PEPT1_DERFA
ID PEPT1_DERFA Reviewed; 321 AA.
AC P16311;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Peptidase 1;
DE EC=3.4.22.65;
DE AltName: Full=Allergen Der f I;
DE AltName: Full=Major mite fecal allergen Der f 1;
DE AltName: Allergen=Der f 1;
DE Flags: Precursor;
GN Name=DERF1;
OS Dermatophagoides farinae (American house dust mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC Pyroglyphidae; Dermatophagoidinae; Dermatophagoides.
OX NCBI_TaxID=6954;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 98-309.
RA Kent N., Hill M.R., Keen J.N., Holland P.W., Hart B.J.;
RL Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 99-128.
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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 99-321, SUBUNIT, DISULFIDE BONDS,
RP AND GLYCOSYLATION AT ASN-151.
RX PubMed=19136006; DOI=10.1016/j.jmb.2008.12.049;
RA Chruszcz M., Chapman M.D., Vailes L.D., Stura E.A., Saint-Remy J.M.,
RA Minor W., Pomes A.;
RT "Crystal structures of mite allergens Der f 1 and Der p 1 reveal
RT differences in surface-exposed residues that may influence antibody
RT binding.";
RL J. Mol. Biol. 386:520-530(2009).
CC -!- FUNCTION: Thiol protease that hydrolyzes proteins, with a preference
CC for Phe or basic residues.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Broad endopeptidase specificity.; EC=3.4.22.65;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19136006}.
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}.
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DR EMBL; X65196; CAA46316.1; -; Genomic_DNA.
DR PIR; A27634; A27634.
DR PIR; A61500; A61500.
DR PDB; 5VPK; X-ray; 2.00 A; A/B/C=99-321.
DR PDB; 5VPL; X-ray; 1.90 A; A=99-321.
DR PDBsum; 5VPK; -.
DR PDBsum; 5VPL; -.
DR AlphaFoldDB; P16311; -.
DR SMR; P16311; -.
DR ChEMBL; CHEMBL3351205; -.
DR Allergome; 295; Der f 1.
DR Allergome; 5896; Der f 1.0106.
DR MEROPS; C01.073; -.
DR iPTMnet; P16311; -.
DR ABCD; P16311; 1 sequenced antibody.
DR BRENDA; 3.4.22.65; 1872.
DR EvolutionaryTrace; P16311; -.
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; Secreted; Signal; Thiol protease;
KW Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..98
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:3372999"
FT /id="PRO_0000026374"
FT CHAIN 99..321
FT /note="Peptidase 1"
FT /id="PRO_0000026375"
FT ACT_SITE 133
FT /evidence="ECO:0000250"
FT ACT_SITE 269
FT /evidence="ECO:0000250"
FT ACT_SITE 288
FT /evidence="ECO:0000250"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19136006"
FT DISULFID 102..216
FT /evidence="ECO:0000269|PubMed:19136006"
FT DISULFID 130..170
FT /evidence="ECO:0000269|PubMed:19136006"
FT DISULFID 164..202
FT /evidence="ECO:0000269|PubMed:19136006"
FT CONFLICT 201
FT /note="R -> Q (in Ref. 2; CAA46316)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="D -> V (in Ref. 2; CAA46316)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 36435 MW; 04523E54EEBB476E CRC64;
MKFVLAIASL LVLSTVYARP ASIKTFEEFK KAFNKNYATV EEEEVARKNF LESLKYVEAN
KGAINHLSDL SLDEFKNRYL MSAEAFEQLK TQFDLNAETS ACRINSVNVP SELDLRSLRT
VTPIRMQGGC GSCWAFSGVA ATESAYLAYR NTSLDLSEQE LVDCASQHGC HGDTIPRGIE
YIQQNGVVEE RSYPYVAREQ RCRRPNSQHY GISNYCQIYP PDVKQIREAL TQTHTAIAVI
IGIKDLRAFQ HYDGRTIIQH DNGYQPNYHA VNIVGYGSTQ GDDYWIVRNS WDTTWGDSGY
GYFQAGNNLM MIEQYPYVVI M
