ID   CHI2_HEVBR              Reviewed;         342 AA.
AC   W0IWL0;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Inactive chitinase-like protein 2 {ECO:0000305};
DE            Short=HbCLP2 {ECO:0000303|PubMed:25104038};
DE   AltName: Allergen=Hev b 11 {ECO:0000250|UniProtKB:Q949H3};
DE   Flags: Precursor;
GN   Name=CHI-L2 {ECO:0000303|PubMed:25104038};
OS   Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC   Hevea.
OX   NCBI_TaxID=3981;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. RRIM 600;
RX   PubMed=25104038; DOI=10.1111/febs.12962;
RA   Martinez-Caballero S., Cano-Sanchez P., Mares-Mejia I., Diaz-Sanchez A.G.,
RA   Macias-Rubalcava M.L., Hermoso J.A., Rodriguez-Romero A.;
RT   "Comparative study of two GH19 chitinase-like proteins from Hevea
RT   brasiliensis, one exhibiting a novel carbohydrate-binding domain.";
RL   FEBS J. 281:4535-4554(2014).
CC   -!- FUNCTION: Inactive chitinase-like protein that does not exhibit
CC       hydrolytic activity toward chitin (PubMed:25104038). Binds strongly to
CC       chitin and possesses antifungal activity toward the fungal pathogen
CC       Altenaria alternata in plate assays (PubMed:25104038). Probably
CC       involved in defense against fungal pathogens through a mechanism that
CC       only involves carbohydrate binding (PubMed:25104038).
CC       {ECO:0000269|PubMed:25104038}.
CC   -!- ALLERGEN: May cause an allergic reaction in human (By similarity).
CC       Binds to IgE from sera of patients allergic to rubber latex (By
CC       similarity). {ECO:0000250|UniProtKB:Q949H3}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily. {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved Glu active site in position 166, which is
CC       replaced by an Ala residue, explaining why it is inactive.
CC       {ECO:0000269|PubMed:25104038}.
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DR   EMBL; KF648873; AHF88837.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0IWL0; -.
DR   SMR; W0IWL0; -.
DR   GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:InterPro.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR   Gene3D; 3.30.60.10; -; 1.
DR   InterPro; IPR001002; Chitin-bd_1.
DR   InterPro; IPR036861; Endochitinase-like_sf.
DR   InterPro; IPR016283; Glyco_hydro_19.
DR   InterPro; IPR000726; Glyco_hydro_19_cat.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   Pfam; PF00187; Chitin_bind_1; 1.
DR   Pfam; PF00182; Glyco_hydro_19; 1.
DR   PIRSF; PIRSF001060; Endochitinase; 1.
DR   PRINTS; PR00451; CHITINBINDNG.
DR   SMART; SM00270; ChtBD1; 2.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   SUPFAM; SSF57016; SSF57016; 1.
DR   PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR   PROSITE; PS00773; CHITINASE_19_1; 1.
DR   PROSITE; PS00774; CHITINASE_19_2; 1.
PE   2: Evidence at transcript level;
KW   Allergen; Chitin-binding; Disulfide bond; Plant defense; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..342
FT                   /note="Inactive chitinase-like protein 2"
FT                   /id="PRO_0000447215"
FT   DOMAIN          20..60
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        22..37
FT                   /evidence="ECO:0000250|UniProtKB:Q8GUD7,
FT                   ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        31..43
FT                   /evidence="ECO:0000250|UniProtKB:Q8GUD7,
FT                   ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        36..80
FT                   /evidence="ECO:0000250|UniProtKB:Q8GUD7,
FT                   ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        84..88
FT                   /evidence="ECO:0000250|UniProtKB:Q8GUD7,
FT                   ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        122..184
FT                   /evidence="ECO:0000250|UniProtKB:Q949H3"
FT   DISULFID        196..204
FT                   /evidence="ECO:0000250|UniProtKB:Q949H3"
FT   DISULFID        301..333
FT                   /evidence="ECO:0000250|UniProtKB:Q949H3"
SQ   SEQUENCE   342 AA;  36236 MW;  1510A7944FAB80CB CRC64;
     MKEIVRALEG YGPPKDKAAE QCGWQAGGAL CPGGLCCSQY GWCANTPEYC GSGCQSQCDG
     GVGGEGGCVD LGCANTPEYC GSGCQSQCDG GVGGEGGCVD LGSIISRSTF EEMLKHRNNA
     ACPAKGFYTY DAFISAAKAF PAFGTTGDVD TCKREIAAFF GQTSHATTGG WPTAPDGPYA
     WGYCHKEELN QASSYCSPSP AYPCAPGKKY YGRGPIQLSW NYGQCGQALG LDLLNNPDLV
     ATDRVISFKA AIWFWMTPQF PKPSCHDVIT GQWSPTGHDI SAGRAPGYGV ITNIINGGLE
     CGRGWDARVE DRIGFYKRYC DMFGVGYGSN LDCYNQTPFG LG