TRYB1_HUMAN
ID TRYB1_HUMAN Reviewed; 275 AA.
AC Q15661; D2E6R9; D2E6S1; P15157; Q15663; Q6B052; Q9H2Y4; Q9H2Y5; Q9UQI1;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Tryptase alpha/beta-1;
DE Short=Tryptase-1;
DE EC=3.4.21.59;
DE AltName: Full=Tryptase I;
DE AltName: Full=Tryptase alpha-1;
DE Flags: Precursor;
GN Name=TPSAB1; Synonyms=TPS1, TPS2, TPSB1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS THR-85; SER-215;
RP GLN-216 AND LYS-221.
RC TISSUE=Lung;
RX PubMed=2677049; DOI=10.1172/jci114284;
RA Miller J.S., Westin E.H., Schwartz L.B.;
RT "Cloning and characterization of complementary DNA for human tryptase.";
RL J. Clin. Invest. 84:1188-1195(1989).
RN [2]
RP SEQUENCE REVISION TO 89-93 AND 108.
RA Schwartz L.B.;
RL Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ALLELE BETA-I) (ISOFORM 1).
RX PubMed=2187193; DOI=10.1073/pnas.87.10.3811;
RA Vanderslice P., Ballinger S.M., Tam E.K., Goldstein S.M., Craik C.S.,
RA Caughey G.H.;
RT "Human mast cell tryptase: multiple cDNAs and genes reveal a multigene
RT serine protease family.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3811-3815(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES ALPHA AND BETA-I) (ISOFORM 1).
RX PubMed=9920877; DOI=10.1074/jbc.274.6.3355;
RA Pallaoro M., Fejzo M.S., Shayesteh L., Blount J.L., Caughey G.H.;
RT "Characterization of genes encoding known and novel human mast cell
RT tryptases on chromosome 16p13.3.";
RL J. Biol. Chem. 274:3355-3362(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 16-275 (ALLELE ALPHA; ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 54-275
RP (ALLELE BETA-I; ISOFORM 2), VARIANTS PRO-15 AND THR-85, FUNCTION,
RP FIBRONECTIN CLEAVAGE, AND TISSUE SPECIFICITY.
RX PubMed=18854315; DOI=10.1074/jbc.m807553200;
RA Jackson N.E., Wang H.W., Bryant K.J., McNeil H.P., Husain A., Liu K.,
RA Tedla N., Thomas P.S., King G.C., Hettiaratchi A., Cairns J., Hunt J.E.;
RT "Alternate mRNA splicing in multiple human tryptase genes is predicted to
RT regulate tetramer formation.";
RL J. Biol. Chem. 283:34178-34187(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS PRO-15;
RP SER-170; SER-215; GLN-216 AND LYS-221.
RX PubMed=19748655; DOI=10.1016/j.jaci.2009.07.026;
RA Trivedi N.N., Tamraz B., Chu C., Kwok P.Y., Caughey G.H.;
RT "Human subjects are protected from mast cell tryptase deficiency despite
RT frequent inheritance of loss-of-function mutations.";
RL J. Allergy Clin. Immunol. 124:1099-1105(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-132.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 31-50, AND PROTEIN SEQUENCE OF 31-38.
RC TISSUE=Lung;
RX PubMed=3543004; DOI=10.1016/s0021-9258(19)75795-0;
RA Cromlish J.A., Seidah N.G., Marcinkiewcz M., Hamelin J., Johnson D.A.,
RA Chretein M.;
RT "Human pituitary tryptase: molecular forms, NH2-terminal sequence,
RT immunocytochemical localization, and specificity with prohormone and
RT fluorogenic substrates.";
RL J. Biol. Chem. 262:1363-1373(1987).
RN [10]
RP FORMATION OF A COMPLEX WITH SERPINB6.
