ID   EURM3_EURMA             Reviewed;         261 AA.
AC   O97370;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Mite allergen Eur m 3;
DE            EC=3.4.21.-;
DE   AltName: Allergen=Eur m 3;
DE   Flags: Precursor;
GN   Name=EURM3;
OS   Euroglyphus maynei (Mayne's house dust mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC   Pyroglyphidae; Pyroglyphinae; Euroglyphus.
OX   NCBI_TaxID=6958;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Smith W., Hart B.J., Thomas W.R.;
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Common symptoms of mite
CC       allergy are bronchial asthma, allergic rhinitis and conjunctivitis.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; AF047615; AAD10712.1; -; mRNA.
DR   AlphaFoldDB; O97370; -.
DR   SMR; O97370; -.
DR   Allergome; 3276; Eur m 3.0101.
DR   Allergome; 343; Eur m 3.
DR   MEROPS; S01.234; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   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..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..29
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000028149"
FT   CHAIN           30..261
FT                   /note="Mite allergen Eur m 3"
FT                   /id="PRO_0000028150"
FT   DOMAIN          30..260
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        69
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        114
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        214
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   SITE            208
FT                   /note="Required for specificity"
FT   DISULFID        54..70
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        181..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        210..236
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   261 AA;  28038 MW;  6B53BFE63B3850BC CRC64;
     MVICNAIIVL LLAFNTLANP ILPSSPNATI VGGQKAKAGE CPYQISLQSS SHFCGGTILD
     EYWILTAAHC VNGQTASKLS IRYNSLKHAS GGEKLSVAQI YQHEKYDSWT IDNDIALIKL
     QSPMTLDQKN AKSVQLPSQG SDVKVGDKVR VSGWGYLKEG SYSLPSDMYR VDIDIVAREQ
     CNKLYEEAGA TITDNMICGG NVADGGVDSC QGDSGGPVVD VASNQIVGIV SWGYGCARKG
     YPGVYTRVGS FIDWIDSKRS Q