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ALL5_DERPT
ID   ALL5_DERPT              Reviewed;         132 AA.
AC   P14004;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Mite allergen Der p 5 {ECO:0000305};
DE   AltName: Full=Allergen Der p V {ECO:0000303|PubMed:7798547};
DE   AltName: Full=IgE-binding allergen {ECO:0000303|PubMed:2794865};
DE   AltName: Allergen=Der p 5 {ECO:0000303|PubMed:18445190, ECO:0000303|PubMed:20534590, ECO:0000303|PubMed:24874917, ECO:0000303|PubMed:29319884};
GN   Name=DERP5;
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 ALLERGEN.
RX   PubMed=7798547; DOI=10.1016/0091-6749(94)90117-1;
RA   Lin K.L., Hsieh K.H., Thomas W.R., Chiang B.L., Chua K.Y.;
RT   "Characterization of Der p V allergen, cDNA analysis, and IgE-mediated
RT   reactivity to the recombinant protein.";
RL   J. Allergy Clin. Immunol. 94:989-996(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RX   PubMed=2794865; DOI=10.1084/jem.170.4.1457;
RA   Tovey E.R., Johnson M.C., Roche A.L., Cobon G.S., Baldo B.A.;
RT   "Cloning and sequencing of a cDNA expressing a recombinant house dust mite
RT   protein that binds human IgE and corresponds to an important low molecular
RT   weight allergen.";
RL   J. Exp. Med. 170:1457-1462(1989).
RN   [3]
RP   SEQUENCE REVISION TO 132.
RA   Cobon G.S.;
RL   Submitted (FEB-1990) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   ALLERGEN.
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   [5]
RP   ALLERGEN.
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   [6]
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).
RN   [7] {ECO:0007744|PDB:3MQ1}
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 34-132, SUBUNIT, AND ALLERGEN.
RX   PubMed=20534590; DOI=10.1074/jbc.m110.128306;
RA   Mueller G.A., Gosavi R.A., Krahn J.M., Edwards L.L., Cuneo M.J.,
RA   Glesner J., Pomes A., Chapman M.D., London R.E., Pedersen L.C.;
RT   "Der p 5 crystal structure provides insight into the group 5 dust mite
RT   allergens.";
RL   J. Biol. Chem. 285:25394-25401(2010).
CC   -!- SUBUNIT: Monomer. Trimer of homodimers. Oligomerizes in a
CC       concentration-dependent manner. {ECO:0000269|PubMed:20534590}.
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 patients allergic to house dust mite (HDM)
CC       (PubMed:7798547, PubMed:2794865, PubMed:18445190, PubMed:24874917,
CC       PubMed:29319884, PubMed:20534590). Recombinant protein binds to IgE in
CC       52% of the 25 patients tested (PubMed:7798547). Recombinant protein
CC       binds to IgE in 31% of the 117 patients tested living in urban area in
CC       Austria allergic to European HDM (PubMed:18445190). Recombinant protein
CC       binds to IgE in 69% of the 96 patients tested living in Bangkok
CC       allergic to European HDM (PubMed:24874917). Recombinant protein of 34-
CC       132 binds to IgE in 35% of the 62 patients tested (PubMed:20534590). In
CC       the skin tests, the recombinant protein produces positive reactions in
CC       67% of the 15 patients tested with asthma and allergic rhinitis, in 58%
CC       of the 13 patients tested with asthma alone and in 29% of the 17
CC       patients tested with allergic rhinitis alone (PubMed:7798547). No
CC       relevant cross-reactivity with Der p 21 allergen (PubMed:29319884).
CC       Causes histamine release from human peripheral blood mononuclear
CC       leukocytes. Up-regulates expression of CD203c activation marker on
CC       basophils (PubMed:18445190). {ECO:0000269|PubMed:18445190,
CC       ECO:0000269|PubMed:20534590, ECO:0000269|PubMed:24874917,
CC       ECO:0000269|PubMed:2794865, ECO:0000269|PubMed:29319884,
CC       ECO:0000269|PubMed:7798547}.
CC   -!- BIOTECHNOLOGY: Non-allergenic peptides identified from the mapped major
CC       conformational IgE epitope-containing areas could be used for the
CC       engineering of house dust mite allergy vaccine.
CC       {ECO:0000305|PubMed:29319884}.
CC   -!- SIMILARITY: Belongs to the mite group 5 allergen family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA35692.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; S76337; AAB32841.1; -; mRNA.
DR   EMBL; S76340; AAB32842.1; -; mRNA.
DR   EMBL; X17699; CAA35692.1; ALT_INIT; mRNA.
DR   PIR; S06734; S06734.
DR   PDB; 3MQ1; X-ray; 2.80 A; A/B/C/D/E/F=34-132.
DR   PDBsum; 3MQ1; -.
DR   AlphaFoldDB; P14004; -.
DR   SMR; P14004; -.
DR   Allergome; 319; Der p 5.
DR   Allergome; 3265; Der p 5.0101.
DR   Allergome; 3266; Der p 5.0102.
DR   EvolutionaryTrace; P14004; -.
DR   Proteomes; UP000515146; Unplaced.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR   GO; GO:0051259; P:protein complex oligomerization; 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   3D-structure; Allergen; Reference proteome.
FT   CHAIN           1..132
FT                   /note="Mite allergen Der p 5"
FT                   /id="PRO_0000151066"
FT   REGION          25..53
FT                   /note="Immunodominant conformational IgE-binding epitope"
FT                   /evidence="ECO:0000269|PubMed:29319884"
FT   REGION          102..132
FT                   /note="Immunodominant conformational IgE-binding epitope"
FT                   /evidence="ECO:0000269|PubMed:29319884"
FT   VARIANT         61
FT                   /note="E -> A"
FT   HELIX           35..61
FT                   /evidence="ECO:0007829|PDB:3MQ1"
FT   HELIX           65..93
FT                   /evidence="ECO:0007829|PDB:3MQ1"
FT   HELIX           100..128
FT                   /evidence="ECO:0007829|PDB:3MQ1"
SQ   SEQUENCE   132 AA;  15615 MW;  3C840C3C26707C05 CRC64;
     MKFIIAFFVA TLAVMTVSGE DKKHDYQNEF DFLLMERIHE QIKKGELALF YLQEQINHFE
     EKPTKEMKDK IVAEMDTIIA MIDGVRGVLD RLMQRKDLDI FEQYNLEMAK KSGDILERDL
     KKEEARVKKI EV
 
 
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