Reviewed, UniProtKB/Swiss-Prot Q9BZJ3 (TRYD_HUMAN)

Names and origin

Protein names

Recommended name:
    Tryptase delta
    EC=3.4.21.59
Alternative name(s):
    Delta-tryptase
    Mast cell mMCP-7-like
    Tryptase-3
    HmMCP-3-like tryptase III

Gene names

Name:

TPSD1

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	242 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 By similarity.
Catalytic activity	Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more restricted specificity than trypsin. Ref.6
Subunit structure	Homotetramer By similarity.
Subcellular location	Secreted By similarity. Note: Released from the secretory granules upon mast cell activation By similarity.
Tissue specificity	Expressed in colon, lung, heart and synovial tissue. May be specific to mast cells. Ref.6
Sequence similarities	Belongs to the peptidase S1 family. Tryptase subfamily. Contains 1 peptidase S1 domain.
Caution	Although Ref.2 reported this as a pseudogene, Ref.6 showed it is expressed and has proteolytic activity when expressed in bacterial cells.

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	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	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9BZJ3-1)

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: Q9BZJ3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     86-94: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Propeptide	26 – 37	12	Activation peptide By similarity		PRO_0000027483
	Chain	38 – 242	205	Tryptase delta		PRO_0000027484
Regions
	Domain	38 – 242	205	Peptidase S1
Sites
	Active site	81	1	Charge relay system By similarity
	Active site	128	1	Charge relay system By similarity
	Active site	231	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	139	1	N-linked (GlcNAc...) Potential
	Disulfide bond	66 ↔ 82		By similarity
	Disulfide bond	162 ↔ 237		By similarity
	Disulfide bond	195 ↔ 218		By similarity
Natural variations
	Alternative sequence	86 – 94	9	Missing in isoform 2.		VSP_008319
	Natural variant	22	1	P → R: dbSNP rs3865205.		VAR_016870
	Natural variant	25	1	V → A: dbSNP rs1800984.		VAR_016871
	Natural variant	83	1	V → M: dbSNP rs3993987.		VAR_016872
Experimental info
	Sequence conflict	25	1	V → G in AAD17861. Ref.1
	Sequence conflict	178	1	P → S in AAL17874. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 16, 2009. Version 2. Checksum: 6E72D8AE1EDEA2F1	FASTA	242	26,584
	10 20 30 40 50 60 MLLLAPQMLS LLLLALPVLA SPAYVAPAPG QALQQTGIVG GQEAPRSKWP WQVSLRVRGP 70 80 90 100 110 120 YWMHFCGGSL IHPQWVLTAA HCVEPDIKDL AALRVQLREQ HLYYQDQLLP VSRIIVHPQF 130 140 150 160 170 180 YIIQTGADIA LLELEEPVNI SSHIHTVTLP PASETFPPGM PCWVTGWGDV DNNVHLPPPY 190 200 210 220 230 240 PLKEVEVPVV ENHLCNAEYH TGLHTGHSFQ IVRDDMLCAG SENHDSCQGD SGGPLVCKVN GT
	Isoform 2. Checksum: 74A9069BFC39CF44	FASTA	233	25,587
	10 20 30 40 50 60 MLLLAPQMLS LLLLALPVLA SPAYVAPAPG QALQQTGIVG GQEAPRSKWP WQVSLRVRGP 70 80 90 100 110 120 YWMHFCGGSL IHPQWVLTAA HCVEPVQLRE QHLYYQDQLL PVSRIIVHPQ FYIIQTGADI 130 140 150 160 170 180 ALLELEEPVN ISSHIHTVTL PPASETFPPG MPCWVTGWGD VDNNVHLPPP YPLKEVEVPV 190 200 210 220 230 VENHLCNAEY HTGLHTGHSF QIVRDDMLCA GSENHDSCQG DSGGPLVCKV NGT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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 ARG-22 AND MET-83.
[2]	"Human mouse mast cell protease 7-like tryptase genes are pseudogenes." Min H.-K., Kambe N., Schwartz L.B. J. Allergy Clin. Immunol. 107:315-321(2001) [PubMed: 11174199] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16." Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R. Hum. Mol. Genet. 10:339-352(2001) [PubMed: 11157797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed: 15616553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Alternate mRNA splicing in multiple human tryptase genes is predicted to regulate tetramer formation." Jackson N.E., Wang H.W., Bryant K.J., McNeil H.P., Husain A., Liu K., Tedla N., Thomas P.S., King G.C., Hettiaratchi A., Cairns J., Hunt J.E. J. Biol. Chem. 283:34178-34187(2008) [PubMed: 18854315] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 40-178 (ISOFORM 2), VARIANT MET-83.
[6]	"Delta tryptase is expressed in multiple human tissues, and a recombinant form has proteolytic activity." Wang H.-W., McNeil H.P., Husain A., Liu K., Tedla N., Thomas P.S., Raftery M., King G.C., Cai Z.Y., Hunt J.E. J. Immunol. 169:5145-5152(2002) [PubMed: 12391231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 53-242 (ISOFORM 1), ENZYME ACTIVITY, TISSUE SPECIFICITY, VARIANT MET-83.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF098327 Genomic DNA. Translation: AAD17845.1. AF099147 Genomic DNA. Translation: AAD17861.1. Different initiation. AF318074 Genomic DNA. Translation: AAK12909.1. Different initiation. AE006466 Genomic DNA. Translation: AAK61272.1. AC120498 Genomic DNA. No translation available. AF421357 mRNA. Translation: AAL86695.1. AF206664 mRNA. Translation: AAG35694.1. AY055427 mRNA. Translation: AAL17874.1.
IPI	IPI00376200. IPI00419573.
UniGene	Hs.677789
3D structure databases
HSSP	HSSP built from PDB template 1A0L based on UniProtKB P20231.
SMR	Q9BZJ3. Positions 31-235.
ModBase	Search...
Protein family/group databases
MEROPS	S01.054.
PTM databases
PhosphoSite	Q9BZJ3.
Proteomic databases
PRIDE	Q9BZJ3.
Genome annotation databases
Ensembl	ENSG00000095917. Homo sapiens. [Contig view]
UCSC	uc002clb.1. human. uc010brm.1. human.
Organism-specific databases
GeneCards	GC16P001246. GC16P001247.
H-InvDB	HIX0029969.
HGNC	HGNC:14118. TPSD1.
HPA	CAB002215.
MIM	609272. gene.
PharmGKB	PA37845.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q9BZJ3.
Enzyme and pathway databases
BRENDA	3.4.21.59. 247.
Gene expression databases
ArrayExpress	Q9BZJ3.
Bgee	Q9BZJ3.
CleanEx	HS_TPSD1.
GermOnline	ENSG00000095917. 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
SOURCE	Search...

Entry information

Entry name

TRYD_HUMAN

Accession

Primary (citable) accession number: Q9BZJ3
Secondary accession number(s): O95824 , Q8TDI6, Q96L36, Q96RZ5, Q9H2Y6, Q9UQI8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	June 16, 2009
Last modified:	July 7, 2009
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)