Reviewed, UniProtKB/Swiss-Prot P15944 (TRYT_CANFA)

Names and origin

Protein names	Recommended name:     Tryptase     EC=3.4.21.59
Organism	Canis familiaris (Dog)
Taxonomic identifier	9615 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length	275 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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.
Sequence similarities	Belongs to the peptidase S1 family. Tryptase subfamily. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Zymogen
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	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Propeptide	21 – 30	10	Activation peptide By similarity		PRO_0000027473
	Chain	31 – 275	245	Tryptase		PRO_0000027474
Regions
	Domain	31 – 272	242	Peptidase S1
Sites
	Active site	74	1	Charge relay system By similarity
	Active site	121	1	Charge relay system By similarity
	Active site	224	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	132	1	N-linked (GlcNAc...) Potential
	Disulfide bond	59 ↔ 75		By similarity
	Disulfide bond	155 ↔ 230		By similarity
	Disulfide bond	188 ↔ 211		By similarity
	Disulfide bond	220 ↔ 248		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P15944-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: C3B869251F248D5B	FASTA	275	30,088
	10 20 30 40 50 60 MPSPLVLALA LLGSLVPVSP APGQALQRVG IVGGREAPGS KWPWQVSLRL KGQYWRHICG 70 80 90 100 110 120 GSLIHPQWVL TAAHCVGPNV VCPEEIRVQL REQHLYYQDH LLPVNRIVMH PNYYTPENGA 130 140 150 160 170 180 DIALLELEDP VNVSAHVQPV TLPPALQTFP TGTPCWVTGW GDVHSGTPLP PPFPLKQVKV 190 200 210 220 230 240 PIVENSMCDV QYHLGLSTGD GVRIVREDML CAGNSKSDSC QGDSGGPLVC RVRGVWLQAG 250 260 270 VVSWGEGCAQ PNRPGIYTRV AYYLDWIHQY VPKEP

References

[1]	"Molecular cloning of dog mast cell tryptase and a related protease: structural evidence of a unique mode of serine protease activation." Vanderslice P., Craik C.S., Nadel J.A., Caughey G.H. Biochemistry 28:4148-4155(1989) [PubMed: 2504277] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	M24664 Genomic DNA. Translation: AAA30854.1.
PIR	A32410.
RefSeq	NP_001091024.1.
UniGene	Cfa.42494
3D structure databases
HSSP	HSSP built from PDB template 1A0L based on UniProtKB P20231.
SMR	P15944. Positions 31-273.
ModBase	Search...
Protein family/group databases
MEROPS	S01.118.
Genome annotation databases
GeneID	100049001.
KEGG	cfa:100049001.
Phylogenomic databases
HOVERGEN	P15944.
Enzyme and pathway databases
BRENDA	3.4.21.59. 463.
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...

Entry information

Entry name

TRYT_CANFA

Accession

Primary (citable) accession number: P15944

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)