RX PubMed=14670919; DOI=10.1182/blood-2003-08-2981;
RA Strik M.C., Wolbink A., Wouters D., Bladergroen B.A., Verlaan A.R.,
RA van Houdt I.S., Hijlkema S., Hack C.E., Kummer J.A.;
RT "Intracellular serpin SERPINB6 (PI6) is abundantly expressed by human mast
RT cells and forms complexes with beta-tryptase monomers.";
RL Blood 103:2710-2717(2004).
RN [11]
RP SUBUNIT.
RX PubMed=18039527; DOI=10.1016/j.intimp.2007.07.007;
RA Fukuoka Y., Schwartz L.B.;
RT "Active monomers of human beta-tryptase have expanded substrate
RT specificities.";
RL Int. Immunopharmacol. 7:1900-1908(2007).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-233.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP INVOLVEMENT IN HEREDITARY ALPHA TRYPTASEMIA.
RX PubMed=27749843; DOI=10.1038/ng.3696;
RA Lyons J.J., Yu X., Hughes J.D., Le Q.T., Jamil A., Bai Y., Ho N., Zhao M.,
RA Liu Y., O'Connell M.P., Trivedi N.N., Nelson C., DiMaggio T., Jones N.,
RA Matthews H., Lewis K.L., Oler A.J., Carlson R.J., Arkwright P.D., Hong C.,
RA Agama S., Wilson T.M., Tucker S., Zhang Y., McElwee J.J., Pao M.,
RA Glover S.C., Rothenberg M.E., Hohman R.J., Stone K.D., Caughey G.H.,
RA Heller T., Metcalfe D.D., Biesecker L.G., Schwartz L.B., Milner J.D.;
RT "Elevated basal serum tryptase identifies a multisystem disorder associated
RT with increased TPSAB1 copy number.";
RL Nat. Genet. 48:1564-1569(2016).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 31-275.
RX PubMed=12162961; DOI=10.1016/s0022-2836(02)00625-3;
RA Marquardt U., Zettl F., Huber R., Bode W., Sommerhoff C.;
RT "The crystal structure of human alpha1-tryptase reveals a blocked
RT substrate-binding region.";
RL J. Mol. Biol. 321:491-502(2002).
RN [16]
RP VARIANTS PRO-15; VAL-18; VAL-23; THR-85; LYS-132; ALA-141; ASN-162;
RP SER-170; SER-215; GLN-216; LYS-221 AND ASN-263.
RX PubMed=10898108; DOI=10.1097/00008571-200007000-00002;
RA Guida M., Riedy M., Lee D., Hall J.;
RT "Characterization of two highly polymorphic human tryptase loci and
RT comparison with a newly discovered monkey tryptase ortholog.";
RL Pharmacogenetics 10:389-396(2000).
CC -!- FUNCTION: Tryptase is the major neutral protease present in mast cells
CC and is secreted upon the coupled activation-degranulation response of
CC this cell type. May play a role in innate immunity. Isoform 2 cleaves
CC large substrates, such as fibronectin, more efficiently than isoform 1,
CC but seems less efficient toward small substrates (PubMed:18854315).
CC {ECO:0000250, ECO:0000250|UniProtKB:P21845,
CC ECO:0000269|PubMed:18854315}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more
CC restricted specificity than trypsin.; EC=3.4.21.59;
CC -!- SUBUNIT: Homotetramer. The active tetramer is converted to inactive
CC monomers at neutral and acidic pH in the absence of heparin. Low
CC concentrations of inactive monomers become active monomers at pH 6.0 in
CC the presence of heparin. When the concentration of active monomers is
CC higher, they convert to active monomers and then to active tetramers.
CC These monomers are active and functionally distinct from the tetrameric
CC enzyme. In contrast to the hidden active sites in the tetrameric form,
CC the active site of the monomeric form is accessible for macromolecular
CC proteins and inhibitors eg: fibrinogen which is a substrate for the
CC monomeric but not for the tetrameric form. The monomeric form forms a
CC complex with SERPINB6. {ECO:0000269|PubMed:18039527}.
CC -!- INTERACTION:
CC Q15661; P16333: NCK1; NbExp=2; IntAct=EBI-1761369, EBI-389883;
CC Q15661; P27986: PIK3R1; NbExp=2; IntAct=EBI-1761369, EBI-79464;
CC Q15661; Q15661: TPSAB1; NbExp=3; IntAct=EBI-1761369, EBI-1761369;
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Released from the secretory
CC granules upon mast cell activation. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15661-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15661-2; Sequence=VSP_005375;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in lung,
CC stomach, spleen, heart and skin; in these tissues, isoform 1 is
CC predominant. Isoform 2 is expressed in aorta, spleen, and breast tumor,
CC with highest levels in the endothelial cells of some blood vessels
CC surrounding the aorta, as well as those surrounding the tumor and low
CC levels, if any, in mast cells (at protein level).
CC {ECO:0000269|PubMed:18854315}.
CC -!- POLYMORPHISM: There are two alleles alpha and beta-I. The sequence
CC shown is that of allele beta-I. {ECO:0000269|PubMed:18854315,
CC ECO:0000269|PubMed:2187193, ECO:0000269|PubMed:9920877}.
CC -!- DISEASE: Note=Hereditary alpha tryptasemia is caused by an increase in
CC the copy number (usually between two and three copies) of the alpha
CC allele. Affected individuals have elevated basal serum tryptase levels
CC that are associated with cutaneous flushing and pruritus, dysautonomia,
CC functional gastrointestinal symptoms, chronic pain, and connective
CC tissue abnormalities. It is not clear if the associated multisystem
CC complaints might be due to the coinheritance of a second functional
CC genetic variant. {ECO:0000269|PubMed:27749843}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Tryptase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M30038; AAA86934.1; -; mRNA.
DR EMBL; M33494; AAC83172.1; -; Genomic_DNA.
DR EMBL; M33491; AAA36778.1; -; mRNA.
DR EMBL; AF098328; AAD17846.1; -; Genomic_DNA.
DR EMBL; AF099144; AAD17860.1; -; Genomic_DNA.
DR EMBL; AF206665; AAG35695.1; -; mRNA.
DR EMBL; AF206666; AAG35696.1; -; mRNA.
DR EMBL; AF206667; AAG35697.1; -; mRNA.
DR EMBL; FJ931116; ACZ98910.1; -; Genomic_DNA.
DR EMBL; FJ931118; ACZ98912.1; -; mRNA.
DR EMBL; AC120498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC074974; AAH74974.1; -; mRNA.
DR CCDS; CCDS10431.1; -. [Q15661-1]
DR PIR; A35863; A35863.
DR PIR; A45754; A45754.
DR PIR; C35863; C35863.
DR RefSeq; NP_003285.2; NM_003294.3. [Q15661-1]
DR PDB; 1LTO; X-ray; 2.20 A; A/B/C/D=31-275.
DR PDB; 2F9N; X-ray; 1.60 A; A/B/C/D=31-275.
DR PDB; 2F9O; X-ray; 2.10 A; A/B/C/D=31-275.
DR PDB; 2F9P; X-ray; 2.30 A; A/B/C/D=31-275.
DR PDB; 2ZEB; X-ray; 2.50 A; A/B/C/D=31-273.
DR PDB; 2ZEC; X-ray; 2.06 A; A/B/C/D=31-273.
DR PDB; 4A6L; X-ray; 2.05 A; A/B/C/D=31-275.
DR PDB; 4MPU; X-ray; 1.65 A; A/B=31-275.
DR PDB; 4MPV; X-ray; 2.31 A; A/B=31-275.
DR PDB; 4MPW; X-ray; 1.95 A; A/B=31-275.
DR PDB; 4MPX; X-ray; 2.00 A; A/B=31-275.
DR PDB; 4MQA; X-ray; 2.25 A; A/B=31-275.
DR PDB; 5F03; X-ray; 1.94 A; A/B=31-275.
DR PDB; 5WI6; X-ray; 2.72 A; A/B/C/D=31-275.
