1.94A/B31-275[»]
ProteinModelPortaliQ15661.
SMRiQ15661.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113029. 2 interactors.
IntActiQ15661. 2 interactors.
STRINGi9606.ENSP00000343577.

Chemistry databases

BindingDBiQ15661.
ChEMBLiCHEMBL2617.
GuidetoPHARMACOLOGYi2424.

Protein family/group databases

MEROPSiS01.143.

PTM databases

iPTMnetiQ15661.
PhosphoSitePlusiQ15661.

Polymorphism and mutation databases

DMDMi18202508.

Proteomic databases

PaxDbiQ15661.
PeptideAtlasiQ15661.
PRIDEiQ15661.

Protocols and materials databases

DNASUi7177.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338844; ENSP00000343577; ENSG00000172236. [Q15661-1]
GeneIDi7177.
KEGGihsa:7177.
UCSCiuc002ckz.4. human. [Q15661-1]

Organism-specific databases

CTDi7177.
DisGeNETi64499.
7177.
GeneCardsiTPSAB1.
H-InvDBHIX0012676.
HGNCiHGNC:12019. TPSAB1.
HPAiCAB016369.
CAB022175.
HPA049153.
HPA049554.
MIMi191080. gene.
neXtProtiNX_Q15661.
OpenTargetsiENSG00000172236.
PharmGKBiPA36698.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118810.
HOVERGENiHBG013304.
InParanoidiQ15661.
KOiK01340.
PhylomeDBiQ15661.
TreeFamiTF351676.

Enzyme and pathway databases

BRENDAi3.4.21.59. 2681.
ReactomeiR-HSA-1592389. Activation of Matrix Metalloproteinases.

Miscellaneous databases

ChiTaRSiTPSAB1. human.
EvolutionaryTraceiQ15661.
GenomeRNAii7177.
PROiQ15661.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000172236.
CleanExiHS_TPSAB1.
ExpressionAtlasiQ15661. baseline and differential.
GenevisibleiQ15661. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: Q15661
Secondary accession number(s): D2E6R9
, D2E6S1, P15157, Q15663, Q6B052, Q9H2Y4, Q9H2Y5, Q9UQI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. 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.