ID TRYD_HUMAN Reviewed; 242 AA. AC Q9BZJ3; O95824; Q8TDI6; Q96L36; Q96RZ5; Q9H2Y6; Q9UQI8; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 2. DT 02-JUN-2021, entry version 159. DE RecName: Full=Tryptase delta; DE EC=3.4.21.59; DE AltName: Full=Delta-tryptase; DE AltName: Full=HmMCP-3-like tryptase III; DE AltName: Full=Mast cell mMCP-7-like; DE AltName: Full=Tryptase-3; DE Flags: Precursor; GN Name=TPSD1; 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 [GENOMIC DNA], AND VARIANTS ARG-22 AND MET-83. 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 [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11174199; DOI=10.1067/mai.2001.112130; RA Min H.-K., Kambe N., Schwartz L.B.; RT "Human mouse mast cell protease 7-like tryptase genes are pseudogenes."; RL J. Allergy Clin. Immunol. 107:315-321(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11157797; DOI=10.1093/hmg/10.4.339; RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.; RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of RT the short arm of human chromosome 16."; RL Hum. Mol. Genet. 10:339-352(2001). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 40-178 (ISOFORM 2), AND VARIANT MET-83. 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 [MRNA] OF 53-242 (ISOFORM 1), ENZYME ACTIVITY, TISSUE RP SPECIFICITY, AND VARIANT MET-83. RX PubMed=12391231; DOI=10.4049/jimmunol.169.9.5145; RA Wang H.-W., McNeil H.P., Husain A., Liu K., Tedla N., Thomas P.S., RA Raftery M., King G.C., Cai Z.Y., Hunt J.E.; RT "Delta tryptase is expressed in multiple human tissues, and a recombinant RT form has proteolytic activity."; RL J. Immunol. 169:5145-5152(2002). 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. {ECO:0000250}. 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 Evidence={ECO:0000269|PubMed:12391231}; CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Released from the CC secretory granules upon mast cell activation. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9BZJ3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BZJ3-2; Sequence=VSP_008319; CC -!- TISSUE SPECIFICITY: Expressed in colon, lung, heart and synovial CC tissue. May be specific to mast cells. {ECO:0000269|PubMed:12391231}. CC -!- SIMILARITY: Belongs to the peptidase S1 family. Tryptase subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00274}. CC -!- CAUTION: Although PubMed:11174199 reported this as a pseudogene, CC PubMed:12391231 showed it is expressed and has proteolytic activity CC when expressed in bacterial cells. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD17861.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAK12909.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AF098327; AAD17845.1; -; Genomic_DNA. DR EMBL; AF099147; AAD17861.1; ALT_INIT; Genomic_DNA. DR EMBL; AF318074; AAK12909.1; ALT_INIT; Genomic_DNA. DR EMBL; AE006466; AAK61272.1; -; Genomic_DNA. DR EMBL; AC120498; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF421357; AAL86695.1; -; mRNA. DR EMBL; AF206664; AAG35694.1; -; mRNA. DR EMBL; AY055427; AAL17874.1; -; mRNA. DR CCDS; CCDS10432.1; -. [Q9BZJ3-1] DR RefSeq; NP_036349.1; NM_012217.2. [Q9BZJ3-1] DR SMR; Q9BZJ3; -. DR STRING; 9606.ENSP00000211076; -. DR BindingDB; Q9BZJ3; -. DR ChEMBL; CHEMBL2095193; -. DR MEROPS; S01.054; -. DR GlyGen; Q9BZJ3; 1 site. DR iPTMnet; Q9BZJ3; -. DR PhosphoSitePlus; Q9BZJ3; -. DR BioMuta; TPSD1; -. DR DMDM; 