Reviewed, UniProtKB/Swiss-Prot Q15661 (TRYB1_HUMAN)

Names and origin

Protein names

Recommended name:
    Tryptase beta-1
      Short name=Tryptase-1
    EC=3.4.21.59
Alternative name(s):
    Tryptase I

Gene names

Name:	TPSAB1
Synonyms:	TPSB1

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.
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 component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: IntAct serine-type endopeptidase activity Ref.1 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCK1	P16333	1	EBI-1761369,EBI-389883
PIK3R1	P27986	1	EBI-1761369,EBI-79464

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15661-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q15661-2)

The sequence of this isoform differs from the canonical sequence as follows:
     79-87: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Potential

Propeptide

19 – 30

12

Activation peptide By similarity

PRO_0000027479

Chain

31 – 275

245

Tryptase beta-1

PRO_0000027480

Regions

Domain

31 – 272

242

Peptidase S1

Sites

Active site

74

1

Charge relay system

Active site

121

1

Charge relay system

Active site

224

1

Charge relay system

Amino acid modifications

Glycosylation

132

1

N-linked (GlcNAc...) Potential

Glycosylation

233

1

N-linked (GlcNAc...) Ref.5

Disulfide bond

59 ↔ 75

By similarity

Disulfide bond

155 ↔ 230

By similarity

Disulfide bond

188 ↔ 211

By similarity

Disulfide bond

220 ↔ 248

By similarity

Natural variations

Alternative sequence

79 – 87

9

Missing in isoform 2.

VSP_005375

Natural variant

18

1

A → V: dbSNP rs1800984. Ref.6

VAR_014557

Natural variant

23

1

G → V: dbSNP rs1141965. Ref.6

VAR_014558

Natural variant

85

1

A → T: dbSNP rs1141968. Ref.6

VAR_014559

Natural variant

132

1

N → K: dbSNP rs1800991. Ref.6 Ref.3

VAR_016102

Natural variant

136

1

H → R: dbSNP rs1064780.

VAR_051830

Natural variant

141

1

T → A: dbSNP rs1800992. Ref.6

VAR_014560

Natural variant

162

1

D → N: dbSNP rs2234641. Ref.6

VAR_014561

Natural variant

170

1

P → S: dbSNP rs2234904. Ref.6

VAR_014562

Natural variant

215

1

T → S: dbSNP rs2234905. Ref.6

VAR_014563

Natural variant

216

1

R → Q: dbSNP rs2234906. Ref.6

VAR_014564

Secondary structure

1

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275

Helix Strand Turn

Details...

Beta strand

47 – 50

4

Beta strand

56 – 59

4

Beta strand

63 – 65

3

Beta strand

68 – 71

4

Helix

73 – 75

3

Helix

83 – 85

3

Beta strand

86 – 89

4

Turn

95 – 98

4

Beta strand

102 – 109

8

Turn

111 – 113

3

Beta strand

123 – 129

7

Beta strand

155 – 157

3

Helix

185 – 193

9

Beta strand

209 – 211

3

Beta strand

216 – 218

3

Beta strand

228 – 231

4

Beta strand

236 – 238

3

Helix

260 – 263

4

Helix

264 – 268

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: ADC48FDC51F37112	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
	Isoform 2. Checksum: 04F79FEB4ABF517D	FASTA	266	29,533
	10 20 30 40 50 60 MLNLLLLALP VLASRAYAAP APGQALQRVG IVGGQEAPRS KWPWQVSLRV HGPYWMHFCG 70 80 90 100 110 120 GSLIHPQWVL TAAHCVGPVQ LREQHLYYQD QLLPVSRIIV HPQFYTAQIG ADIALLELEE 130 140 150 160 170 180 PVNVSSHVHT VTLPPASETF PPGMPCWVTG WGDVDNDERL PPPFPLKQVK VPIMENHICD 190 200 210 220 230 240 AKYHLGAYTG DDVRIVRDDM LCAGNTRRDS CQGDSGGPLV CKVNGTWLQA GVVSWGEGCA 250 260 QPNRPGIYTR VTYYLDWIHH YVPKKP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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 [GENOMIC DNA / MRNA].
[2]	"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].
[3]	"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] (ISOFORM 1), VARIANT LYS-132.
[4]	"Molecular cloning and characterization of novel human tryptase cDNAs and splicing variants." Wang H.W., McNeil H.P., Thomas P.S., Murphy B.N., Webster M.J., Hettiaratchi A., King G., Heywood G.J., Huang C., Stevens R.L., Hunt J.E. Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 54-275 (ISOFORM 2).
[5]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-233, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Characterization of two highly polymorphic human tryptase loci and comparison with a newly discovered monkey tryptase ortholog." Guida M., Riedy M., Lee D., Hall J. Pharmacogenetics 10:389-396(2000) [PubMed: 10898108] [Abstract] Cited for: VARIANTS VAL-18; VAL-23; THR-85; LYS-132; ALA-141; ASN-162; SER-170; SER-215 AND GLN-216.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M33494 Genomic DNA. Translation: AAC83172.1.
M33491 mRNA. Translation: AAA36778.1.
AF099144 Genomic DNA. Translation: AAD17860.1.
BC074974 mRNA. Translation: AAH74974.1.
AF206667 mRNA. Translation: AAG35697.1.

IPI

IPI00419942.
IPI00472739.

PIR

A35863.
C35863.

RefSeq

NP_003285.2.

UniGene

Hs.405479

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ZEB	X-ray	2.50	A/B/C/D	31-273	[»]
2ZEC	X-ray	2.06	A/B/C/D	31-273	[»]

SMR

Q15661. Positions 31-273.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15661. 2 interactions.

STRING

Q15661.

Protein family/group databases

MEROPS

S01.015.

Proteomic databases

PRIDE

Q15661.

Genome annotation databases

Ensembl

ENST00000338844; ENSP00000343577; ENSG00000172236; Homo sapiens. [Genome view]
ENST00000382804; ENSP00000372254; ENSG00000172236; Homo sapiens. [Genome view]
ENST00000423126; ENSP00000405779; ENSG00000172236; Homo sapiens. [Genome view]
ENST00000430512; ENSP00000412409; ENSG00000172236; Homo sapiens. [Genome view]

GeneID

7177.

KEGG

hsa:7177.

UCSC

uc002ckz.1. human.
uc002cla.2. human.

Organism-specific databases

CTD

7177.

GeneCards

GC16P001233.

HGNC

HGNC:12019. TPSAB1.

HPA

CAB022175.

MIM

191081. gene.

PharmGKB

PA36698.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q15661.

Enzyme and pathway databases

BRENDA

3.4.21.59. 247.

Gene expression databases

Bgee

Q15661.

CleanEx

HS_TPSAB1.

Genevestigator

Q15661.

GermOnline

ENSG00000172236. Homo sapiens.

Family and domain databases

InterPro

IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[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

Search...

Other Resources

NextBio

28132.

SOURCE

Search...

Entry information

Entry name

TRYB1_HUMAN

Accession

Primary (citable) accession number: Q15661
Secondary accession number(s): Q15663, Q6B052, Q9H2Y4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	November 1, 1996
Last modified:	October 13, 2009
This is version 91 of the entry and version 1 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.