DEP23_DERPT
ID DEP23_DERPT Reviewed; 90 AA.
AC L7N6F8;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Major mite allergen Der p 23 {ECO:0000303|PubMed:23460742, ECO:0000303|PubMed:26602749};
DE AltName: Full=Major house dust mite allergen Der p 23 {ECO:0000303|PubMed:24733847};
DE Short=Major HDM allergen Der p 23 {ECO:0000303|PubMed:24733847};
DE AltName: Full=Peritrophin-like protein Der p 23 {ECO:0000303|PubMed:23460742};
DE AltName: Allergen=Der p 23 {ECO:0000303|PubMed:23460742, ECO:0000303|PubMed:26602749};
DE Flags: Precursor;
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 {ECO:0000312|EMBL:ACB46292.1};
RN [1] {ECO:0000312|EMBL:ACB46292.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND ALLERGEN.
RX PubMed=23460742; DOI=10.4049/jimmunol.1202288;
RA Weghofer M., Grote M., Resch Y., Casset A., Kneidinger M., Kopec J.,
RA Thomas W.R., Fernandez-Caldas E., Kabesch M., Ferrara R., Mari A.,
RA Purohit A., Pauli G., Horak F., Keller W., Valent P., Valenta R.,
RA Vrtala S.;
RT "Identification of Der p 23, a Peritrophin-like Protein, as a New Major
RT Dermatophagoides pteronyssinus Allergen Associated with the Peritrophic
RT Matrix of Mite Fecal Pellets.";
RL J. Immunol. 190:3059-3067(2013).
RN [2]
RP ALLERGEN, BIOTECHNOLOGY, AND REGION.
RX PubMed=24733847; DOI=10.4049/jimmunol.1400064;
RA Banerjee S., Weber M., Blatt K., Swoboda I., Focke-Tejkl M., Valent P.,
RA Valenta R., Vrtala S.;
RT "Conversion of Der p 23, a new major house dust mite allergen, into a
RT hypoallergenic vaccine.";
RL J. Immunol. 192:4867-4875(2014).
RN [3] {ECO:0007744|PDB:4ZCE}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 44-90, FUNCTION, SUBUNIT,
RP ALLERGEN, AND DISULFIDE BONDS.
RX PubMed=26602749; DOI=10.1111/cea.12680;
RA Mueller G.A., Randall T.A., Glesner J., Pedersen L.C., Perera L.,
RA Edwards L.L., DeRose E.F., Chapman M.D., London R.E., Pomes A.;
RT "Serological, genomic and structural analyses of the major mite allergen
RT Der p 23.";
RL Clin. Exp. Allergy 46:365-376(2016).
CC -!- FUNCTION: Does not bind chitin in vitro. {ECO:0000269|PubMed:26602749}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23460742,
CC ECO:0000269|PubMed:26602749}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23460742}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:23460742}. Cytoplasmic
CC vesicle {ECO:0000269|PubMed:23460742}. Note=Localizes to the
CC peritrophic matrix ligning the midgut and on the surface of fecal
CC pellets. {ECO:0000269|PubMed:23460742}.
CC -!- TISSUE SPECIFICITY: Expressed in epithelial cells of the midgut.
CC {ECO:0000269|PubMed:23460742}.
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 74% of 374 house dust mite allergic patients from
CC different countries. {ECO:0000269|PubMed:23460742,
CC ECO:0000269|PubMed:24733847, ECO:0000269|PubMed:26602749}.
CC -!- BIOTECHNOLOGY: Non-allergenic peptides derived from the C-terminal IgE
CC epitope-containing part might be used for immunotherapy to desensitize
CC individuals with mite allergy. {ECO:0000269|PubMed:24733847}.
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DR EMBL; EU414751; ACB46292.1; -; mRNA.
DR PDB; 4ZCE; X-ray; 1.55 A; A/B=44-90.
DR PDBsum; 4ZCE; -.
DR AlphaFoldDB; L7N6F8; -.
DR SMR; L7N6F8; -.
DR Allergome; 5747; Der p 23.
DR Allergome; 5748; Der p 23.0101.
DR Proteomes; UP000515146; Unplaced.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0019863; F:IgE binding; IMP:UniProtKB.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR Pfam; PF01607; CBM_14; 1.
DR SUPFAM; SSF57625; SSF57625; 1.
DR PROSITE; PS50940; CHIT_BIND_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Cytoplasmic vesicle; Disulfide bond;
KW Endoplasmic reticulum; IgE-binding protein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000305|PubMed:23460742"
FT CHAIN 22..90
FT /note="Major mite allergen Der p 23"
FT /evidence="ECO:0000255"
FT /id="PRO_5003982384"
FT DOMAIN 44..90
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT REGION 22..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..90
FT /note="Important for IgE-binding"
FT /evidence="ECO:0000269|PubMed:24733847"
FT COMPBIAS 23..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 47..66
FT /evidence="ECO:0000269|PubMed:26602749,
FT ECO:0007744|PDB:4ZCE"
FT DISULFID 76..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144,
FT ECO:0000269|PubMed:26602749, ECO:0007744|PDB:4ZCE"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:4ZCE"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:4ZCE"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:4ZCE"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:4ZCE"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:4ZCE"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:4ZCE"
SQ SEQUENCE 90 AA; 10343 MW; 0002F9AE12ABA0EC CRC64;
MKFNIIIVFI SLAILVHSSY AANDNDDDPT TTVHPTTTEQ PDDKFECPSR FGYFADPKDP
HKFYICSNWE AVHKDCPGNT RWNEDEETCT
