TYRP3_TYRPU
ID TYRP3_TYRPU Reviewed; 285 AA.
AC C6ZDB5;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Trypsin Tyr p 3.0101 {ECO:0000305};
DE EC=3.4.21.4 {ECO:0000269|PubMed:19339798};
DE AltName: Full=Mite group 3 allergen Tyr p 3 {ECO:0000303|PubMed:19339798};
DE AltName: Allergen=Tyr p 3.0101 {ECO:0000305};
DE Flags: Precursor;
OS Tyrophagus putrescentiae (Mold mite) (Acarus putrescentiae).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Acaroidea; Acaridae; Tyrophaginae;
OC Tyrophagus.
OX NCBI_TaxID=59818 {ECO:0000312|EMBL:ABZ81991.1};
RN [1] {ECO:0000312|EMBL:ABZ81991.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-41, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND ALLERGEN.
RX PubMed=19339798; DOI=10.1159/000210376;
RA Liao E.C., Hsu E.L., Tsai J.J., Ho C.M.;
RT "Immunologic characterization and allergenicity of recombinant Tyr p 3
RT allergen from the storage mite Tyrophagus putrescentiae.";
RL Int. Arch. Allergy Immunol. 150:15-24(2009).
RN [2]
RP ALLERGEN.
RX PubMed=20197679; DOI=10.1159/000288290;
RA Liao E.C., Ho C.M., Tsai J.J.;
RT "Prevalence of Tyrophagus putrescentiae hypersensitivity in subjects over
RT 70 years of age in a veterans' nursing home in Taiwan.";
RL Int. Arch. Allergy Immunol. 152:368-377(2010).
RN [3]
RP ALLERGEN.
RX PubMed=20683648; DOI=10.1007/s10875-010-9446-x;
RA Liao E.C., Ho C.M., Lin M.Y., Tsai J.J.;
RT "Dermatophagoides pteronyssinus and Tyrophagus putrescentiae allergy in
RT allergic rhinitis caused by cross-reactivity not dual-sensitization.";
RL J. Clin. Immunol. 30:830-839(2010).
CC -!- FUNCTION: Digests TAMe (p-toluene arginine methyl ester), but not ethyl
CC N-benzoyl-L-tyrosinate (BTEE). {ECO:0000269|PubMed:19339798}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC Evidence={ECO:0000269|PubMed:19339798};
CC -!- ACTIVITY REGULATION: Inhibited by the serine protease inhibitor
CC phenylmethylsulfonyl, and trypsin inhibitors soybean trypsin inhibitor
CC and tosyllysine chloromethyl ketone. Not inhibited by dithiothreitol, a
CC cysteine protease inhibitor. {ECO:0000269|PubMed:19339798}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19339798}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC patients allergic to storage mite T.putrescentiae (PubMed:19339798,
CC PubMed:20197679, PubMed:20683648). Binds to IgE in 58% of the 110
CC patients tested (PubMed:19339798). Binds to IgE in 50% of the 44
CC elderly patients (aged 70-90) tested (PubMed:20197679). Binds to IgE in
CC 45% of the 22 young adult rhinitis patients tested allergic to mites
CC (both T.putrescentiae and D.pteronyssinus). This protein might be a
CC T.putrescentiae specific allergen since it cannot be absorbed by group
CC 3 allergen (Der p 3) of D.pteronyssinus in the IgE immunoblot
CC inhibition assay (PubMed:20683648). Is able to induce histamine release
CC from human basophils (PubMed:19339798). {ECO:0000269|PubMed:19339798,
CC ECO:0000269|PubMed:20197679, ECO:0000269|PubMed:20683648}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR EMBL; EU302595; ABZ81991.1; -; mRNA.
DR AlphaFoldDB; C6ZDB5; -.
DR SMR; C6ZDB5; -.
DR Allergome; 3903; Tyr p 3.
DR Allergome; 9493; Tyr p 3.0101.
DR MEROPS; S01.234; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
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 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.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..33
FT /evidence="ECO:0000255, ECO:0000305|PubMed:19339798"
FT /id="PRO_0000448081"
FT CHAIN 34..285
FT /note="Trypsin Tyr p 3.0101"
FT /evidence="ECO:0000305|PubMed:19339798"
FT /id="PRO_5002974670"
FT DOMAIN 34..262
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 73
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 120
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 218
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT SITE 212
FT /note="Required for specificity"
FT /evidence="ECO:0000305"
FT DISULFID 58..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 186..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 214..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 285 AA; 30177 MW; F2A44EF14AC2045E CRC64;
MKILLFLCFL VSVAFAKPPT IQLKSNTKSQ NGFIVGGTEA VDGDAPHQVS LQHTSHFCGG
SIISERWILT AAHCIDADDL SNPGGMSVRY NTLNLKSGTL VKVKSIKVHE QYSNVTSDND
IALLETVASM NLNQTNAVAA KLPAKGNDPQ DGDLFLSGWG TLHSGDTTIP TNLQKVTVPL
TNRSVCAEAY TGIVNITENM FCAGKMGIGG VDSCQGDSGG GAMLNKELVG VVSFGVGCGD
PKYPGVYTRV SQYLDWIELS AKSSATTLVA VNITLFLTLF IGAIW
