PEPT1_DERPT
ID PEPT1_DERPT Reviewed; 320 AA.
AC P08176; Q24616;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Peptidase 1;
DE EC=3.4.22.65;
DE AltName: Full=Allergen Der p I;
DE AltName: Full=Major mite fecal allergen Der p 1;
DE AltName: Allergen=Der p 1;
DE Flags: Precursor;
GN Name=DERP1;
OS Dermatophagoides pteronyssinus (European house dust mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC Pyroglyphidae; Dermatophagoidinae; Dermatophagoides.
OX NCBI_TaxID=6956;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND POLYMORPHISM.
RX PubMed=8353459; DOI=10.1159/000236478;
RA Chua K.Y., Kehal P.K., Thomas W.R.;
RT "Sequence polymorphisms of cDNA clones encoding the mite allergen Der p
RT I.";
RL Int. Arch. Allergy Immunol. 101:364-368(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 76-320.
RX PubMed=3335830; DOI=10.1084/jem.167.1.175;
RA Chua K.Y., Stewart G.A., Thomas W.R., Simpson R.J., Dilworth R.J.,
RA Plozza T.M., Turner K.J.;
RT "Sequence analysis of cDNA coding for a major house dust mite allergen, Der
RT p 1. Homology with cysteine proteases.";
RL J. Exp. Med. 167:175-182(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 81-176.
RX PubMed=3276629; DOI=10.1159/000234488;
RA Thomas W.R., Stewart G.A., Simpson R.J., Chua K.Y., Plozza T.M.,
RA Dilworth R.J., Nisbet A., Turner K.J.;
RT "Cloning and expression of DNA coding for the major house dust mite
RT allergen Der p 1 in Escherichia coli.";
RL Int. Arch. Allergy Appl. Immunol. 85:127-129(1988).
RN [4]
RP SEQUENCE REVISION TO 232-241.
RX PubMed=2021874; DOI=10.1111/j.1365-2222.1991.tb00800.x;
RA Dilworth R.J., Chua K.Y., Thomas W.R.;
RT "Sequence analysis of cDNA coding for a major house dust mite allergen, Der
RT f I.";
RL Clin. Exp. Allergy 21:25-32(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 99-308.
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).
RN [6]
RP PROTEIN SEQUENCE OF 99-127.
RX PubMed=3372999;
RA Lind P., Hansen O.C., Horn N.;
RT "The binding of mouse hybridoma and human IgE antibodies to the major fecal
RT allergen, Der p I, of Dermatophagoides pteronyssinus. Relative binding site
RT location and species specificity studied by solid-phase inhibition assays
RT with radiolabeled antigen.";
RL J. Immunol. 140:4256-4262(1988).
RN [7]
RP PROTEIN SEQUENCE OF 99-139; 177-192; 208-224 AND 260-277, AND VARIANT
RP ALA-222.
RX PubMed=2911558;
RA Simpson R.J., Nice E.C., Moritz R.L., Stewart G.A.;
RT "Structural studies on the allergen Der p1 from the house dust mite
RT Dermatophagoides pteronyssinus: similarity with cysteine proteinases.";
RL Protein Seq. Data Anal. 2:17-21(1989).
RN [8]
RP 3D-STRUCTURE MODELING.
RX PubMed=7971950; DOI=10.1093/protein/7.7.869;
RA Topham C.M., Srinivasan N., Thorpe C.J., Overington J.P., Kalsheker N.A.;
RT "Comparative modelling of major house dust mite allergen Der p I: structure
RT validation using an extended environmental amino acid propensity table.";
RL Protein Eng. 7:869-894(1994).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF 22-320 OF MUTANT ALA-132/GLU-150,
RP PROTEIN SEQUENCE OF N-TERMINUS, AND GLYCOSYLATION AT ASN-150.
RX PubMed=16148130; DOI=10.4049/jimmunol.175.6.3835;
RA Meno K., Thorsted P.B., Ipsen H., Kristensen O., Larsen J.N.,
RA Spangfort M.D., Gajhede M., Lund K.;
RT "The crystal structure of recombinant proDer p 1, a major house dust mite
RT proteolytic allergen.";
RL J. Immunol. 175:3835-3845(2005).
CC -!- FUNCTION: Thiol protease, with a preference for substrates with a large
CC hydrophobic side chain in the P2 position, or with basic residues.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Broad endopeptidase specificity.; EC=3.4.22.65;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: N-glycosylated. N-glycanase treatment does not completely remove
CC carbohydrates, suggesting that the protein contains additional
CC glycosylation sites. {ECO:0000269|PubMed:16148130}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Common symptoms of mite
CC allergy are bronchial asthma, allergic rhinitis and conjunctivitis.
