DERP3_DERPT
ID DERP3_DERPT Reviewed; 261 AA.
AC P39675;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Mite allergen Der p 3;
DE EC=3.4.21.-;
DE AltName: Full=Allergen Der p III;
DE AltName: Allergen=Der p 3;
DE Flags: Precursor;
GN Name=DERP3;
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 PROTEIN SEQUENCE OF 30-59.
RX PubMed=8012853; DOI=10.1111/j.1365-2222.1994.tb00223.x;
RA Smith W.-A., Chua K.-Y., Kuo M.C., Rogers B.L., Thomas W.R.;
RT "Cloning and sequencing of the Dermatophagoides pteronyssinus group III
RT allergen, Der p III.";
RL Clin. Exp. Allergy 24:220-228(1994).
RN [2]
RP PROTEIN SEQUENCE OF 30-47 AND 223-229.
RX PubMed=1537598;
RA Stewart G.A., Ward L.D., Simpson R.J., Thompson P.J.;
RT "The group III allergen from the house dust mite Dermatophagoides
RT pteronyssinus is a trypsin-like enzyme.";
RL Immunology 75:29-35(1992).
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; U11719; AAA19973.1; -; mRNA.
DR AlphaFoldDB; P39675; -.
DR SMR; P39675; -.
DR Allergome; 317; Der p 3.
DR Allergome; 3263; Der p 3.0101.
DR MEROPS; S01.031; -.
DR SABIO-RK; P39675; -.
DR Proteomes; UP000515146; Unplaced.
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; Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..29
FT /evidence="ECO:0000269|PubMed:1537598,
FT ECO:0000269|PubMed:8012853"
FT /id="PRO_0000028145"
FT CHAIN 30..261
FT /note="Mite allergen Der p 3"
FT /id="PRO_0000028146"
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; 28060 MW; 066C7C25E0D67FBD CRC64;
MIIYNILIVL LLAINTLANP ILPASPNATI VGGEKALAGE CPYQISLQSS SHFCGGTILD
EYWILTAAHC VAGQTASKLS IRYNSLKHSL GGEKISVAKI FAHEKYDSYQ IDNDIALIKL
KSPMKLNQKN AKAVGLPAKG SDVKVGDQVR VSGWGYLEEG SYSLPSELRR VDIAVVSRKE
CNELYSKANA EVTDNMICGG DVANGGKDSC QGDSGGPVVD VKNNQVVGIV SWGYGCARKG
YPGVYTRVGN FIDWIESKRS Q