[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; DOI=10.1084/jem.185.1.13; PubMed=8996238 [NCBI, ExPASy, EBI, Israel, Japan] Lutzelschwab C., Pejler G., Aveskogh M., Hellman L.; "Secretory granule proteases in rat mast cells. Cloning of 10 different serine proteases and a carboxypeptidase A from various rat mast cell populations."; J. Exp. Med. 185:13-29(1997).
[2]	PROTEIN SEQUENCE OF 29-53. STRAIN=Sprague-Dawley; TISSUE=Skin; DOI=10.1021/bi00234a023; PubMed=2036367 [NCBI, ExPASy, EBI, Israel, Japan] Braganza V.J., Simmons W.H.; "Tryptase from rat skin: purification and properties."; Biochemistry 30:4997-5007(1991).
[3]	PROTEIN SEQUENCE OF 29-51. TISSUE=Mammary carcinoma; PubMed=1314562 [NCBI, ExPASy, EBI, Israel, Japan] Eto I., Grubbs C.J.; "Separation, purification and N-terminal sequence analysis of a novel leupeptin-sensitive serine endopeptidase present in chemically induced rat mammary tumour."; Biochem. J. 283:209-216(1992).

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: Homotetramer.
SUBCELLULAR LOCATION: Secreted. Note=Released from the secretory granules upon mast cell activation.
TISSUE SPECIFICITY: Mast cells.
PTM: Glycosylated (Probable).
SIMILARITY: Belongs to the peptidase S1 family. Tryptase subfamily [view classification].
SIMILARITY: Contains 1 peptidase S1 domain [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U67910; AAB48263.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A23698; A23698.
S21275; S21275.

RefSeq

NP_062195.2; -.

UniGene

Rn.10699

3D structure databases

HSSP

P20231; 1A0L. [HSSP ENTRY / PDB]

SMR

P27435; 29-271.

ModBase

P27435.

Protein family/group databases

MEROPS

S01.026; -.

Organism-specific databases

RGD

3066; Tpsab1.

Gene expression databases

ArrayExpress

P27435; -.

GermOnline

ENSRNOG00000024181; Rattus norvegicus.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.

Pfam

PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00722; CHYMOTRYPSIN.

SMART

SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSRNOG00000024181; Rattus norvegicus. [Contig view]

GeneID

54271; -.

KEGG

rno:54271; -.

Phylogenomic databases

HOVERGEN

P27435; -.

Other

NextBio

610832; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Glycoprotein; Hydrolase; Protease; Secreted; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`	`Potential.`
`PROPEP`	`19 28`	`10`	`Activation peptide.`	`PRO_0000027496`
`CHAIN`	`29 273`	`245`	`Tryptase.`	`PRO_0000027497`
`DOMAIN`	`29 270`	`242`	`Peptidase S1.`
`ACT_SITE`	`72 72`		`Charge relay system (By similarity).`
`ACT_SITE`	`119 119`		`Charge relay system (By similarity).`
`ACT_SITE`	`222 222`		`Charge relay system (By similarity).`
`CARBOHYD`	`49 49`		`N-linked (GlcNAc...) (Probable).`
`DISULFID`	`57 73`		`By similarity.`
`DISULFID`	`153 228`		`By similarity.`
`DISULFID`	`186 209`		`By similarity.`
`DISULFID`	`218 246`		`By similarity.`
`CONFLICT`	`42 42`		`W -> V (in Ref. 3; AA sequence).`
`CONFLICT`	`49 51`		`NDT -> WLP (in Ref. 3; AA sequence).`

Sequence information

Length: 273 AA [This is the length of the unprocessed precursor]

Molecular weight: 30400 Da [This is the MW of the unprocessed precursor]

CRC64: 65A5ED4D279FB284 [This is a checksum on the sequence]

        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

P27435 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools