TRYD_HUMAN
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 03-AUG-2022, entry version 163.
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};
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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 AlphaFoldDB; Q9BZJ3; -.
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; 105 antibodies from 22 providers.
DR DNASU; 23430; -.
DR Ensembl; ENST00000211076.5; ENSP00000211076.3; ENSG00000095917.14. [Q9BZJ3-1]
DR GeneID; 23430; -.
DR KEGG; hsa:23430; -.
DR MANE-Select; ENST00000211076.5; ENSP00000211076.3; NM_012217.3; NP_036349.1.
DR UCSC; uc002clb.2; human. [Q9BZJ3-1]
DR CTD; 23430; -.
DR DisGeNET; 23430; -.
DR GeneCards; TPSD1; -.
DR HGNC; HGNC:14118; TPSD1.
DR HPA; ENSG00000095917; Tissue enhanced (stomach).
DR MIM; 609272; gene.
DR neXtProt; NX_Q9BZJ3; -.
DR OpenTargets; ENSG00000095917; -.
DR PharmGKB; PA37845; -.
DR VEuPathDB; HostDB:ENSG00000095917; -.
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; 15 hits in 1063 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 mucosa of transverse colon and 87 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
