ID   PEPT1_EURMA             Reviewed;         321 AA.
AC   P25780; Q9TZZ3; Q9TZZ4; Q9UBA0;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 2.
DT   02-SEP-2026, entry version 107.
DE   RecName: Full=Peptidase 1;
DE            EC=3.4.22.65;
DE   AltName: Full=Allergen Eur m I;
DE   AltName: Full=Mite group 1 allergen Eur m 1;
DE   AltName: Allergen=Eur m 1;
DE   Flags: Precursor;
GN   Name=EURM1;
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] (EUR M 1.0101 AND EUR M 1.0102).
RX   PubMed=9925958; DOI=10.1159/000024026;
RA   Smith W., Mills K., Hazell L., Hart B.J., Thomas W.;
RT   "Molecular analysis of the group 1 and 2 allergens from the house dust
RT   mite, Euroglyphus maynei.";
RL   Int. Arch. Allergy Immunol. 118:15-22(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 99-309.
RX   PubMed=1483062; DOI=10.1159/000236349;
RA   Kent N.A., Hill M.R., Keen J.N., Holland P.W., Hart B.J.;
RT   "Molecular characterisation of group I allergen Eur m I from house dust
RT   mite Euroglyphus maynei.";
RL   Int. Arch. Allergy Immunol. 99:150-152(1992).
CC   -!- FUNCTION: Probable thiol protease.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Broad endopeptidase specificity.; EC=3.4.22.65;
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 C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC       ECO:0000255|PROSITE-ProRule:PRU10090}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC82352.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF047610; AAC82351.1; -; mRNA.
DR   EMBL; AF047611; AAC82352.1; ALT_INIT; mRNA.
DR   EMBL; AF047612; AAC82353.1; -; mRNA.
DR   EMBL; X60073; CAA42677.1; -; Genomic_DNA.
DR   PIR; S21864; S21864.
DR   AlphaFoldDB; P25780; -.
DR   SMR; P25780; -.
DR   Allergome; 1359; Eur m 1.0101.
DR   Allergome; 1360; Eur m 1.0102.
DR   Allergome; 338; Eur m 1.
DR   MEROPS; C01.073; -.
DR   GlyCosmos; P25780; 2 sites, No reported glycans.
DR   OrthoDB; 10253408at2759; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00848; Inhibitor_I29; 1.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   1: Evidence at protein level;
KW   Allergen; Disulfide bond; Glycoprotein; Hydrolase; Protease; Secreted;
KW   Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..98
FT                   /id="PRO_0000026378"
FT   CHAIN           99..321
FT                   /note="Peptidase 1"
FT                   /id="PRO_0000026379"
FT   ACT_SITE        133
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        289
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        34
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        130..170
FT                   /evidence="ECO:0000250"
FT   VARIANT         36
FT                   /note="T -> S (in Eur m 1.0102)"
FT   VARIANT         126
FT                   /note="M -> N (in Eur m 1.0102)"
FT   VARIANT         320
FT                   /note="M -> I (in Eur m 1.0102)"
SQ   SEQUENCE   321 AA;  36290 MW;  6CFD44FEC725999E CRC64;
     MKIILAIASL LVLSAVYARP ASIKTFEEFK KAFNKTYATP EKEEVARKNF LESLKYVESN
     KGAINHLSDL SLDEFKNQFL MNANAFEQLK TQFDLNAETY ACSINSVSLP SELDLRSLRT
     VTPIRMQGGC GSCWAFSGVA STESAYLAYR NMSLDLAEQE LVDCASQNGC HGDTIPRGIE
     YIQQNGVVQE HYYPYVAREQ SCHRPNAQRY GLKNYCQISP PDSNKIRQAL TQTHTAVAVI
     IGIKDLNAFR HYDGRTIMQH DNGYQPNYHA VNIVGYGNTQ GVDYWIVRNS WDTTWGDNGY
     GYFAANINLM MIEQYPYVVM L
//