CHIL_HEVBR
ID CHIL_HEVBR Reviewed; 295 AA.
AC Q8GUD7;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Probable inactive chitinase-like protein LaCIC {ECO:0000305};
DE AltName: Full=Leaf class I chitinase {ECO:0000305};
DE Short=LaCIC {ECO:0000303|PubMed:12653800};
DE AltName: Allergen=Hev b 11 {ECO:0000303|PubMed:12653800};
DE Flags: Fragment;
GN Name=LACIC {ECO:0000312|EMBL:CAD24068.1};
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], AND ALLERGEN.
RC STRAIN=cv. RRIM 600; TISSUE=Leaf;
RX PubMed=12653800; DOI=10.1034/j.1398-9995.2003.00058.x;
RA Rihs H.P., Dumont B., Raulf-Heimsoth M., Rozynek P., Lundberg M.,
RA Cremer R., Bruening T.;
RT "Molecular cloning, purification, and IgE-binding of a recombinant class I
RT chitinase from Hevea brasiliensis leaves (rHev b 11.0102).";
RL Allergy 58:246-251(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-43, AND DISULFIDE BONDS.
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: Probable inactive chitinase-like protein that does not
CC exhibit hydrolytic activity toward chitin (By similarity). May bind
CC chitin and be involved in plant defense against fungal pathogens (By
CC similarity). {ECO:0000250|UniProtKB:Q949H3}.
CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:12653800). Binds
CC to IgE from sera of patients allergic to rubber latex
CC (PubMed:12653800). {ECO:0000269|PubMed:12653800}.
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 117, which is
CC replaced by an Ala residue, explaining why it is inactive.
CC {ECO:0000305}.
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DR EMBL; AJ431363; CAD24068.1; -; mRNA.
DR PDB; 4MPI; X-ray; 1.60 A; A/B=1-43.
DR PDBsum; 4MPI; -.
DR AlphaFoldDB; Q8GUD7; -.
DR SMR; Q8GUD7; -.
DR Allergome; 384; Hev b 11.
DR Allergome; 978; Hev b 11.0102.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:InterPro.
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:0006952; P:defense response; IEA:UniProtKB-KW.
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; 1.
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 1: Evidence at protein level;
KW 3D-structure; Allergen; Chitin-binding; Disulfide bond; Plant defense.
FT CHAIN <1..295
FT /note="Probable inactive chitinase-like protein LaCIC"
FT /id="PRO_0000447216"
FT DOMAIN 1..41
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 3..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:25104038, ECO:0007744|PDB:4MPI"
FT DISULFID 12..24
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:25104038, ECO:0007744|PDB:4MPI"
FT DISULFID 17..31
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:25104038, ECO:0007744|PDB:4MPI"
FT DISULFID 35..39
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:25104038, ECO:0007744|PDB:4MPI"
FT DISULFID 73..135
FT /evidence="ECO:0000250|UniProtKB:Q949H3"
FT DISULFID 147..155
FT /evidence="ECO:0000250|UniProtKB:Q949H3"
FT DISULFID 254..286
FT /evidence="ECO:0000250|UniProtKB:Q949H3"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:CAD24068.1"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:4MPI"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:4MPI"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:4MPI"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:4MPI"
SQ SEQUENCE 295 AA; 31553 MW; 5C246D4C02E8B04E CRC64;
EQCGRQAGGA LCPGGLCCSQ YGWCANTPEY CGSGCQSQCD GGVGGEGGCV DLGSIISRST
FEEMLKHRNN AACPAKGFYT YDAFISAAKA FPAFGTTGDV DTCKREIAAF FGQTSHATTG
GWPTAPDGPY AWGYCHKEEL NQASSYCSPS PAYPCAPGKK YYGRGPIQLS WNYNYGQCGQ
ALGLDLLNNP DLVATDRVIS FKAAIWFWMT PQFPKPSCHD VITGQWSPTG HDISAGRAPG
YGVITNIING GLECGSGWDA RVEDRIGFYK RYCDMFGVGY GSNLDCYNQT PFGLG
