CHL18_DERPT
ID CHL18_DERPT Reviewed; 462 AA.
AC Q4JK71;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Chitinase-like mite allergen Der p 18.0101 {ECO:0000305};
DE AltName: Full=Allergen Der p 18 {ECO:0000303|PubMed:16776685, ECO:0000303|PubMed:23075813, ECO:0000303|PubMed:27548813};
DE AltName: Full=Chitinase-like house dust mite allergen Der p 18 {ECO:0000303|PubMed:23075813, ECO:0000303|PubMed:27548813};
DE AltName: Full=Group 18 allergen protein {ECO:0000312|EMBL:AAY84563.1};
DE AltName: Allergen=Der p 18.0101 {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:AAY84563.1};
RN [1] {ECO:0000312|EMBL:AAY84563.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND ALLERGEN.
RX PubMed=16776685; DOI=10.1111/j.1365-2222.2006.02497.x;
RA O'Neil S.E., Heinrich T.K., Hales B.J., Hazell L.A., Holt D.C., Fischer K.,
RA Thomas W.R.;
RT "The chitinase allergens Der p 15 and Der p 18 from Dermatophagoides
RT pteronyssinus.";
RL Clin. Exp. Allergy 36:831-839(2006).
RN [2]
RP ALLERGEN, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=23075813; DOI=10.1159/000339760;
RA Hales B.J., Elliot C.E., Chai L.Y., Pearce L.J., Tipayanon T., Hazell L.,
RA Stone S., Piboonpocanun S., Thomas W.R., Smith W.A.;
RT "Quantitation of IgE binding to the chitinase and chitinase-like house dust
RT mite allergens Der p 15 and Der p 18 compared to the major and mid-range
RT allergens.";
RL Int. Arch. Allergy Immunol. 160:233-240(2013).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ALLERGEN, 3D-STRUCTURE
RP MODELING, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=27548813; DOI=10.1371/journal.pone.0160641;
RA Resch Y., Blatt K., Malkus U., Fercher C., Swoboda I., Focke-Tejkl M.,
RA Chen K.W., Seiberler S., Mittermann I., Lupinek C., Rodriguez-Dominguez A.,
RA Zieglmayer P., Zieglmayer R., Keller W., Krzyzanek V., Valent P.,
RA Valenta R., Vrtala S.;
RT "Molecular, Structural and Immunological Characterization of Der p 18, a
RT Chitinase-Like House Dust Mite Allergen.";
RL PLoS ONE 11:e0160641-e0160641(2016).
CC -!- FUNCTION: Probably a non-catalytic chitinase-like protein, which binds
CC to insoluble chitin and enhances the activity of the catalytic
CC chitinases (PubMed:16776685). Has weak chitin-binding activity
CC (PubMed:27548813). {ECO:0000269|PubMed:27548813,
CC ECO:0000305|PubMed:16776685}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27548813}.
CC -!- TISSUE SPECIFICITY: Expressed in the peritrophic matrix of the midgut,
CC and only very weakly in fecal pellets. {ECO:0000269|PubMed:27548813}.
CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:16776685,
CC PubMed:23075813, PubMed:27548813). Recombinant protein binds to IgE in
CC 63% of the 27 patients tested allergic to house dust mite (HDM)
CC (PubMed:16776685). The recombinant protein has 38%, 16% and 3%
CC prevalences of IgE-binding with titers equal or above 0.1 ng/ml, 0.84
CC ng/ml and 10 ng/ml, respectively, of the 37 adult patients tested
CC living in Perth, Australia allergic to European HDM (PubMed:23075813).
CC Recombinant protein binds to IgE in 10% of the 91 adult Austrian
CC patients tested allergic to European HDM. Binds to IgE in 15% of both
CC the 20 and 13 patients tested with respiratory (asthma and allergic
CC rhinitis) or skin (atopic dermatitis) manifestations, respectively.
CC Induces activation of human basophils (PubMed:27548813).
CC {ECO:0000269|PubMed:16776685, ECO:0000269|PubMed:23075813,
CC ECO:0000269|PubMed:27548813}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the glycosyl hydrolase 18 family, Ser-
CC 148 is present instead of the conserved Glu which is an active site
CC residue. Therefore this protein may lack chitinase activity.
CC {ECO:0000305|PubMed:16776685, ECO:0000305|PubMed:27548813}.
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DR EMBL; DQ078739; AAY84563.1; -; mRNA.
DR AlphaFoldDB; Q4JK71; -.
DR SMR; Q4JK71; -.
DR Allergome; 10802; Der p 18.0101.
DR Allergome; 2699; Der p 18.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR Proteomes; UP000515146; Unplaced.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.10.50.10; -; 1.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF01607; CBM_14; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 1.
DR SUPFAM; SSF57625; SSF57625; 1.
DR PROSITE; PS50940; CHIT_BIND_II; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW Allergen; Chitin-binding; Disulfide bond; Glycoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..462
FT /note="Chitinase-like mite allergen Der p 18.0101"
FT /evidence="ECO:0000255"
FT /id="PRO_5004239394"
FT DOMAIN 29..378
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DOMAIN 404..462
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 33..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 439..453
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
SQ SEQUENCE 462 AA; 52012 MW; 8358D4CC2577B3F2 CRC64;
MTRLSFTVLI FLAAYFGSNI RPNVATLDPK TVCYYESWVH WRQGDGKMDP EDIDTSLCSH
IVYSYFGIDA SSHEIKLLDQ YLMITLHDME HFTKHKGNAK AMIAVGGASM SDQFSKTAAV
EHYRETFVVS TIDLMTKYGF DGVMIDWSGM QAKDSDNFVK LLDKFDEKFA QTSFVMGVTL
PATIASYDNY NIPAISNYVD FMNVLTLDYD GPWAYTVGHA SALPEQLKTL EAYNKRGAPR
HKMVMAVPFF ARTWILEKMD KQDVGDKASG PGPKGQFTQT PGFLSYNELC VQIQAETNAF
SITRDHDNTA IYAVYVHDNH AEWISFEDRH TLGDKARNIT EQGYGGMSVY TLSNEDVHGV
CGDKNPLLHA INSNYFRGIV TEPTVVTVTP VTHTTEHVTD IPGVFHCHQE GFFRDKTYCA
KYYECKKGDF GLEQTVHHCP NHSQAFDEVS RTCVDHAKIP GC
