Tryptase beta-2 precursor - Homo sapiens (Human)

Names and origin

Protein names

Recommended name:
    Tryptase beta-2
      Short name=Tryptase-2
    EC=3.4.21.59
Alternative name(s):
    Tryptase II

Gene names

Name:	TPSB2
Synonyms:	TPS2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	275 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Has an immunoprotective role during bacterial infection. Required to efficiently combat K.pneumoniae infection By similarity.
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.
Polymorphism	There are two alleles; beta-II and beta-III which differ by 3 residues.
Sequence similarities	Belongs to the peptidase S1 family. Tryptase subfamily. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Phosphoprotein Zymogen
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	proteolysis Non-traceable author statement. Source: UniProtKB
Cellular component	extracellular region Non-traceable author statement. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction. Source: IntAct serine-type endopeptidase activity Ref.4 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCK1	P16333	1	EBI-1761383,EBI-389883
PIK3R1	P27986	1	EBI-1761383,EBI-79464

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

Potential

Propeptide

19 – 30

Activation peptide

PRO_0000027481

Chain

31 – 275

245

Tryptase beta-2

PRO_0000027482

Regions

Domain

31 – 272

242

Peptidase S1

Sites

Active site

Charge relay system

Active site

121

Charge relay system

Active site

224

Charge relay system

Amino acid modifications

Modified residue

Phosphotyrosine By similarity

Glycosylation

233

N-linked (GlcNAc...) Potential

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Natural variations

Natural variant

51 – 53

HGP → RDR in beta-III.

VAR_012104

Experimental info

Sequence conflict

N → K in AAA51843. Ref.1

Sequence conflict

N → K in AAD13876. Ref.2

Sequence conflict

N → K in AAA36779. Ref.3

Sequence conflict

N → K in AAA36780. Ref.3

Sequence conflict

N → K in AAD17858. Ref.4

Sequence conflict

N → K in AAH29356. Ref.6

Secondary structure

275

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P20231-1 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: ADC48FDC51F37112
Show »

FASTA

275

30,515

        10         20         30         40         50         60 
MLNLLLLALP VLASRAYAAP APGQALQRVG IVGGQEAPRS KWPWQVSLRV HGPYWMHFCG 

        70         80         90        100        110        120 
GSLIHPQWVL TAAHCVGPDV KDLAALRVQL REQHLYYQDQ LLPVSRIIVH PQFYTAQIGA 

       130        140        150        160        170        180 
DIALLELEEP VNVSSHVHTV TLPPASETFP PGMPCWVTGW GDVDNDERLP PPFPLKQVKV 

       190        200        210        220        230        240 
PIMENHICDA KYHLGAYTGD DVRIVRDDML CAGNTRRDSC QGDSGGPLVC KVNGTWLQAG 

       250        260        270 
VVSWGEGCAQ PNRPGIYTRV TYYLDWIHHY VPKKP

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a second complementary DNA for human tryptase." Miller J.S., Moxley G., Schwartz L.B. J. Clin. Invest. 86:864-870(1990) [PubMed: 2203827] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VARIANT BETA-2). Tissue: Lung.
[2]	"Human mast cell tryptase: multiple cDNAs and genes reveal a multigene serine protease family." Vanderslice P., Ballinger S.M., Tam E.K., Goldstein S.M., Craik C.S., Caughey G.H. Proc. Natl. Acad. Sci. U.S.A. 87:3811-3815(1990) [PubMed: 2187193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VARIANTS BETA-2 AND BETA-3).
[3]	"Characterization of a tryptase mRNA expressed in the human basophil cell line KU812." Blom T., Hellman L. Scand. J. Immunol. 37:203-208(1993) [PubMed: 8434231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VARIANT BETA-2).
[4]	"Characterization of genes encoding known and novel human mast cell tryptases on chromosome 16p13.3." Pallaoro M., Fejzo M.S., Shayesteh L., Blount J.L., Caughey G.H. J. Biol. Chem. 274:3355-3362(1999) [PubMed: 9920877] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (VARIANTS BETA-2 AND BETA-3).
[5]	Pallaoro M., Fejzo M.S., Shayesteh L., Blount J.L., Caughey G.H. Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[7]	"Human beta-tryptase is a ring-like tetramer with active sites facing a central pore." Pereira P.J.B., Bergner A., Macedo-Ribeiro S., Huber R., Matschiner G., Fritz H., Sommerhoff C.P., Bode W. Nature 392:306-311(1998) [PubMed: 9521329] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[8]	"The structure of the human betaII-tryptase tetramer: fo(u)r better or worse." Sommerhoff C.P., Bode W., Pereira P.J.B., Stubbs M.T., Stuerzebecher J., Piechottka G.P., Matschiner G., Bergner A. Proc. Natl. Acad. Sci. U.S.A. 96:10984-10991(1999) [PubMed: 10500112] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M37488 mRNA. Translation: AAA51843.1.
M33492 mRNA. Translation: AAA36779.1.
M33493 mRNA. Translation: AAA36780.1.
S55551 mRNA. Translation: AAD13876.1.
AF099143 Genomic DNA. Translation: AAD17859.2.
AF099145 Genomic DNA. Translation: AAD17857.1.
AF099146 Genomic DNA. Translation: AAD17858.1.
BC029356 mRNA. Translation: AAH29356.1.

