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 22-JUL-2015, entry version 120. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT 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., RA Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., RA Higgs D.R.; RT "Sequence, structure and pathology of the fully annotated terminal 2 RT Mb of 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., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA 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., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA 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., RA Hunt J.E.; RT "Alternate mRNA splicing in multiple human tryptase genes is predicted RT to regulate tetramer formation."; RL J. Biol. Chem. 283:34178-34187(2008). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 53-242 (ISOFORM 1), ENZYME ACTIVITY, RP TISSUE 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 RT recombinant form has proteolytic activity."; RL J. Immunol. 169:5145-5152(2002). CC -!- FUNCTION: Tryptase is the major neutral protease present in mast CC cells and is secreted upon the coupled activation-degranulation CC response of this cell type. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, CC but with more restricted specificity than trypsin. CC {ECO:0000269|PubMed:12391231}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Released from CC the 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. CC {ECO:0000269|PubMed:12391231}. CC -!- SIMILARITY: Belongs to the peptidase S1 family. Tryptase CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}. CC -!- SIMILARITY: Contains 1 peptidase S1 domain. {ECO:0000255|PROSITE- CC ProRule:PRU00274}. CC -!- CAUTION: Although PubMed:11174199 reported this as a pseudogene, CC PubMed:12391231 showed it is expressed and has proteolytic CC activity 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 UniGene; Hs.677789; -. DR ProteinModelPortal; Q9BZJ3; -. DR SMR; Q9BZJ3; 38-242. DR STRING; 9606.ENSP00000211076; -. DR ChEMBL; CHEMBL2095193; -. DR MEROPS; S01.054; -. DR PhosphoSite; Q9BZJ3; -. DR BioMuta; TPSD1; -. DR DMDM; 239938722; -. DR PaxDb; Q9BZJ3; -. DR PRIDE; Q9BZJ3; -. DR Ensembl; ENST00000211076; ENSP00000211076; ENSG00000095917. DR GeneID; 23430; -. DR KEGG; hsa:23430; -. DR UCSC; uc002clb.1; human. [Q9BZJ3-1] DR UCSC; uc010brm.1; human. [Q9BZJ3-2] DR CTD; 23430; -. DR GeneCards; GC16P001307; -. DR H-InvDB; HIX0038551; -. DR HGNC; HGNC:14118; TPSD1. DR HPA; CAB002215; -. DR HPA; CAB032871; -. DR HPA; HPA040182; -. DR HPA; HPA049554; -. DR MIM; 609272; gene. DR neXtProt; NX_Q9BZJ3; -. DR PharmGKB; PA37845; -. DR eggNOG; COG5640; -. DR GeneTree; ENSGT00760000118810; -. DR HOVERGEN; HBG013304; -. DR InParanoid; Q9BZJ3; -. DR KO; K01340; -. DR OMA; CAGSENH; -. DR OrthoDB; EOG75B84T; -. DR PhylomeDB; Q9BZJ3; -. DR TreeFam; TF351676; -. DR GeneWiki; TPSD1; -. DR GenomeRNAi; 23430; -. DR NextBio; 45673; -. DR PRO; PR:Q9BZJ3; -. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; Q9BZJ3; -. DR CleanEx; HS_TPSD1; -. DR Genevisible; Q9BZJ3; HS. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc. DR InterPro; IPR001254; Peptidase_S1. DR InterPro; IPR018114; Peptidase_S1_AS. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR009003; Trypsin-like_Pept_dom. 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; Complete proteome; Disulfide bond; Glycoprotein; KW Hydrolase; Polymorphism; Protease; Reference proteome; Secreted; KW Serine protease; Signal; Zymogen. FT SIGNAL 1 25 {ECO:0000255}. FT PROPEP 26 37 Activation peptide. {ECO:0000250}. FT /FTId=PRO_0000027483. FT CHAIN 38 242 Tryptase delta. FT /FTId=PRO_0000027484. FT DOMAIN 38 242 Peptidase S1. {ECO:0000255|PROSITE- FT ProRule:PRU00274}. FT ACT_SITE 81 81 Charge relay system. {ECO:0000250}. FT ACT_SITE 128 128 Charge relay system. {ECO:0000250}. FT ACT_SITE 231 231 Charge relay system. {ECO:0000250}. FT CARBOHYD 139 139 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 66 82 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 162 237 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 195 218 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT VAR_SEQ 86 94 Missing (in isoform 2). FT {ECO:0000303|PubMed:18854315}. FT /FTId=VSP_008319. FT VARIANT 22 22 P -> R (in dbSNP:rs3865205). FT {ECO:0000269|PubMed:9920877}. FT /FTId=VAR_016870. FT VARIANT 25 25 V -> A (in dbSNP:rs1800984). FT /FTId=VAR_016871. FT VARIANT 83 83 V -> M (in dbSNP:rs3993987). FT {ECO:0000269|PubMed:12391231, FT ECO:0000269|PubMed:18854315, FT ECO:0000269|PubMed:9920877}. FT /FTId=VAR_016872. FT CONFLICT 25 25 V -> G (in Ref. 1; AAD17861). FT {ECO:0000305}. FT CONFLICT 178 178 P -> S (in Ref. 6; AAL17874). FT {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 //