CHIT_PERAE
ID CHIT_PERAE Reviewed; 326 AA.
AC P93680;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 2.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Endochitinase {ECO:0000303|PubMed:10231327, ECO:0000303|PubMed:9774427, ECO:0000312|EMBL:CAB01591.1};
DE EC=3.2.1.14 {ECO:0000269|PubMed:9679856, ECO:0000269|PubMed:9774427, ECO:0000312|EMBL:CAB01591.1};
DE AltName: Full=Allergen Pers a 1 {ECO:0000303|PubMed:18205857, ECO:0000303|PubMed:21284746, ECO:0000303|PubMed:23019098};
DE AltName: Full=Allergen Prs a 1 {ECO:0000303|PubMed:10482846, ECO:0000303|PubMed:10887324, ECO:0000303|PubMed:14610495, ECO:0000303|PubMed:16433216, ECO:0000303|PubMed:9774427};
DE AltName: Full=Chitin-binding avocado protein {ECO:0000303|PubMed:10231327};
DE Short=CBAP {ECO:0000303|PubMed:10231327};
DE AltName: Full=Class I chitinase {ECO:0000303|PubMed:10231327, ECO:0000303|PubMed:10482846, ECO:0000303|PubMed:18205857, ECO:0000303|PubMed:9679856};
DE AltName: Full=PaI1 {ECO:0000303|PubMed:9679856};
DE AltName: Allergen=Pers a 1.0101 {ECO:0000305};
DE Flags: Precursor;
GN Name=chi1 {ECO:0000312|EMBL:CAB01591.1};
OS Persea americana (Avocado).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Persea.
OX NCBI_TaxID=3435 {ECO:0000312|EMBL:CAB01591.1};
RN [1] {ECO:0000312|EMBL:CAB01591.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-51; 188-203 AND 226-238,
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND ALLERGEN.
RC STRAIN=cv. Hass {ECO:0000303|PubMed:9774427};
RC TISSUE=Mesocarp {ECO:0000303|PubMed:9774427, ECO:0000312|EMBL:CAB01591.1};
RX PubMed=9774427; DOI=10.1074/jbc.273.43.28091;
RA Sowka S., Hsieh L.S., Krebitz M., Akasawa A., Martin B.M., Starrett D.,
RA Peterbauer C.K., Scheiner O., Breiteneder H.;
RT "Identification and cloning of prs a 1, a 32-kDa endochitinase and major
RT allergen of avocado, and its expression in the yeast Pichia pastoris.";
RL J. Biol. Chem. 273:28091-28097(1998).
RN [2]
RP PROTEIN SEQUENCE OF 26-52, CATALYTIC ACTIVITY, CHITIN-BINDING, TISSUE
RP SPECIFICITY, AND ALLERGEN.
RC TISSUE=Fruit flesh {ECO:0000303|PubMed:9679856};
RX PubMed=9679856; DOI=10.1016/s0091-6749(98)70063-6;
RA Diaz-Perales A., Collada C., Blanco C., Sanchez-Monge R., Carrillo T.,
RA Aragoncillo C., Salcedo G.;
RT "Class I chitinases with hevein-like domain, but not class II enzymes, are
RT relevant chestnut and avocado allergens.";
RL J. Allergy Clin. Immunol. 102:127-133(1998).
RN [3]
RP PROTEIN SEQUENCE OF 26-40, CHITIN-BINDING, AND ALLERGEN.
RC TISSUE=Fruit {ECO:0000303|PubMed:10231327};
RX PubMed=10231327; DOI=10.1046/j.1365-2222.1999.00502.x;
RA Posch A., Wheeler C.H., Chen Z., Flagge A., Dunn M.J., Papenfuss F.,
RA Raulf-Heimsoth M., Baur X.;
RT "Class I endochitinase containing a hevein domain is the causative allergen
RT in latex-associated avocado allergy.";
RL Clin. Exp. Allergy 29:667-672(1999).
RN [4]
RP PROTEIN SEQUENCE OF 26-30; 62-65; 220-223; 270-276; 299-303 AND 307-313,
RP TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, AND ALLERGEN.
RC TISSUE=Fruit {ECO:0000303|PubMed:14610495};
RX PubMed=14610495; DOI=10.1016/j.jaci.2003.07.006;
RA Diaz-Perales A., Blanco C., Sanchez-Monge R., Varela J., Carrillo T.,
RA Salcedo G.;
RT "Analysis of avocado allergen (Prs a 1) IgE-binding peptides generated by
RT simulated gastric fluid digestion.";
RL J. Allergy Clin. Immunol. 112:1002-1007(2003).
RN [5]
RP ALLERGEN.
RX PubMed=10482846; DOI=10.1016/s0091-6749(99)70342-8;
RA Diaz-Perales A., Collada C., Blanco C., Sanchez-Monge R., Carrillo T.,
RA Aragoncillo C., Salcedo G.;
RT "Cross-reactions in the latex-fruit syndrome: A relevant role of chitinases
RT but not of complex asparagine-linked glycans.";
RL J. Allergy Clin. Immunol. 104:681-687(1999).
RN [6]
RP ALLERGEN.
RX PubMed=10887324; DOI=10.1067/mai.2000.107599;
RA Sanchez-Monge R., Blanco C., Perales A.D., Collada C., Carrillo T.,
RA Aragoncillo C., Salcedo G.;
RT "Class I chitinases, the panallergens responsible for the latex-fruit
RT syndrome, are induced by ethylene treatment and inactivated by heating.";
RL J. Allergy Clin. Immunol. 106:190-195(2000).
RN [7]
RP ALLERGEN.
RX PubMed=16433216;
RA Gamboa P.M., Sanchez-Monge R., Diaz-Perales A., Salcedo G., Ansotegui J.,
RA Sanz M.L.;
RT "Latex-vegetable syndrome due to custard apple and aubergine: new
RT variations of the hevein symphony.";
RL J. Investig. Allergol. Clin. Immunol. 15:308-311(2005).
RN [8]
RP ALLERGEN.
RX PubMed=18205857; DOI=10.1111/j.1365-2222.2007.02927.x;
RA Palacin A., Rodriguez J., Blanco C., Lopez-Torrejon G., Sanchez-Monge R.,
RA Varela J., Jimenez M.A., Cumplido J., Carrillo T., Crespo J.F., Salcedo G.;
RT "Immunoglobulin E recognition patterns to purified Kiwifruit (Actinidinia
RT deliciosa) allergens in patients sensitized to Kiwi with different clinical
RT symptoms.";
RL Clin. Exp. Allergy 38:1220-1228(2008).
RN [9]
RP ALLERGEN.
RX PubMed=21284746; DOI=10.1111/j.1399-3038.2010.01125.x;
RA Palacin A., Quirce S., Sanchez-Monge R., Bobolea I., Diaz-Perales A.,
RA Martin-Munoz F., Pascual C., Salcedo G.;
RT "Sensitization profiles to purified plant food allergens among pediatric
RT patients with allergy to banana.";
RL Pediatr. Allergy Immunol. 22:186-195(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=23019098; DOI=10.1002/elps.201200254;
RA Esteve C., D'Amato A., Marina M.L., Garcia M.C., Righetti P.G.;
RT "Identification of avocado (Persea americana) pulp proteins by nano-LC-
RT MS/MS via combinatorial peptide ligand libraries.";
RL Electrophoresis 33:2799-2805(2012).
CC -!- FUNCTION: Defense against chitin-containing fungal pathogens. Has in
CC vitro antifungal activity against F.oxysporum inhibiting its growth and
CC the branching of its hyphae. Has endochitinase activity, but no
CC exochitinase or lysozyme activities. {ECO:0000269|PubMed:9774427}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC Evidence={ECO:0000269|PubMed:9679856, ECO:0000269|PubMed:9774427};
CC -!- TISSUE SPECIFICITY: Expressed in the pulp of the fruit (at protein
CC level) (PubMed:9679856, PubMed:14610495, PubMed:23019098). Expressed in
CC mesocarp (at protein level) (PubMed:9774427).
CC {ECO:0000269|PubMed:14610495, ECO:0000269|PubMed:23019098,
CC ECO:0000269|PubMed:9679856, ECO:0000269|PubMed:9774427}.
CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:9774427,
CC PubMed:9679856, PubMed:10231327, PubMed:14610495, PubMed:10482846,
CC PubMed:10887324, PubMed:16433216, PubMed:18205857, PubMed:21284746).
CC Involved (at least via the N-terminal chitin-binding hevein-like
CC domain) in cross-reactions with natural rubber latex (latex-fruit
CC allergy syndrome) (PubMed:9774427, PubMed:9679856, PubMed:10231327,
CC PubMed:14610495, PubMed:10482846, PubMed:10887324, PubMed:16433216).
CC Binds to IgE of patients allergic to avocado, chestnut and/or banana
CC (PubMed:9679856, PubMed:10482846, PubMed:16433216, PubMed:21284746).
CC Binds to IgE in 75% of the 20 patients tested allergic to latex
CC (PubMed:9774427). Binds to IgE in 80% of the 15 patients tested
CC allergic to avocado and latex (PubMed:10231327). Binds to IgE in 53% of
CC the 92 and 38% of the 26 kiwifruit-allergic patients tested by ELISA
CC and IgE immunodetection assays, respectively. Only 12% of the 25
CC kiwifruit-allergic patients tested are found positive by skin prick
CC test (PubMed:18205857). Binds to IgE in 29% of the 51 pediatric
CC patients tested allergic to banana (PubMed:21284746). IgE-binding is
CC not abolished by digestion with artificial gastric juice or simulated
CC gastric fluid (PubMed:10231327, PubMed:14610495). In vitro IgE-binding
CC and in vivo allergenicity (skin prick test) is abolished by heating
CC (PubMed:10887324). Induces degranulation of human basohphils and
CC histamine release (PubMed:16433216). {ECO:0000269|PubMed:10231327,
CC ECO:0000269|PubMed:10482846, ECO:0000269|PubMed:10887324,
CC ECO:0000269|PubMed:14610495, ECO:0000269|PubMed:16433216,
CC ECO:0000269|PubMed:18205857, ECO:0000269|PubMed:21284746,
CC ECO:0000269|PubMed:9679856, ECO:0000269|PubMed:9774427}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I subfamily. {ECO:0000305}.
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DR EMBL; Z78202; CAB01591.1; -; mRNA.
DR AlphaFoldDB; P93680; -.
DR SMR; P93680; -.
DR Allergome; 3414; Pers a 1.0101.
DR Allergome; 546; Pers a 1.
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:0004568; F:chitinase activity; IDA:UniProtKB.
DR GO; GO:0008843; F:endochitinase activity; IDA:UniProtKB.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.60.10; -; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
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; PS00026; CHIT_BIND_I_1; 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 Allergen; Antimicrobial; Carbohydrate metabolism; Chitin degradation;
KW Chitin-binding; Direct protein sequencing; Disulfide bond; Glycosidase;
KW Hydrolase; Pathogenesis-related protein; Plant defense;
KW Polysaccharide degradation; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255, ECO:0000269|PubMed:10231327,
FT ECO:0000269|PubMed:14610495, ECO:0000269|PubMed:9679856,
FT ECO:0000269|PubMed:9774427"
FT CHAIN 26..326
FT /note="Endochitinase"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:10231327,
FT ECO:0000305|PubMed:14610495, ECO:0000305|PubMed:9679856,
FT ECO:0000305|PubMed:9774427"
FT /id="PRO_5004161896"
FT DOMAIN 26..66
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000305"
FT ACT_SITE 140
FT /note="Proton donor"
FT /evidence="ECO:0000255|PIRSR:PIRSR001060-1"
FT DISULFID 28..43
FT /evidence="ECO:0000255|PIRSR:PIRSR001060-2,
FT ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 37..49
FT /evidence="ECO:0000255|PIRSR:PIRSR001060-2,
FT ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 42..56
FT /evidence="ECO:0000255|PIRSR:PIRSR001060-2,
FT ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 60..64
FT /evidence="ECO:0000255|PIRSR:PIRSR001060-2,
FT ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 96..158
FT /evidence="ECO:0000255|PIRSR:PIRSR001060-2"
FT DISULFID 170..178
FT /evidence="ECO:0000255|PIRSR:PIRSR001060-2"
FT DISULFID 277..309
FT /evidence="ECO:0000255|PIRSR:PIRSR001060-2"
FT CONFLICT 203
FT /note="R -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 34586 MW; 643B20589E062E61 CRC64;
MVYCTASLPL LLLLLVGLLA GEAFAEQCGR QAGGALCPGG LCCSQFGWCG STSDYCGPTC
QSQCGGVTPS PGGGVASLIS QSVFNQMLKH RNDAACQAKG FYTYNAFIAA ANSFNGFASV
GDTATRKREI AAFLAQTSHE TTGGWATAPD GPYAWGYCFL KEQGNPPDYC VPTAQWPCAP
GKKYYGRGPI QISYNYNYGP AGRAIGYDLI NNPDAVATDP VISFKTALWF WMTPQSPKPS
CHNVITGRWT PSAADRAAGR LPGYGVITNI INGGIECGKG FNDKVADRIG FYKRYCDLLG
VSYGSNLDCY NQRSFGVSTN PLAASS
