Q9NRR2 (TRYG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tryptase gamma
EC=3.4.21.-

Alternative name(s):
Serine protease 31
Transmembrane tryptase

Cleaved into the following 2 chains:

1. Tryptase gamma light chain
2. Tryptase gamma heavy chain

Gene names

Name:	TPSG1
Synonyms:	PRSS31, TMT

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	321 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Subcellular location	Membrane; Single-pass membrane protein Potential.
Tissue specificity	Expressed in many tissues.
Polymorphism	There are two alleles; gamma-I and gamma-II which differ by 5 residues.
Sequence similarities	Belongs to the peptidase S1 family. Tryptase subfamily. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane Transmembrane helix
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	integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc
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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 321	302	Tryptase gamma		PRO_0000027498
	Chain	20 – 36	17	Tryptase gamma light chain		PRO_0000027499
	Chain	38 – 321	284	Tryptase gamma heavy chain		PRO_0000027500
Regions
	Transmembrane	284 – 304	21	Helical; Potential
	Domain	38 – 270	233	Peptidase S1
Sites
	Active site	78	1	Charge relay system By similarity
	Active site	125	1	Charge relay system By similarity
	Active site	222	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	85	1	N-linked (GlcNAc...) Potential
	Disulfide bond	26 ↔ 145		Interchain (between light and heavy chains) Potential
	Disulfide bond	63 ↔ 79		By similarity
	Disulfide bond	159 ↔ 228		By similarity
	Disulfide bond	192 ↔ 210		By similarity
	Disulfide bond	218 ↔ 246		By similarity
Natural variations
	Natural variant	60	1	M → V in allele gamma-II. Ref.2 Ref.3 Corresponds to variant rs760357 [ dbSNP | Ensembl ].		VAR_012097
	Natural variant	126	1	I → M in allele gamma-II. Ref.2		VAR_012098
	Natural variant	132	1	S → T in allele gamma-II. Ref.2		VAR_012099
	Natural variant	160	1	W → S. Ref.2 Corresponds to variant rs4984638 [ dbSNP | Ensembl ].		VAR_025012
	Natural variant	204	1	L → I in allele gamma-II. Ref.2		VAR_012100
	Natural variant	239	1	T → I. Ref.1 Ref.2 Ref.3 Ref.5 Corresponds to variant rs11248860 [ dbSNP | Ensembl ].		VAR_061773
	Natural variant	288	1	L → F in allele gamma-II. Ref.2 Ref.3 Corresponds to variant rs1004041 [ dbSNP | Ensembl ].		VAR_012101

Sequences

	Sequence		Length	Mass (Da)
	Q9NRR2 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: D2F7A5A1D66F59C7	FASTA	321	33,815
	10 20 30 40 50 60 MALGACGLLL LLAVPGVSLR TLQPGCGRPQ VSDAGGRIVG GHAAPAGAWP WQASLRLRRM 70 80 90 100 110 120 HVCGGSLLSP QWVLTAAHCF SGSLNSSDYQ VHLGELEITL SPHFSTVRQI ILHSSPSGQP 130 140 150 160 170 180 GTSGDIALVE LSVPVTLSSR ILPVCLPEAS DDFCPGIRCW VTGWGYTREG EPLPPPYSLR 190 200 210 220 230 240 EVKVSVVDTE TCRRDYPGPG GSILQPDMLC ARGPGDACQD DSGGPLVCQV NGAWVQAGTV 250 260 270 280 290 300 SWGEGCGRPN RPGVYTRVPA YVNWIRRHIT ASGGSESGYP RLPLLAGLFL PGLFLLLVSC 310 320 VLLAKCLLHP SADGTPFPAP D

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a new member of the tryptase family of mouse and human mast cell proteases which possesses a novel COOH-terminal hydrophobic extension." Wong G.W., Tang Y., Feyfant E., Sali A., Li L., Li Y., Huang C., Friend D.S., Krilis S.A., Stevens R.L. J. Biol. Chem. 274:30784-30793(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT ILE-239.
[2]	"Characterization of human gamma-tryptases, novel members of the chromosome 16p mast cell tryptase and prostasin gene families." Caughey G.H., Raymond W.W., Blount J.L., Hau L.W., Pallaoro M., Wolters P.J., Verghese G.M. J. Immunol. 164:6566-6575(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-60; MET-126; THR-132; SER-160; ILE-204; ILE-239 AND PHE-288.
[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], VARIANTS VAL-60; ILE-239 AND PHE-288.
[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]	"Organization and alternative splicing of CACNA1H." Mittman S., Agnew W.S. Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 220-321, VARIANT ILE-239.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF175522 mRNA. Translation: AAF03695.1. AF175759 Genomic DNA. Translation: AAF03697.1. AF191031 Genomic DNA. Translation: AAF76457.1. AF195508 Genomic DNA. Translation: AAF76458.1. AE006466 Genomic DNA. Translation: AAK61269.1. AC120498 Genomic DNA. No translation available. AF223563 Genomic DNA. Translation: AAG48852.2.
IPI	IPI00018384.
RefSeq	NP_036599.3. NM_012467.3.
UniGene	Hs.592076.
3D structure databases
ProteinModelPortal	Q9NRR2.
SMR	Q9NRR2. Positions 38-269.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000234798.
Protein family/group databases
MEROPS	S01.028.
Polymorphism databases
DMDM	296453005.
Proteomic databases
PaxDb	Q9NRR2.
PRIDE	Q9NRR2.
Protocols and materials databases
DNASU	25823.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000234798; ENSP00000234798; ENSG00000116176.
GeneID	25823.
KEGG	hsa:25823.
UCSC	uc002ckw.2. human.
Organism-specific databases
CTD	25823.
GeneCards	GC16M001271.
H-InvDB	HIX0038548.
HGNC	HGNC:14134. TPSG1.
MIM	609341. gene.
neXtProt	NX_Q9NRR2.
PharmGKB	PA37849.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5640.
HOGENOM	HOG000251820.
HOVERGEN	HBG013304.
InParanoid	Q9NRR2.
KO	K09615.
OrthoDB	EOG4DR9D1.
Gene expression databases
Bgee	Q9NRR2.
CleanEx	HS_TPSG1.
Genevestigator	Q9NRR2.
GermOnline	ENSG00000116176. 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. False negative. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL4955.
GenomeRNAi	25823.
NextBio	47087.
SOURCE	Search...

Entry information

Entry name

TRYG1_HUMAN

Accession

Primary (citable) accession number: Q9NRR2
Secondary accession number(s): Q96RZ8 , Q9C015, Q9NRQ8, Q9UBB2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 99 of the entry and version 3 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.