BLOT3_BLOTA
ID BLOT3_BLOTA Reviewed; 266 AA.
AC A1KXI1;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Trypsin Blo t 3 {ECO:0000305};
DE EC=3.4.21.4 {ECO:0000250|UniProtKB:P35030};
DE AltName: Full=Mite allergen Blo t 3 {ECO:0000303|PubMed:12708986};
DE AltName: Allergen=Blo t 3 {ECO:0000303|PubMed:12708986, ECO:0000303|PubMed:12752596};
DE Flags: Precursor;
OS Blomia tropicalis (Mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Glycyphagoidea; Echimyopodidae;
OC Blomia.
OX NCBI_TaxID=40697 {ECO:0000312|EMBL:AAQ24542.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RX PubMed=12708986; DOI=10.1034/j.1398-9995.2003.00033.x;
RA Cheong N., Yang L., Lee B.W., Chua K.Y.;
RT "Cloning of a group 3 allergen from Blomia tropicalis mites.";
RL Allergy 58:352-356(2003).
RN [2] {ECO:0000312|EMBL:AAQ24542.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chew F.T., Wang W.-L., Shang H.S., Kuay K.T., Lim S.H., Lee B.W.;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION, AND ALLERGEN.
RX PubMed=12752596; DOI=10.1046/j.1365-2222.2003.01648.x;
RA Yang L., Cheong N., Wang D.Y., Lee B.W., Kuo I.C., Huang C.H., Chua K.Y.;
RT "Generation of monoclonal antibodies against Blo t 3 using DNA immunization
RT with in vivo electroporation.";
RL Clin. Exp. Allergy 33:663-668(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC Evidence={ECO:0000250|UniProtKB:P35030};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12752596}.
CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:12708986,
CC PubMed:12752596). Recombinant protein binds to IgE in 51% of the 45
CC patients tested allergic to B.tropicalis mites (PubMed:12708986).
CC Native protein binds to IgE in 57% of the 44 patients tested allergic
CC to B.tropicalis mites (PubMed:12752596). {ECO:0000269|PubMed:12708986,
CC ECO:0000269|PubMed:12752596}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274, ECO:0000305}.
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DR EMBL; AY291323; AAQ24542.1; -; mRNA.
DR AlphaFoldDB; A1KXI1; -.
DR SMR; A1KXI1; -.
DR Allergome; 687; Blo t 3.
DR MEROPS; S01.234; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Allergen; Disulfide bond; Hydrolase; Protease; Secreted; Serine protease;
KW Signal; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT PROPEP 16..35
FT /evidence="ECO:0000250|UniProtKB:P39675, ECO:0000255"
FT /id="PRO_0000447699"
FT CHAIN 36..266
FT /note="Trypsin Blo t 3"
FT /id="PRO_5012813329"
FT DOMAIN 36..260
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 75
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 220
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT SITE 214
FT /note="Required for specificity"
FT /evidence="ECO:0000305"
FT DISULFID 60..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 187..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 216..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 38
FT /note="D -> G (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="A -> T (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="S -> P (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="E -> K (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 266 AA; 27555 MW; 149251A6FC8CE0DC CRC64;
MKVLVLFCLV SLAAAGPLKD ALNKAQVDAF YAEGYIVDGS NAADGDAPYQ VSLQRTSHFC
GGSIIADNYI LTAAHCIQGL SASSLTIRYN TLRHNSGGLT VKASRIIGHE KYDSNTIDND
IALIQTASKM STGTTNAQAI KLPEQGSDPK ASSEVLITGW GTLSSGASSL PTKLQKVTVP
IVDRKTCNAN YGAVGADITD NMFCAGILNV GGKDACQGDS GGPVAANGVL VGAVSWGYGC
AQAKYPGVYT RVGNYISWIK GKGVPV