DR PDB; 6O1F; X-ray; 2.15 A; A=31-275.
DR PDB; 6P0P; X-ray; 2.55 A; A/B=1-275.
DR PDB; 6VVU; X-ray; 3.00 A; A/B/C/D=1-275.
DR PDBsum; 1LTO; -.
DR PDBsum; 2F9N; -.
DR PDBsum; 2F9O; -.
DR PDBsum; 2F9P; -.
DR PDBsum; 2ZEB; -.
DR PDBsum; 2ZEC; -.
DR PDBsum; 4A6L; -.
DR PDBsum; 4MPU; -.
DR PDBsum; 4MPV; -.
DR PDBsum; 4MPW; -.
DR PDBsum; 4MPX; -.
DR PDBsum; 4MQA; -.
DR PDBsum; 5F03; -.
DR PDBsum; 5WI6; -.
DR PDBsum; 6O1F; -.
DR PDBsum; 6P0P; -.
DR PDBsum; 6VVU; -.
DR AlphaFoldDB; Q15661; -.
DR SMR; Q15661; -.
DR BioGRID; 113029; 15.
DR ComplexPortal; CPX-3785; Tryptase alpha/beta-1 complex.
DR IntAct; Q15661; 3.
DR MINT; Q15661; -.
DR STRING; 9606.ENSP00000343577; -.
DR BindingDB; Q15661; -.
DR ChEMBL; CHEMBL2617; -.
DR DrugBank; DB06848; 1-(1'-{[3-(methylsulfanyl)-2-benzothiophen-1-yl]carbonyl}spiro[1-benzofuran-3,4'-piperidin]-5-yl)methanamine.
DR DrugBank; DB06849; 1-[1'-(3-phenylacryloyl)spiro[1-benzofuran-3,4'-piperidin]-5-yl]methanamine.
DR DrugCentral; Q15661; -.
DR GuidetoPHARMACOLOGY; 2424; -.
DR MEROPS; S01.015; -.
DR MEROPS; S01.143; -.
DR GlyConnect; 1861; 12 N-Linked glycans (2 sites).
DR GlyGen; Q15661; 2 sites, 11 N-linked glycans (2 sites).
DR iPTMnet; Q15661; -.
DR PhosphoSitePlus; Q15661; -.
DR BioMuta; TPSAB1; -.
DR DMDM; 18202508; -.
DR jPOST; Q15661; -.
DR MassIVE; Q15661; -.
DR PaxDb; Q15661; -.
DR PRIDE; Q15661; -.
DR Antibodypedia; 9463; 490 antibodies from 39 providers.
DR DNASU; 7177; -.
DR Ensembl; ENST00000338844.8; ENSP00000343577.3; ENSG00000172236.18. [Q15661-1]
DR Ensembl; ENST00000561736.2; ENSP00000456821.2; ENSG00000172236.18. [Q15661-2]
DR Ensembl; ENST00000677899.1; ENSP00000502948.1; ENSG00000172236.18. [Q15661-1]
DR GeneID; 7177; -.
DR KEGG; hsa:7177; -.
DR MANE-Select; ENST00000338844.8; ENSP00000343577.3; NM_003294.4; NP_003285.2.
DR UCSC; uc002ckz.4; human. [Q15661-1]
DR CTD; 7177; -.
DR DisGeNET; 7177; -.
DR GeneCards; TPSAB1; -.
DR HGNC; HGNC:12019; TPSAB1.
DR HPA; ENSG00000172236; Low tissue specificity.
DR MIM; 191080; gene.
DR neXtProt; NX_Q15661; -.
DR OpenTargets; ENSG00000172236; -.
DR PharmGKB; PA36698; -.
DR VEuPathDB; HostDB:ENSG00000172236; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000164974; -.
DR InParanoid; Q15661; -.
DR OMA; RIIRDDM; -.
DR PhylomeDB; Q15661; -.
DR TreeFam; TF351676; -.
DR BRENDA; 3.4.21.59; 2681.
DR PathwayCommons; Q15661; -.
