CHL18_DERFA
ID CHL18_DERFA Reviewed; 462 AA.
AC Q86R84;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Chitinase-like mite allergen Der f 18.0101 {ECO:0000305};
DE AltName: Full=60 kDa allergen {ECO:0000303|PubMed:12847483};
DE AltName: Full=60 kDa chitinase homolog {ECO:0000303|PubMed:12847483};
DE AltName: Full=Allergen Der f 18 {ECO:0000303|PubMed:12847483};
DE AltName: Allergen=Der f 18.0101 {ECO:0000305};
DE Flags: Precursor;
OS Dermatophagoides farinae (American house dust mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC Pyroglyphidae; Dermatophagoidinae; Dermatophagoides.
OX NCBI_TaxID=6954 {ECO:0000312|EMBL:AAM19082.1};
RN [1] {ECO:0000312|EMBL:AAM19082.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-48; 54-73; 88-101;
RP 112-124; 146-153; 156-161; 175-205; 208-226; 266-274; 281-298 AND 356-393,
RP TISSUE SPECIFICITY, AND ALLERGEN.
RX PubMed=12847483; DOI=10.1067/mai.2003.1602;
RA Weber E., Hunter S., Stedman K., Dreitz S., Olivry T., Hillier A.,
RA McCall C.;
RT "Identification, characterization, and cloning of a complementary DNA
RT encoding a 60-kd house dust mite allergen (Der f 18) for human beings and
RT dogs.";
RL J. Allergy Clin. Immunol. 112:79-86(2003).
CC -!- FUNCTION: Probably a non-catalytic chitinase-like protein, which binds
CC to insoluble chitin and enhances the activity of the catalytic
CC chitinases. Has weak chitin-binding activity.
CC {ECO:0000250|UniProtKB:Q4JK71}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q4JK71}.
CC -!- TISSUE SPECIFICITY: Expressed in the upper digestive tract. Staining is
CC observed in the ventriculus, and in very rare individuals, also in the
CC intestine or esophagus. No expression in fecal pellets neither inside
CC the rectum nor defecated outside of the body.
CC {ECO:0000269|PubMed:12847483}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Natural protein binds
CC to IgE in 54% of the 24 patients from the Western USA tested allergic
CC to American house dust mite (HDM). Causes an allergic reaction in dog.
CC Natural protein binds to IgE in 57% of the 21 dogs with atopic
CC dermatitis tested allergic to American HDM. In the intradermal tests,
CC the natural protein produces positive reactions in 37% of the 19 dogs
CC with atopic dermatitis tested allergic to American HDM. Binds to IgE in
CC 77% of the 35 dogs with putative atopic dermatitis tested allergic to
CC American HDM. {ECO:0000269|PubMed:12847483}.
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:0000250|UniProtKB:Q4JK71}.
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DR EMBL; AY093656; AAM19082.1; -; mRNA.
DR AlphaFoldDB; Q86R84; -.
DR SMR; Q86R84; -.
DR Allergome; 301; Der f 18.
DR Allergome; 3254; Der f 18.0101.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0008061; F:chitin binding; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.10.50.10; -; 1.
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; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW Allergen; Chitin-binding; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:12847483"
FT CHAIN 26..462
FT /note="Chitinase-like mite allergen Der f 18.0101"
FT /evidence="ECO:0000305|PubMed:12847483"
FT /id="PRO_5004300467"
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 DISULFID 33..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 439..453
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT CONFLICT 190
FT /note="Y -> YY (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 52103 MW; 7F9F06E2FE016F79 CRC64;
MTRFSLTVLA VLAACFGSNI RPNVATLEPK TVCYYESWVH WRQGEGKMDP EDIDTSLCTH
IVYSYFGIDA ATHEIKLLDE YLMKDLHDME HFTQHKGNAK AMIAVGGSTM SDQFSKTAAV
EHYRETFVVS TVDLMTRYGF DGVMIDWSGM QAKDSDNFIK LLDKFDEKFA HTSFVMGVTL
PATIASYDNY NIPAISNYVD FMNVLSLDYT GSWAHTVGHA SPFPEQLKTL EAYHKRGAPR
HKMVMAVPFY ARTWILEKMN KQDIGDKASG PGPRGQFTQT DGFLSYNELC VQIQAETNAF
TITRDHDNTA IYAVYVHSNH AEWISFEDRH TLGEKAKNIT QQGYAGMSVY TLSNEDVHGV
CGDKNPLLHA IQSNYYHGVV TEPTVVTLPP VTHTTEHVTD IPGVFHCHEE GFFRDKTYCA
TYYECKKGDF GLEKTVHHCA NHLQAFDEVS RTCIDHTKIP GC