CC Binds to IgE in 80% of patients with house dust allergy.
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=AAA28296.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U11695; AAB60215.1; -; mRNA.
DR EMBL; M24794; AAA28296.1; ALT_INIT; mRNA.
DR EMBL; X65197; CAA46317.1; -; Genomic_DNA.
DR PIR; JQ0337; JQ0337.
DR PDB; 1XKG; X-ray; 1.61 A; A=19-320.
DR PDB; 2AS8; X-ray; 1.95 A; A/B=99-320.
DR PDB; 5VCN; X-ray; 3.00 A; A/B=99-320.
DR PDB; 5VCO; X-ray; 2.74 A; E/F=99-320.
DR PDB; 5VPG; X-ray; 1.95 A; A=99-320.
DR PDB; 5VPH; X-ray; 2.50 A; A=99-320.
DR PDBsum; 1XKG; -.
DR PDBsum; 2AS8; -.
DR PDBsum; 5VCN; -.
DR PDBsum; 5VCO; -.
DR PDBsum; 5VPG; -.
DR PDBsum; 5VPH; -.
DR AlphaFoldDB; P08176; -.
DR SMR; P08176; -.
DR BindingDB; P08176; -.
DR ChEMBL; CHEMBL3351204; -.
DR Allergome; 1232; Der p 1.0111.
DR Allergome; 310; Der p 1.
DR MEROPS; C01.073; -.
DR iPTMnet; P08176; -.
DR ABCD; P08176; 6 sequenced antibodies.
DR BRENDA; 3.4.22.65; 1873.
DR EvolutionaryTrace; P08176; -.
DR Proteomes; UP000515146; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02248; Peptidase_C1A; 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; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
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; SSF54001; 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 3D-structure; Allergen; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Protease; Reference proteome; Secreted; Signal;
KW Thiol protease; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:16148130"
FT PROPEP 19..98
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:16148130,
FT ECO:0000269|PubMed:2911558, ECO:0000269|PubMed:3372999"
FT /id="PRO_0000026376"
FT CHAIN 99..320
FT /note="Peptidase 1"
FT /id="PRO_0000026377"
FT ACT_SITE 132
FT /evidence="ECO:0000250"
FT ACT_SITE 268
FT /evidence="ECO:0000250"
FT ACT_SITE 288
FT /evidence="ECO:0000250"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16148130"
FT DISULFID 102..215
FT DISULFID 129..169
FT DISULFID 163..201
FT VARIANT 148
FT /note="Y -> H"
FT VARIANT 179
FT /note="E -> K"
FT VARIANT 222
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:2911558"
FT VARIANT 234
FT /note="S -> T"
FT VARIANT 313
FT /note="E -> Q"
FT MUTAGEN 132
FT /note="C->A: Loss of activity."
FT MUTAGEN 150
FT /note="N->E: Loss of N-glycosylation."
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:1XKG"
FT HELIX 40..60
FT /evidence="ECO:0007829|PDB:1XKG"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:1XKG"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:1XKG"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:1XKG"
FT TURN 114..118
FT /evidence="ECO:0007829|PDB:1XKG"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1XKG"
FT HELIX 132..149
FT /evidence="ECO:0007829|PDB:1XKG"
FT HELIX 157..163
FT /evidence="ECO:0007829|PDB:1XKG"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:1XKG"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1XKG"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:1XKG"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:1XKG"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:1XKG"
FT STRAND 236..243
FT /evidence="ECO:0007829|PDB:1XKG"
FT HELIX 245..249
FT /evidence="ECO:0007829|PDB:1XKG"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1XKG"
FT STRAND 266..278
FT /evidence="ECO:0007829|PDB:1XKG"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:1XKG"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:1XKG"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:1XKG"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:1XKG"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:1XKG"
SQ SEQUENCE 320 AA; 36104 MW; A0B1F4DD09791DFE CRC64;
MKIVLAIASL LALSAVYARP SSIKTFEEYK KAFNKSYATF EDEEAARKNF LESVKYVQSN
GGAINHLSDL SLDEFKNRFL MSAEAFEHLK TQFDLNAETN ACSINGNAPA EIDLRQMRTV
TPIRMQGGCG SCWAFSGVAA TESAYLAYRN QSLDLAEQEL VDCASQHGCH GDTIPRGIEY
IQHNGVVQES YYRYVAREQS CRRPNAQRFG ISNYCQIYPP NVNKIREALA QTHSAIAVII
GIKDLDAFRH YDGRTIIQRD NGYQPNYHAV NIVGYSNAQG VDYWIVRNSW DTNWGDNGYG
YFAANIDLMM IEEYPYVVIL
