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   27-MAR-2024, entry version 101.
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,
RC   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   CDD; cd00325; chitinase_GH19; 1.
DR   CDD; cd06921; ChtBD1_GH19_hevein; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.30.20.10; Endochitinase, domain 2; 1.
DR   Gene3D; 3.30.60.10; Endochitinase-like; 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   PANTHER; PTHR22595:SF79; BASIC ENDOCHITINASE B; 1.
DR   PANTHER; PTHR22595; CHITINASE-RELATED; 1.
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; Lysozyme-like; 1.
DR   SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 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
//