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Reviewed, UniProtKB/Swiss-Prot Q9N2D1 (TRYT_PIG)

Last modified November 24, 2009. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Tryptase
    EC=3.4.21.59
Gene names
Name: MCT7
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

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
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Zymogen
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 3010Activation peptide By similarity
PRO_0000027486
Chain31 – 275245Tryptase
PRO_0000027487

Regions

Domain31 – 272242Peptidase S1

Sites

Active site741Charge relay system By similarity
Active site1211Charge relay system By similarity
Active site2241Charge relay system By similarity

Amino acid modifications

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

Sequences

Sequence LengthMass (Da)Tools
Q9N2D1-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: ACC582647FCCB973

FASTA27530,439
        10         20         30         40         50         60 
MLNLLVLALP LLVSLVHTAP APGQALERAG IVGGKEAPGH KWPWQVSLRC LDQYWKHFCG 

        70         80         90        100        110        120 
GSLIHPQWVL TAAHCFGPEK ADPLYIRVQL GEQHLYYQDR LLLVSRIIVH PNYYDEVNGA 

       130        140        150        160        170        180 
DIALLELEDP VNLSSHVQPV TLPPASETFP KGTRCWVTGW GDVHSGWPLP PPYPLKQVRV 

       190        200        210        220        230        240 
PIVENSECDM QYHLGLSTGD NIPIVRDDML CAGSEGHDSC QGDSGGPLVC RVNGTWLQAG 

       250        260        270 
VVSWGEGCAL PNRPGIYTRV THYLDWIHQC IPRES 

« Hide

References

[1]"Mast cell tryptase from pig lungs triggers infection by pneumotropic Sendai and influenza A viruses. Purification and characterization."
Chen Y., Shiota M., Ohuchi M., Towatari T., Tashiro J., Murakami M., Yano M., Yang B., Kido H.
Eur. J. Biochem. 267:3189-3197(2000) [PubMed: 10824103] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB038652 mRNA. Translation: BAA93614.1.
RefSeqNP_999356.1.
UniGeneSsc.5614

3D structure databases

SMRQ9N2D1. Positions 31-273.
ModBaseSearch...

Protein family/group databases

MEROPSS01.118.

Genome annotation databases

GeneID397389.
KEGGssc:397389.

Organism-specific databases

CTD397389.

Phylogenomic databases

HOVERGENQ9N2D1.

Enzyme and pathway databases

BRENDA3.4.21.59. 249.

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...

Entry information

Entry nameTRYT_PIG
AccessionPrimary (citable) accession number: Q9N2D1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: October 1, 2000
Last modified: November 24, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents