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Reviewed, UniProtKB/Swiss-Prot P15157 (TRYA1_HUMAN)

Last modified January 19, 2010. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Tryptase alpha-1
      Short name=Tryptase-1
    EC=3.4.21.59
Gene names
Name: TPSAB1
Synonyms: TPS1, TPS2, TPSB1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Catalytic activity

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

Subunit structure

Homotetramer.

Subcellular location

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

Sequence similarities

Belongs to the peptidase S1 family. Tryptase subfamily.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processdefense response Ref.1

Traceable author statement. Source: ProtInc

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCK1P163331EBI-1762849,EBI-389883
PIK3R1P279861EBI-1762849,EBI-79464

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P15157-1)

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.
Isoform 2 (identifier: P15157-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 3012Activation peptide
PRO_0000027477
Chain31 – 275245Tryptase alpha-1
PRO_0000027478

Regions

Domain31 – 272242Peptidase S1

Sites

Active site741Charge relay system
Active site1211Charge relay system
Active site2241Charge relay system

Amino acid modifications

Glycosylation1321N-linked (GlcNAc...) Potential
Glycosylation2331N-linked (GlcNAc...) Potential
Disulfide bond59 ↔ 75
Disulfide bond155 ↔ 230
Disulfide bond188 ↔ 211
Disulfide bond220 ↔ 248

Natural variations

Alternative sequence79 – 879Missing in isoform 2.
VSP_005374
Natural variant151R → P in alpha-II.
VAR_012102
Natural variant2211K → Q in alpha-II. dbSNP rs1137382.
VAR_012103

Experimental info

Sequence conflict215 – 2162TR → SQ in AAA86934. Ref.1

Secondary structure

.......................................... 275
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 18, 2001. Version 3.
Checksum: B9BAC4BBCB91CE75

FASTA27530,773
        10         20         30         40         50         60 
MLSLLLLALP VLASRAYAAP APVQALQQAG IVGGQEAPRS KWPWQVSLRV RDRYWMHFCG 

        70         80         90        100        110        120 
GSLIHPQWVL TAAHCLGPDV KDLATLRVQL REQHLYYQDQ LLPVSRIIVH PQFYIIQTGA 

       130        140        150        160        170        180 
DIALLELEEP VNISSRVHTV MLPPASETFP PGMPCWVTGW GDVDNDEPLP PPFPLKQVKV 

       190        200        210        220        230        240 
PIMENHICDA KYHLGAYTGD DVRIIRDDML CAGNTRRDSC KGDSGGPLVC KVNGTWLQAG 

       250        260        270 
VVSWDEGCAQ PNRPGIYTRV TYYLDWIHHY VPKKP 

« Hide

Isoform 2.

Checksum: C3812E3A77A31257
Show »

FASTA26629,760

References

[1]"Cloning and characterization of complementary DNA for human tryptase."
Miller J.S., Westin E.H., Schwartz L.B.
J. Clin. Invest. 84:1188-1195(1989) [PubMed: 2677049] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Lung.
[2]Schwartz L.B.
Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 89-93 AND 108.
[3]"Characterization of genes encoding known and novel human mast cell tryptases on chromosome 16p13.3."
Pallaoro M., Fejzo M.S., Shayesteh L., Blount J.L., Caughey G.H.
J. Biol. Chem. 274:3355-3362(1999) [PubMed: 9920877] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Molecular cloning and characterization of novel human tryptase cDNAs and splicing variants."
Wang H.W., McNeil H.P., Thomas P.S., Murphy B.N., Webster M.J., Hettiaratchi A., King G., Heywood G.J., Huang C., Stevens R.L., Hunt J.E.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Lung.
[5]"Human pituitary tryptase: molecular forms, NH2-terminal sequence, immunocytochemical localization, and specificity with prohormone and fluorogenic substrates."
Cromlish J.A., Seidah N.G., Marcinkiewcz M., Hamelin J., Johnson D.A., Chretein M.
J. Biol. Chem. 262:1363-1373(1987) [PubMed: 3543004] [Abstract]
Cited for: PROTEIN SEQUENCE OF 31-50, PROTEIN SEQUENCE OF 31-38.
Tissue: Lung.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M30038 mRNA. Translation: AAA86934.1.
AF098328 Genomic DNA. Translation: AAD17846.1.
AF206665 mRNA. Translation: AAG35695.1.
AF206666 mRNA. Translation: AAG35696.1.
IPIIPI00010274.
IPI00219931.
PIRA45754.
UniGeneHs.405479

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP15157. 2 interactions.
STRINGP15157.

Protein family/group databases

MEROPSS01.143.

PTM databases

PhosphoSiteP15157.

Proteomic databases

PRIDEP15157.

Genome annotation databases

EnsemblENST00000338844; ENSP00000343577; ENSG00000172236; Homo sapiens. [Genome view]
ENST00000382804; ENSP00000372254; ENSG00000172236; Homo sapiens. [Genome view]
ENST00000461509; ENSP00000418247; ENSG00000172236; Homo sapiens. [Genome view]

Organism-specific databases

GeneCardsGC16P001233.
HGNCHGNC:12019. TPSAB1.
MIM191080. gene.
PharmGKBPA36698.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG05667.
HOVERGENP15157.
InParanoidP15157.

Enzyme and pathway databases

BRENDA3.4.21.59. 247.

Gene expression databases

CleanExHS_TPSAB1.
GenevestigatorP15157.
GermOnlineENSG00000197253. Homo sapiens.

Family and domain databases

InterProIPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
IPR009003. Ser/Cys_Pept_Trypsin-like.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameTRYA1_HUMAN
AccessionPrimary (citable) accession number: P15157
Secondary accession number(s): Q9H2Y5, Q9UQI1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 18, 2001
Last modified: January 19, 2010
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents