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P27435 (TRYB1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Tpsab1
Synonyms:Mcp7, Mcpt7, Tpsb1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length273 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.

Tissue specificity

Mast cells.

Post-translational modification

Glycosylated Probable.

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
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   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
PRO_0000027496
Chain29 – 273245Tryptase
PRO_0000027497

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

Glycosylation491N-linked (GlcNAc...) Probable
Disulfide bond57 ↔ 73 By similarity
Disulfide bond153 ↔ 228 By similarity
Disulfide bond186 ↔ 209 By similarity
Disulfide bond218 ↔ 246 By similarity

Experimental info

Sequence conflict421W → V AA sequence Ref.3
Sequence conflict49 – 513NDT → WLP AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P27435 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 65A5ED4D279FB284

FASTA27330,400
        10         20         30         40         50         60 
MLKLLLLTLP LLSSLVHAAP SLAMPREGIV GGQEASGNKW PWQVSLRVND TYWMHFCGGS 

        70         80         90        100        110        120 
LIHPQWVLTA AHCVGPNKAD PNKLRVQLRK QYLYYHDHLL TVSQIISHPD FYIAQDGADI 

       130        140        150        160        170        180 
ALLKLTNPVN ITSNVHTVSL PPASETFPSG TLCWVTGWGN INNDVSLPPP FPLEEVQVPI 

       190        200        210        220        230        240 
VENRLCDLKY HKGLNTGDNV HIVRDDMLCA GNEGHDSCQG DSGGPLVCKV EDTWLQAGVV 

       250        260        270 
SWGEGCAQPN RPGIYTRVTY YLDWIYRYVP KYF 

« Hide

References

[1]"Secretory granule proteases in rat mast cells. Cloning of 10 different serine proteases and a carboxypeptidase A from various rat mast cell populations."
Lutzelschwab C., Pejler G., Aveskogh M., Hellman L.
J. Exp. Med. 185:13-29(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
[2]"Tryptase from rat skin: purification and properties."
Braganza V.J., Simmons W.H.
Biochemistry 30:4997-5007(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-53.
Strain: Sprague-Dawley.
Tissue: Skin.
[3]"Separation, purification and N-terminal sequence analysis of a novel leupeptin-sensitive serine endopeptidase present in chemically induced rat mammary tumour."
Eto I., Grubbs C.J.
Biochem. J. 283:209-216(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-51.
Tissue: Mammary carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U67910 mRNA. Translation: AAB48263.1.
PIRA23698.
S21275.
RefSeqNP_062195.2. NM_019322.2.
UniGeneRn.10699.

3D structure databases

ProteinModelPortalP27435.
SMRP27435. Positions 29-271.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP27435.
ChEMBLCHEMBL3320.

Protein family/group databases

MEROPSS01.026.

Proteomic databases

PaxDbP27435.
PRIDEP27435.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID54271.
KEGGrno:54271.
UCSCRGD:3066. rat.

Organism-specific databases

CTD7177.
RGD3066. Tpsab1.

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
HOVERGENHBG013304.
InParanoidP27435.
KOK01340.
PhylomeDBP27435.

Gene expression databases

GenevestigatorP27435.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio610832.

Entry information

Entry nameTRYB1_RAT
AccessionPrimary (citable) accession number: P27435
Secondary accession number(s): P27436
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries