CHI1_HEVBR
ID CHI1_HEVBR Reviewed; 314 AA.
AC Q949H3; W0IVX0;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 2.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Inactive chitinase-like protein 1 {ECO:0000305};
DE Short=HbCLP1 {ECO:0000303|PubMed:25104038};
DE AltName: Allergen=Hev b 11 {ECO:0000303|PubMed:11940078};
DE Flags: Precursor;
GN Name=CHI-L1 {ECO:0000312|EMBL:AHF88836.1};
GN Synonyms=RQ30 {ECO:0000312|EMBL:CAC42881.1};
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 [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS)
RP OF 73-314, DISULFIDE BONDS, AND FUNCTION.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-314, AND ALLERGEN.
RC STRAIN=cv. RRIM 600;
RX PubMed=11940078; DOI=10.1046/j.1365-2222.2002.01312.x;
RA O'Riordain G., Radauer C., Hoffmann-Sommergruber K., Adhami F.,
RA Peterbauer C.K., Blanco C., Godnic-Cvar J., Scheiner O., Ebner C.,
RA Breitender H.;
RT "Cloning and molecular characterization of the Hevea brasiliensis allergen
RT Hev b 11, a class I chitinase.";
RL Clin. Exp. Allergy 32:455-462(2002).
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). Inhibits the
CC growth of Fusarium oxysporum on plate assays (PubMed:11940078).
CC Probably involved in defense against fungal pathogens through a
CC mechanism that only involves carbohydrate binding (PubMed:25104038).
CC {ECO:0000269|PubMed:11940078, ECO:0000269|PubMed:25104038}.
CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:11940078). Binds
CC to IgE from sera of patients allergic to rubber latex
CC (PubMed:11940078). {ECO:0000269|PubMed:11940078}.
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 136, which is
CC replaced by an Ala residue, explaining why it is inactive.
CC {ECO:0000269|PubMed:25104038}.
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DR EMBL; KF648872; AHF88836.1; -; Genomic_DNA.
DR EMBL; AJ238579; CAC42881.1; -; mRNA.
DR PDB; 4MST; X-ray; 1.93 A; A/B=73-314.
DR PDBsum; 4MST; -.
DR AlphaFoldDB; Q949H3; -.
DR SMR; Q949H3; -.
DR Allergome; 384; Hev b 11.
DR Allergome; 977; Hev b 11.0101.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
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; 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;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..314
FT /note="Inactive chitinase-like protein 1"
FT /id="PRO_0000447214"
FT DOMAIN 20..60
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 22..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 31..43
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 36..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 54..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 92..154
FT /evidence="ECO:0000269|PubMed:25104038,
FT ECO:0007744|PDB:4MST"
FT DISULFID 166..174
FT /evidence="ECO:0000269|PubMed:25104038,
FT ECO:0007744|PDB:4MST"
FT DISULFID 273..305
FT /evidence="ECO:0000269|PubMed:25104038,
FT ECO:0007744|PDB:4MST"
FT CONFLICT 24
FT /note="W -> R (in Ref. 2; CAC42881)"
FT CONFLICT 122
FT /note="R -> C (in Ref. 2; CAC42881)"
FT CONFLICT 139
FT /note="Missing (in Ref. 1; AHF88836)"
FT /evidence="ECO:0000305"
FT HELIX 77..83
FT /evidence="ECO:0007829|PDB:4MST"
FT TURN 84..88
FT /evidence="ECO:0007829|PDB:4MST"
FT TURN 93..97
FT /evidence="ECO:0007829|PDB:4MST"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:4MST"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:4MST"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:4MST"
FT HELIX 119..136
FT /evidence="ECO:0007829|PDB:4MST"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:4MST"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:4MST"
FT TURN 184..187
FT /evidence="ECO:0007829|PDB:4MST"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:4MST"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:4MST"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:4MST"
FT HELIX 216..228
FT /evidence="ECO:0007829|PDB:4MST"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:4MST"
FT HELIX 249..253
FT /evidence="ECO:0007829|PDB:4MST"
FT HELIX 260..272
FT /evidence="ECO:0007829|PDB:4MST"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:4MST"
FT HELIX 279..295
FT /evidence="ECO:0007829|PDB:4MST"
SQ SEQUENCE 314 AA; 33786 MW; 1BA40AFA0629AF67 CRC64;
MKEIVRALEG YGPPKDKAAE QCGWQAGGAL CPGGLCCSQY GWCANTPEYC GSGCQSQCDG
GGGGEDGGID LGSIISRSTF EEMLKHRNDA ACPAKGFYTY DAFISAAKAF PAFGTTGDVD
TRKREIAAFF GQTSHATTGG WPTAPDGPYA WGYCYKEELN QASSYCSPSP AYPCAPGKKY
YGRGPIQLSW NYNYGQCGQA LGLDLLNNPD LVATDRVISF KAAIWFWMTP QFPKPSCHDV
ITGQWSPTGH DISAGRAPGY GVITNIINGG LECGRGWDAR VEDRIGFYKR YCDMFAVGYG
SNLDCYNQTP FGLG
