Reviewed, UniProtKB/Swiss-Prot P27435 (TRYB1_RAT)

Names and origin

Protein names

Recommended name:
    Tryptase
    EC=3.4.21.59
Alternative name(s):
    Mast cell protease 7
    MMCP-7
    Tryptase alpha/beta-1
    Tryptase, skin

Gene names

Name:	Tpsab1
Synonyms:	Mcp7, Mcpt7, Tpsb1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	273 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.
Subcellular location	Secreted. Note: Released from the secretory granules upon mast cell activation.
Tissue specificity	Mast cells.
Post-translational modification	Glycosylated Probable.
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
Technical term	Direct protein sequencing
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 – 18	18	Potential
	Propeptide	19 – 28	10	Activation peptide Ref.2 Ref.3		PRO_0000027496
	Chain	29 – 273	245	Tryptase		PRO_0000027497
Regions
	Domain	29 – 270	242	Peptidase S1
Sites
	Active site	72	1	Charge relay system By similarity
	Active site	119	1	Charge relay system By similarity
	Active site	222	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	49	1	N-linked (GlcNAc...) Probable
	Disulfide bond	57 ↔ 73		By similarity
	Disulfide bond	153 ↔ 228		By similarity
	Disulfide bond	186 ↔ 209		By similarity
	Disulfide bond	218 ↔ 246		By similarity
Experimental info
	Sequence conflict	42	1	W → V AA sequence Ref.3
	Sequence conflict	49 – 51	3	NDT → WLP AA sequence Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P27435-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 65A5ED4D279FB284	FASTA	273	30,400
	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

References

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

Cross-references

Sequence databases
EMBLGenBankDDBJ	U67910 mRNA. Translation: AAB48263.1.
IPI	IPI00196866.
PIR	A23698. S21275.
RefSeq	NP_062195.2.
UniGene	Rn.10699
3D structure databases
HSSP	HSSP built from PDB template 1A0L based on UniProtKB P20231.
SMR	P27435. Positions 29-271.
ModBase	Search...
Protein family/group databases
MEROPS	S01.026.
Genome annotation databases
Ensembl	ENSRNOG00000024181. Rattus norvegicus. [Contig view]
GeneID	54271.
KEGG	rno:54271.
Organism-specific databases
RGD	3066. Tpsab1.
Phylogenomic databases
HOVERGEN	P27435.
Enzyme and pathway databases
BRENDA	3.4.21.59. 248.
Gene expression databases
ArrayExpress	P27435.
GermOnline	ENSRNOG00000024181. Rattus norvegicus.
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	610832.

Entry information

Entry name

TRYB1_RAT

Accession

Primary (citable) accession number: P27435
Secondary accession number(s): P27436

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)