ALL21_DERPT
ID ALL21_DERPT Reviewed; 140 AA.
AC Q2L7C5;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Mite allergen Der p 21.0101 {ECO:0000305};
DE AltName: Full=Allergen Der p 21 {ECO:0000303|PubMed:18445190, ECO:0000303|PubMed:24874917, ECO:0000303|PubMed:29319884};
DE AltName: Allergen=Der p 21.0101 {ECO:0000305};
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:ABC73706.1};
RN [1] {ECO:0000312|EMBL:ABC73706.1}
RP NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ALLERGEN, AND CIRCULAR DICHROISM
RP ANALYSIS.
RX PubMed=18445190; DOI=10.1111/j.1398-9995.2008.01647.x;
RA Weghofer M., Dall'Antonia Y., Grote M., Stocklinger A., Kneidinger M.,
RA Balic N., Krauth M.T., Fernandez-Caldas E., Thomas W.R., van Hage M.,
RA Vieths S., Spitzauer S., Horak F., Svergun D.I., Konarev P.V., Valent P.,
RA Thalhamer J., Keller W., Valenta R., Vrtala S.;
RT "Characterization of Der p 21, a new important allergen derived from the
RT gut of house dust mites.";
RL Allergy 63:758-767(2008).
RN [2]
RP SUBUNIT, ALLERGEN, BIOTECHNOLOGY, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=24874917; DOI=10.1016/j.pep.2014.05.001;
RA Pulsawat P., Theeraapisakkun M., Nony E., Le Mignon M., Jain K.,
RA Buaklin A., Wongpiyabovorn J., Ruxrungtham K., Jacquet A.;
RT "Characterization of the house dust mite allergen Der p 21 produced in
RT Pichia pastoris.";
RL Protein Expr. Purif. 101:8-13(2014).
RN [3]
RP ALLERGEN, BIOTECHNOLOGY, REGIONS, AND 3D-STRUCTURE MODELING.
RX PubMed=29319884; DOI=10.1111/all.13398;
RA Curin M., Garmatiuk T., Resch-Marat Y., Chen K.W., Hofer G., Fauland K.,
RA Keller W., Hemmer W., Vrtala S., Focke-Tejkl M., Valenta R.;
RT "Similar localization of conformational IgE epitopes on the house dust mite
RT allergens Der p 5 and Der p 21 despite limited IgE cross-reactivity.";
RL Allergy 73:1653-1661(2018).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable. Upon heating, unfolds only partially even at 95 degrees
CC Celsius. Upon cooling to room temperature, almost completely restores
CC its structure, indicating high heat stability and refolding capacity.
CC {ECO:0000269|PubMed:18445190};
CC -!- SUBUNIT: Monomer (PubMed:24874917). Homodimer (PubMed:18445190).
CC {ECO:0000269|PubMed:18445190, ECO:0000269|PubMed:24874917}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18445190}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:18445190}. Vesicle
CC {ECO:0000269|PubMed:18445190}. Secreted {ECO:0000269|PubMed:18445190}.
CC Note=Associated with cytoplasmic matrix, detached cytoplasmatic
CC material and with electron-dense droplets, which presumably represent
CC transport vesicles. {ECO:0000269|PubMed:18445190}.
CC -!- TISSUE SPECIFICITY: Expressed in the epithelium, lumen and microvilli
CC of the midgut, and in feces. {ECO:0000269|PubMed:18445190}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Recombinant protein
CC binds to IgE in patients allergic to house dust mite (HDM)
CC (PubMed:18445190, PubMed:24874917, PubMed:29319884). Recombinant
CC protein binds to IgE in 26% of the 117 patients tested living in urban
CC area in Austria allergic to European HDM (PubMed:18445190). Recombinant
CC protein binds to IgE in 25% of the 96 patients tested living in Bangkok
CC allergic to European HDM (PubMed:24874917). No relevant cross-
CC reactivity with Der p 5 allergen (PubMed:18445190, PubMed:29319884). No
CC relevant cross-reactivity with Blot t 5 or Lep d 5 allergens. Causes
CC histamine release from human peripheral blood mononuclear leukocytes.
CC Up-regulates expression of CD203c activation marker on basophils.
CC Induces degranulation of humanized rat basophil leukemia (RBL) cells
CC and the release of beta-hexosaminidase from them (PubMed:18445190).
CC Triggers interleukin-8 production in human airway epithelial cells
CC through Toll-like receptor 2 (TLR2)-dependent signaling
CC (PubMed:24874917). {ECO:0000269|PubMed:18445190,
CC ECO:0000269|PubMed:24874917, ECO:0000269|PubMed:29319884}.
CC -!- BIOTECHNOLOGY: The Pichia pastoris-produced protein seems to be well
CC suited for in vitro immune cell activation assays and for in vivo
CC applications such as immunotherapy and skin-prick testing, because it
CC is properly folded, free of endotoxins and has the appropriate
CC allergenic characteristics (PubMed:24874917). Non-allergenic peptides
CC identified from the mapped major conformational IgE epitope-containing
CC areas could be used for the engineering of house dust mite allergy
CC vaccine (PubMed:29319884). {ECO:0000305|PubMed:24874917,
CC ECO:0000305|PubMed:29319884}.
CC -!- SIMILARITY: Belongs to the mite group 5 allergen family. {ECO:0000305}.
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DR EMBL; DQ354124; ABC73706.1; -; mRNA.
DR AlphaFoldDB; Q2L7C5; -.
DR SMR; Q2L7C5; -.
DR Allergome; 2863; Der p 21.
DR Allergome; 3262; Der p 21.0101.
DR Proteomes; UP000515146; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR Gene3D; 1.20.58.970; -; 1.
DR InterPro; IPR020306; Mite_allergen_group-5/21.
DR InterPro; IPR038455; Mite_allergen_group-5/21_sf.
DR Pfam; PF11642; Blo-t-5; 1.
PE 1: Evidence at protein level;
KW Allergen; Cytoplasm; Endoplasmic reticulum; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..140
FT /note="Mite allergen Der p 21.0101"
FT /evidence="ECO:0000255"
FT /id="PRO_5004212025"
FT REGION 20..53
FT /note="Immunodominant conformational IgE-binding epitope"
FT /evidence="ECO:0000269|PubMed:29319884"
FT REGION 108..140
FT /note="Immunodominant conformational IgE-binding epitope"
FT /evidence="ECO:0000269|PubMed:29319884"
SQ SEQUENCE 140 AA; 16531 MW; FE47CFD322A5B61C CRC64;
MKFIITLFAA IVMAAAVSGF IVGDKKEDEW RMAFDRLMME ELETKIDQVE KGLLHLSEQY
KELEKTKSKE LKEQILRELT IGENFMKGAL KFFEMEAKRT DLNMFERYNY EFALESIKLL
IKKLDELAKK VKAVNPDEYY