IPI

IPI00419942.

PIR

B35863.
C35863.

RefSeq

NP_003285.2.
NP_077078.5.

UniGene

Hs.405479
Hs.592982

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A0L	X-ray	3.00	A/B/C/D	31-274	[»]
1AAO	model	-	A	31-275	[»]
2BM2	X-ray	2.20	A/B/C/D	31-275	[»]
2FPZ	X-ray	2.00	A/B/C/D	31-275	[»]
2FS8	X-ray	2.50	A/B/C/D	31-275	[»]
2FS9	X-ray	2.30	A/B/C/D	31-275	[»]
2FWW	X-ray	2.25	A/B/C/D	31-275	[»]
2FXR	X-ray	2.50	A/B/C/D	31-275	[»]
2GDD	X-ray	2.35	A/B/C/D	31-275	[»]
2ZA5	X-ray	2.30	A/B/C/D	31-275	[»]

ModBase

Protein-protein interaction databases

IntAct

P20231. 2 interactions.

STRING

P20231.

Protein family/group databases

MEROPS

S01.015.

PTM databases

PhosphoSite

P20231.

Proteomic databases

PRIDE

P20231.

Genome annotation databases

Ensembl

ENST00000338844; ENSP00000343577; ENSG00000172236; Homo sapiens. [Genome view]
ENST00000382804; ENSP00000372254; ENSG00000172236; Homo sapiens. [Genome view]
ENST00000461509; ENSP00000418247; ENSG00000172236; Homo sapiens. [Genome view]

GeneID

64499.
7177.

KEGG

hsa:64499.
hsa:7177.

Organism-specific databases

CTD

64499.
7177.

GeneCards

GC16M001219.

H-InvDB

HIX0012676.

HGNC

HGNC:14120. TPSB2.

MIM

191081. gene.

PharmGKB

PA37846.

GenAtlas

Phylogenomic databases

eggNOG

prNOG05667.

HOVERGEN

P20231.

InParanoid

P20231.

PhylomeDB

P20231.

Enzyme and pathway databases

BRENDA

3.4.21.59. 247.

Gene expression databases

ArrayExpress

P20231.

Bgee

P20231.

CleanEx

HS_TPSB2.

Genevestigator

P20231.

GermOnline

ENSG00000172236. Homo sapiens.

Family and domain databases

InterPro

IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
IPR009003. Ser/Cys_Pept_Trypsin-like.
[Graphical view]

Pfam

PF00089. Trypsin. 1 hit.
[Graphical view]

PRINTS

PR00722. CHYMOTRYPSIN.

SMART

SM00020. Tryp_SPc. 1 hit.
[Graphical view]

PROSITE

PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

Other Resources

NextBio

28132.

SOURCE

Entry information

Entry name

TRYB2_HUMAN

Accession

Primary (citable) accession number: P20231
Secondary accession number(s): O95827

Q9UQI7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	October 17, 2006
Last modified:	January 19, 2010
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.