DR Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
DR SignaLink; Q15661; -.
DR SIGNOR; Q15661; -.
DR BioGRID-ORCS; 7177; 14 hits in 1026 CRISPR screens.
DR EvolutionaryTrace; Q15661; -.
DR GenomeRNAi; 7177; -.
DR Pharos; Q15661; Tclin.
DR PRO; PR:Q15661; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q15661; protein.
DR Bgee; ENSG00000172236; Expressed in gall bladder and 88 other tissues.
DR ExpressionAtlas; Q15661; baseline and differential.
DR Genevisible; Q15661; HS.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:1905368; C:peptidase complex; IPI:ComplexPortal.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
DR GO; GO:0006952; P:defense response; TAS:ProtInc.
DR GO; GO:0022617; P:extracellular matrix disassembly; IDA:BHF-UCL.
DR GO; GO:0006508; P:proteolysis; IDA:ComplexPortal.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..30
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027479"
FT CHAIN 31..275
FT /note="Tryptase alpha/beta-1"
FT /id="PRO_0000027480"
FT DOMAIN 31..272
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 74
FT /note="Charge relay system"
FT ACT_SITE 121
FT /note="Charge relay system"
FT ACT_SITE 224
FT /note="Charge relay system"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 59..75
FT DISULFID 155..230
FT DISULFID 188..211
FT DISULFID 220..248
FT VAR_SEQ 79..87
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005375"
FT VARIANT 3
FT /note="N -> S (in allele alpha; dbSNP:rs371929937)"
FT /id="VAR_064277"
FT VARIANT 15
FT /note="R -> P (in dbSNP:rs761476435)"
FT /evidence="ECO:0000269|PubMed:10898108,
FT ECO:0000269|PubMed:18854315, ECO:0000269|PubMed:19748655"
FT /id="VAR_064278"
FT VARIANT 18
FT /note="A -> V (in dbSNP:rs562518617)"
FT /evidence="ECO:0000269|PubMed:10898108"
FT /id="VAR_014557"
FT VARIANT 23
FT /note="G -> V (in allele alpha; dbSNP:rs141519544)"
FT /evidence="ECO:0000269|PubMed:10898108"
FT /id="VAR_014558"
FT VARIANT 28
FT /note="R -> Q (in allele alpha; dbSNP:rs146223687)"
FT /id="VAR_064279"
FT VARIANT 29
FT /note="V -> A (in allele alpha; dbSNP:rs112944038)"
FT /id="VAR_064280"
FT VARIANT 51
FT /note="H -> R (in allele alpha; dbSNP:rs1060281)"
FT /id="VAR_064281"
FT VARIANT 52
FT /note="G -> D (in allele alpha; dbSNP:rs17841227)"
FT /id="VAR_064282"
FT VARIANT 53
FT /note="P -> R (in allele alpha; dbSNP:rs17841226)"
FT /id="VAR_064283"
FT VARIANT 76
FT /note="V -> L (in allele alpha; dbSNP:rs151324823)"
FT /id="VAR_064284"
FT VARIANT 85
FT /note="A -> T (in dbSNP:rs201351744)"
FT /evidence="ECO:0000269|PubMed:10898108,
FT ECO:0000269|PubMed:18854315, ECO:0000269|PubMed:2677049"
FT /id="VAR_014559"
FT VARIANT 115
FT /note="T -> I (in allele alpha; dbSNP:rs199625169)"
FT /id="VAR_064285"
FT VARIANT 116
FT /note="A -> I (in allele alpha; requires 2 nucleotide
FT substitutions)"
FT /id="VAR_064286"
FT VARIANT 118
FT /note="I -> T (in allele alpha; dbSNP:rs202044288)"
FT /id="VAR_064287"
FT VARIANT 132
FT /note="N -> K (in dbSNP:rs144979264)"
FT /evidence="ECO:0000269|PubMed:10898108,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_016102"
FT VARIANT 133
FT /note="V -> I (in allele alpha; dbSNP:rs200334042)"
FT /id="VAR_064288"
FT VARIANT 136
FT /note="H -> R (in allele alpha; dbSNP:rs1064780)"
FT /id="VAR_051830"
