ID TRYD_HUMAN STANDARD; PRT; 235 AA. AC Q9BZJ3; O95824; Q8TDI6; Q96L36; Q96RZ5; Q9H2Y6; Q9UQI8; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-SEP-2003 (Rel. 42, Last annotation update) DE Tryptase delta precursor (EC 3.4.21.59) (Delta tryptase) (Mast cell DE mMCP-7-like) (HmMCP-3-like tryptase III). GN TPSD1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A., AND VARIANTS ARG-15 AND MET-76. RX MEDLINE=99121069; PubMed=9920877; 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 SEQUENCE FROM N.A. RX MEDLINE=21101554; PubMed=11174199; 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 SEQUENCE FROM N.A. RX MEDLINE=21096910; PubMed=11157797; 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 SEQUENCE OF 33-235 FROM N.A. (ISOFORMS 1 AND 2), ENZYMATIC ACTIVITY, RP TISSUE SPECIFICITY, AND VARIANT MET-76. RX MEDLINE=22278650; PubMed=12391231; 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 (By similarity). CC -!- CATALYTIC ACTIVITY: Preferential cleavage: Arg-|-, Lys-|-, but CC with more restricted specificity than trypsin. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Released from the secretory granules upon CC mast cell activation (By similarity). 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 -!- SIMILARITY: Belongs to peptidase family S1. Tryptase subfamily. CC -!- CAUTION: Although Ref.2 reported this as a pseudogene, Ref.4 CC showed it is expressed and has proteolytic activity when expressed CC in bacterial cells. 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; ALT_INIT. DR EMBL; AF099147; AAD17861.1; -. DR EMBL; AF318074; AAK12909.1; -. DR EMBL; AE006466; AAK61272.1; ALT_INIT. DR EMBL; AF206664; AAG35694.1; -. DR EMBL; AF421357; AAL86695.1; -. DR EMBL; AY055427; AAL17874.1; -. DR HSSP; P20231; 1AAO. DR MEROPS; S01.054; -. DR Genew; HGNC:14118; TPSD1. DR InterPro; IPR001314; Chymotrypsin. DR InterPro; IPR001254; Ser_protease_Try. DR Pfam; PF00089; trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. KW Hydrolase; Serine protease; Signal; Zymogen; Glycoprotein; KW Alternative splicing; Polymorphism. FT SIGNAL 1 18 POTENTIAL. FT PROPEP 19 30 ACTIVATION PEPTIDE (BY SIMILARITY). FT CHAIN 31 235 TRYPTASE DELTA. FT ACT_SITE 74 74 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 121 121 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 224 224 CHARGE RELAY SYSTEM (BY SIMILARITY). FT DISULFID 59 75 BY SIMILARITY. FT DISULFID 155 230 BY SIMILARITY. FT DISULFID 188 211 BY SIMILARITY. FT CARBOHYD 132 132 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 79 87 Missing (in isoform 2). FT /FTId=VSP_008319. FT VARIANT 15 15 P -> R (in dbSNP:3865205). FT /FTId=VAR_016870. FT VARIANT 18 18 V -> A (in dbSNP:1800984). FT /FTId=VAR_016871. FT VARIANT 76 76 V -> M (in dbSNP:3993987). FT /FTId=VAR_016872. FT CONFLICT 18 18 V -> G (IN REF. 1; AAD17861). FT CONFLICT 171 171 P -> S (IN REF. 4; AAL17874). SQ SEQUENCE 235 AA; 25816 MW; B1FFB6C2A8006B22 CRC64; MLSLLLLALP VLASPAYVAP APGQALQQTG IVGGQEAPRS KWPWQVSLRV RGPYWMHFCG GSLIHPQWVL TAAHCVEPDI KDLAALRVQL REQHLYYQDQ LLPVSRIIVH PQFYIIQTGA DIALLELEEP VNISSHIHTV TLPPASETFP PGMPCWVTGW GDVDNNVHLP PPYPLKEVEV PVVENHLCNA EYHTGLHTGH SFQIVRDDML CAGSENHDSC QGDSGGPLVC KVNGT //