239938722; -. DR jPOST; Q9BZJ3; -. DR MassIVE; Q9BZJ3; -. DR PaxDb; Q9BZJ3; -. DR PeptideAtlas; Q9BZJ3; -. DR PRIDE; Q9BZJ3; -. DR ProteomicsDB; 79856; -. [Q9BZJ3-1] DR ProteomicsDB; 79857; -. [Q9BZJ3-2] DR Antibodypedia; 55908; 102 antibodies. DR DNASU; 23430; -. DR Ensembl; ENST00000211076; ENSP00000211076; ENSG00000095917. [Q9BZJ3-1] DR GeneID; 23430; -. DR KEGG; hsa:23430; -. DR UCSC; uc002clb.2; human. [Q9BZJ3-1] DR CTD; 23430; -. DR DisGeNET; 23430; -. DR GeneCards; TPSD1; -. DR HGNC; HGNC:14118; TPSD1. DR HPA; ENSG00000095917; Low tissue specificity. DR MIM; 609272; gene. DR neXtProt; NX_Q9BZJ3; -. DR OpenTargets; ENSG00000095917; -. DR PharmGKB; PA37845; -. DR VEuPathDB; HostDB:ENSG00000095917.13; -. DR eggNOG; KOG3627; Eukaryota. DR GeneTree; ENSGT00940000165532; -. DR HOGENOM; CLU_006842_1_2_1; -. DR InParanoid; Q9BZJ3; -. DR OMA; NQLCDAE; -. DR OrthoDB; 1314811at2759; -. DR PhylomeDB; Q9BZJ3; -. DR TreeFam; TF351676; -. DR PathwayCommons; Q9BZJ3; -. DR BioGRID-ORCS; 23430; 12 hits in 980 CRISPR screens. DR GeneWiki; TPSD1; -. DR GenomeRNAi; 23430; -. DR Pharos; Q9BZJ3; Tbio. DR PRO; PR:Q9BZJ3; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q9BZJ3; protein. DR Bgee; ENSG00000095917; Expressed in esophagogastric junction muscularis propria and 102 other tissues. DR ExpressionAtlas; Q9BZJ3; baseline and differential. DR Genevisible; Q9BZJ3; HS. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. 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:0006508; P:proteolysis; IBA:GO_Central. 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 2: Evidence at transcript level; KW Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase; Protease; KW Reference proteome; Secreted; Serine protease; Signal; Zymogen. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT PROPEP 26..37 FT /note="Activation peptide" FT /evidence="ECO:0000250" FT /id="PRO_0000027483" FT CHAIN 38..242 FT /note="Tryptase delta" FT /id="PRO_0000027484" FT DOMAIN 38..242 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 81 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 128 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 231 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT CARBOHYD 139 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 66..82 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 162..237 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 195..218 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT VAR_SEQ 86..94 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:18854315" FT /id="VSP_008319" FT VARIANT 22 FT /note="P -> R (in dbSNP:rs3865205)" FT /evidence="ECO:0000269|PubMed:9920877" FT /id="VAR_016870" FT VARIANT 25 FT /note="V -> A (in dbSNP:rs1800984)" FT /id="VAR_016871" FT VARIANT 83 FT /note="V -> M (in dbSNP:rs1141967)" FT /evidence="ECO:0000269|PubMed:12391231, FT ECO:0000269|PubMed:18854315, ECO:0000269|PubMed:9920877" FT /id="VAR_016872" FT CONFLICT 25 FT /note="V -> G (in Ref. 1; AAD17861)" FT /evidence="ECO:0000305" FT CONFLICT 178 FT /note="P -> S (in Ref. 6; AAL17874)" FT /evidence="ECO:0000305" SQ SEQUENCE 242 AA; 26584 MW; 6E72D8AE1EDEA2F1 CRC64; MLLLAPQMLS LLLLALPVLA SPAYVAPAPG QALQQTGIVG GQEAPRSKWP WQVSLRVRGP YWMHFCGGSL IHPQWVLTAA HCVEPDIKDL AALRVQLREQ HLYYQDQLLP VSRIIVHPQF YIIQTGADIA LLELEEPVNI SSHIHTVTLP PASETFPPGM PCWVTGWGDV DNNVHLPPPY PLKEVEVPVV ENHLCNAEYH TGLHTGHSFQ IVRDDMLCAG SENHDSCQGD SGGPLVCKVN GT //