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Reviewed, UniProtKB/Swiss-Prot Q9XSM2 (TRYT_SHEEP)

Last modified June 16, 2009. Version 52. 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-2
    EC=3.4.21.59
OrganismOvis aries (Sheep)
Taxonomic identifier9940 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis

Protein attributes

Sequence length273 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 – 1818 Potential
Propeptide19 – 2810Activation peptide By similarity
PRO_0000027488
Chain29 – 273245Tryptase-2
PRO_0000027489

Regions

Domain29 – 270242Peptidase S1

Sites

Active site721Charge relay system By similarity
Active site1191Charge relay system By similarity
Active site2221Charge relay system By similarity

Amino acid modifications

Glycosylation2311N-linked (GlcNAc...) Potential
Disulfide bond57 ↔ 73 By similarity
Disulfide bond153 ↔ 228 By similarity
Disulfide bond186 ↔ 209 By similarity
Disulfide bond218 ↔ 246 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9XSM2-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: DE9BA79218C3E67D

FASTA27330,288
        10         20         30         40         50         60 
MLHLLALALL LSLVSAAPAP GQALQRSGII GGKEAPGSRW PWQVSLRVRD QYWRHQCGGS 

        70         80         90        100        110        120 
LIHPQWVLTA AHCIGPELQE PSDFRVQLRE QHLYYQDRLL PISRVIPHPH YYMVENGADI 

       130        140        150        160        170        180 
ALLQLEEPVS ISRHVQPVTL PPASETFPPE SQCWVTGWGD VDNGRPLPPP YPLKQVKVPI 

       190        200        210        220        230        240 
VENSVCDWKY HSGLSTDYSV PIVQEDNLCA GDGGRDSCQG DSGGPLVCKV NGTWLQAGVV 

       250        260        270 
SWGDGCAKPN RPGIYTRITS YLDWIHQYVP QEP 

« Hide

References

[1]"cDNA sequence of two sheep mast cell tryptases and the differential expression of tryptase and sheep mast cell proteinase-1 in lung, dermis and gastrointestinal tract."
Pemberton A.D., McAleese S.M., Huntley J.F., Collie D.D.S., Scudamore C.L., McEuen A.R., Walls A.F., Miller H.R.P.
Clin. Exp. Allergy 30:818-832(2000) [PubMed: 10848900] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Abomasum.

Cross-references

Sequence databases

Y18224 mRNA. Translation: CAB41989.1.
RefSeqNP_001116478.1.
UniGeneOar.751

3D structure databases

HSSPHSSP built from PDB template 1EZX based on UniProtKB P00760.
SMRQ9XSM2. Positions 29-271.
ModBaseSearch...

Protein family/group databases

MEROPSS01.118.

Genome annotation databases

GeneID100144429.

Phylogenomic databases

HOVERGENQ9XSM2.

Enzyme and pathway databases

BRENDA3.4.21.59. 271.

Family and domain databases

InterProIPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[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_SHEEP
AccessionPrimary (citable) accession number: Q9XSM2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: November 1, 1999
Last modified: June 16, 2009
This is version 52 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