FT VARIANT 141
FT /note="T -> A (in dbSNP:rs149113013)"
FT /evidence="ECO:0000269|PubMed:10898108"
FT /id="VAR_014560"
FT VARIANT 141
FT /note="T -> M (in allele alpha)"
FT /id="VAR_064289"
FT VARIANT 162
FT /note="D -> N (in dbSNP:rs143210825)"
FT /evidence="ECO:0000269|PubMed:10898108"
FT /id="VAR_014561"
FT VARIANT 168
FT /note="R -> P (in allele alpha; dbSNP:rs202156919)"
FT /id="VAR_064290"
FT VARIANT 170
FT /note="P -> S (in dbSNP:rs201345428)"
FT /evidence="ECO:0000269|PubMed:10898108,
FT ECO:0000269|PubMed:19748655"
FT /id="VAR_014562"
FT VARIANT 205
FT /note="V -> I (in allele alpha; dbSNP:rs1060284)"
FT /id="VAR_064291"
FT VARIANT 215
FT /note="T -> S (in dbSNP:rs2234905)"
FT /evidence="ECO:0000269|PubMed:10898108,
FT ECO:0000269|PubMed:19748655, ECO:0000269|PubMed:2677049"
FT /id="VAR_014563"
FT VARIANT 216
FT /note="R -> Q (in dbSNP:rs2234906)"
FT /evidence="ECO:0000269|PubMed:10898108,
FT ECO:0000269|PubMed:19748655, ECO:0000269|PubMed:2677049"
FT /id="VAR_014564"
FT VARIANT 221
FT /note="Q -> K (in dbSNP:rs201192435)"
FT /evidence="ECO:0000269|PubMed:10898108,
FT ECO:0000269|PubMed:19748655, ECO:0000269|PubMed:2677049"
FT /id="VAR_064292"
FT VARIANT 245
FT /note="G -> D (in allele alpha; dbSNP:rs145402040)"
FT /id="VAR_064293"
FT VARIANT 263
FT /note="Y -> N (in dbSNP:rs200355084)"
FT /evidence="ECO:0000269|PubMed:10898108"
FT /id="VAR_064294"
FT CONFLICT 129
FT /note="E -> K (in Ref. 6; ACZ98912)"
FT /evidence="ECO:0000305"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:5F03"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:6VVU"
FT STRAND 45..65
FT /evidence="ECO:0007829|PDB:2F9N"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:2F9N"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:2F9N"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2F9N"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:2F9N"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:2F9N"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:2F9N"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:4MPU"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:2F9N"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:2F9N"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:2F9N"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:2F9N"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:2F9N"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:2F9O"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:2F9N"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:2F9N"
FT TURN 221..225
FT /evidence="ECO:0007829|PDB:2F9P"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:2F9N"
FT STRAND 235..244
FT /evidence="ECO:0007829|PDB:2F9N"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:2F9N"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:2F9N"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:2F9N"
FT HELIX 264..270
FT /evidence="ECO:0007829|PDB:2F9N"
SQ SEQUENCE 275 AA; 30515 MW; ADC48FDC51F37112 CRC64;
MLNLLLLALP VLASRAYAAP APGQALQRVG IVGGQEAPRS KWPWQVSLRV HGPYWMHFCG
GSLIHPQWVL TAAHCVGPDV KDLAALRVQL REQHLYYQDQ LLPVSRIIVH PQFYTAQIGA
DIALLELEEP VNVSSHVHTV TLPPASETFP PGMPCWVTGW GDVDNDERLP PPFPLKQVKV
PIMENHICDA KYHLGAYTGD DVRIVRDDML CAGNTRRDSC QGDSGGPLVC KVNGTWLQAG
VVSWGEGCAQ PNRPGIYTRV TYYLDWIHHY VPKKP
