Q9BZJ3 (TRYD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tryptase delta
EC=3.4.21.59

Alternative name(s):
Delta-tryptase
HmMCP-3-like tryptase III
Mast cell mMCP-7-like
Tryptase-3

Gene names

Name:

TPSD1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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.
Sequence caution	The sequence AAD17861.1 differs from that shown. Reason: Erroneous initiation. The sequence AAK12909.1 differs from that shown. Reason: Erroneous initiation.

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 Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro serine-type peptidase activity Traceable author statement Ref.1. Source: ProtInc
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. Ref.1 Corresponds to variant rs3865205 [ dbSNP | Ensembl ].		VAR_016870
	Natural variant	25	1	V → A. Corresponds to variant rs1800984 [ dbSNP | Ensembl ].		VAR_016871
	Natural variant	83	1	V → M. Ref.1 Ref.5 Ref.6 Corresponds to variant rs3993987 [ dbSNP | Ensembl ].		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 [UniParc]. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 53-242 (ISOFORM 1), ENZYME ACTIVITY, TISSUE SPECIFICITY, VARIANT MET-83.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
RefSeq	NP_036349.1. NM_012217.2.
UniGene	Hs.677789.
3D structure databases
ProteinModelPortal	Q9BZJ3.
ModBase	Search...
Protein family/group databases
MEROPS	S01.054.
PTM databases
PhosphoSite	Q9BZJ3.
Polymorphism databases
DMDM	239938722.
Proteomic databases
PaxDb	Q9BZJ3.
PRIDE	Q9BZJ3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000211076; ENSP00000211076; ENSG00000095917. ENST00000397534; ENSP00000380668; ENSG00000095917.
GeneID	23430.
KEGG	hsa:23430.
UCSC	uc002clb.1. human.
Organism-specific databases
CTD	23430.
GeneCards	GC16P001307.
H-InvDB	HIX0038551.
HGNC	HGNC:14118. TPSD1.
HPA	CAB002215.
MIM	609272. gene.
neXtProt	NX_Q9BZJ3.
PharmGKB	PA37845.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5640.
HOVERGEN	HBG013304.
InParanoid	Q9BZJ3.
KO	K01340.
OMA	SSHIHTV.
PhylomeDB	Q9BZJ3.
Gene expression databases
Bgee	Q9BZJ3.
CleanEx	HS_TPSD1.
Genevestigator	Q9BZJ3.
GermOnline	ENSG00000095917. Homo sapiens.
Family and domain databases
InterPro	IPR001254. Peptidase_S1. IPR018114. Peptidase_S1_AS. IPR001314. Peptidase_S1A. IPR009003. Trypsin-like_Pept_dom. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
SUPFAM	SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9BZJ3.
ChEMBL	CHEMBL2402.
GenomeRNAi	23430.
NextBio	45673.
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:	May 1, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.