[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=1995638 [NCBI, ExPASy, EBI, Israel, Japan] Reynolds D.S., Gurley D.S., Austen K.F., Serafin W.E.; "Cloning of the cDNA and gene of mouse mast cell protease-6. Transcription by progenitor mast cells and mast cells of the connective tissue subclass."; J. Biol. Chem. 266:3847-3853(1991).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Leaden X A1; PubMed=8210998 [NCBI, ExPASy, EBI, Israel, Japan] Huang R., Abrink M., Gobl A.E., Nilsson G., Aveskogh M., Larsson L.G., Nilsson K., Hellman L.; "Expression of a mast cell tryptase in the human monocytic cell lines U-937 and Mono Mac 6."; Scand. J. Immunol. 38:359-367(1993).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT). STRAIN=Leaden X A1; DOI=10.1007/BF00177823; PubMed=7959952 [NCBI, ExPASy, EBI, Israel, Japan] Huang R., Hellman L.T.; "Genes for mast-cell serine protease and their molecular evolution."; Immunogenetics 40:397-414(1994).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). STRAIN=FVB/N; TISSUE=Colon; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	PROTEIN SEQUENCE OF 32-54. PubMed=2326280 [NCBI, ExPASy, EBI, Israel, Japan] Reynolds D.S., Stevens R.L., Lane W.S., Carr M.H., Austen K.F., Serafin W.E.; "Different mouse mast cell populations express various combinations of at least six distinct mast cell serine proteases."; Proc. Natl. Acad. Sci. U.S.A. 87:3230-3234(1990).
[6]	FUNCTION, AND KNOCKOUT. DOI=10.1074/jbc.M611842200; PubMed=17456473 [NCBI, ExPASy, EBI, Israel, Japan] Thakurdas S.M., Melicoff E., Sansores-Garcia L., Moreira D.C., Petrova Y., Stevens R.L., Adachi R.; "The mast cell-restricted tryptase mMCP-6 has a critical immunoprotective role in bacterial infections."; J. Biol. Chem. 282:20809-20815(2007).
[7]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-98, AND MASS SPECTROMETRY. TISSUE=Mast cell; PubMed=17947660 [NCBI, ExPASy, EBI, Israel, Japan] Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.; "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."; J. Immunol. 179:5864-5876(2007).
[8]	TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. DOI=10.1016/j.molimm.2006.04.019; PubMed=16777228 [NCBI, ExPASy, EBI, Israel, Japan] Abraham D., Oster H., Huber M., Leitges M.; "The expression pattern of three mast cell specific proteases during mouse development."; Mol. Immunol. 44:732-740(2007).

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. Has an immunoprotective role during bacterial infection. Required to efficiently combat K.pneumoniae infection.
CATALYTIC ACTIVITY: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more restricted specificity than trypsin.
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Secreted (By similarity). Note=Released from the secretory granules upon mast cell activation (By similarity).

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	Long
Isoform ID	P21845-1
This is the isoform sequence displayed in this entry.

Name	Short
Isoform ID	P21845-2
Note: Probably non functional.
Features which should be applied to build the isoform sequence: VSP_005376, VSP_005377.

TISSUE SPECIFICITY: During embryogenesis, detected primarily in skin.
DEVELOPMENTAL STAGE: Not detected at early embryonic stages but is abundantly expressed in later stages with a peak at E17.5-E18.5.
MISCELLANEOUS: Mice lacking Tpsb2 are unable to efficiently combat K.pneumoniae infection of the peritoneal cavity.
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

M57626; AAA39988.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M57625; AAA39987.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L31853; AAA39725.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X78542; CAA55288.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC024374; AAH24374.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A38654; A38654.
I48685; I48685.

UniGene

Mm.7409

3D structure databases

HSSP

P20231; 1A0L. [HSSP ENTRY / PDB]

SMR

P21845; 32-274.

ModBase

P21845.

Protein family/group databases

MEROPS

S01.025; -.

Organism-specific databases

MGI

MGI:96942; Tpsb2.

Gene expression databases

ArrayExpress

P21845; -.

CleanEx

MM_TPSB2; -.

GermOnline

ENSMUSG00000033825; Mus musculus.

Ontologies

GO:0005576;	Cellular component: extracellular region (traceable author statement from MGI).
GO:0008201;	Molecular function: heparin binding (inferred from direct assay from MGI).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from MGI).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006954;	Biological process: inflammatory response (traceable author statement from MGI).
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).

ProtoNet

P21845.

Genome annotation databases

Ensembl

ENSMUSG00000033825; Mus musculus. [Contig view]

Phylogenomic databases

HOGENOM

P21845; -.

HOVERGEN

P21845; -.

Other

SOURCE

Tpsb2; Mus musculus.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`
`PROPEP`	`22 31`	`10`	`Activation peptide.`	`PRO_0000027490`
`CHAIN`	`32 276`	`245`	`Tryptase beta-2.`	`PRO_0000027491`
`DOMAIN`	`32 273`	`242`	`Peptidase S1.`
`ACT_SITE`	`75 75`		`Charge relay system (By similarity).`
`ACT_SITE`	`122 122`		`Charge relay system (By similarity).`
`ACT_SITE`	`225 225`		`Charge relay system (By similarity).`
`MOD_RES`	`98 98`		`Phosphotyrosine.`
`CARBOHYD`	`133 133`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`60 76`		`By similarity.`
`DISULFID`	`156 231`		`By similarity.`
`DISULFID`	`189 212`		`By similarity.`
`DISULFID`	`221 249`		`By similarity.`
`VAR_SEQ`	`223 230`		`GDSGGPLV -> PFCIGDDI (in isoform Short).`	`VSP_005376`
`VAR_SEQ`	`231 276`		`Missing (in isoform Short).`	`VSP_005377`

Sequence information

Length: 276 AA [This is the length of the unprocessed precursor]

Molecular weight: 30927 Da [This is the MW of the unprocessed precursor]

CRC64: 525B2C9A04A72200 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLKRRLLLLW ALSLLASLVY SAPRPANQRV GIVGGHEASE SKWPWQVSLR FKLNYWIHFC 

        70         80         90        100        110        120 
GGSLIHPQWV LTAAHCVGPH IKSPQLFRVQ LREQYLYYGD QLLSLNRIVV HPHYYTAEGG 

       130        140        150        160        170        180 
ADVALLELEV PVNVSTHIHP ISLPPASETF PPGTSCWVTG WGDIDNDEPL PPPYPLKQVK 

       190        200        210        220        230        240 
VPIVENSLCD RKYHTGLYTG DDFPIVHDGM LCAGNTRRDS CQGDSGGPLV CKVKGTWLQA 

       250        260        270 
GVVSWGEGCA QPNKPGIYTR VTYYLDWIHR YVPEHS

P21845 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