ID   CHIT3_VITVI             Reviewed;         301 AA.
AC   P51614;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Acidic endochitinase;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=CHIT3;
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Pinot;
RX   PubMed=9390436; DOI=10.1104/pp.115.3.1029;
RA   Busam G., Kassemeyer H.H., Matern U.;
RT   "Differential expression of chitinases in Vitis vinifera L. responding to
RT   systemic acquired resistance activators or fungal challenge.";
RL   Plant Physiol. 115:1029-1038(1997).
CC   -!- FUNCTION: Defense against chitin containing fungal pathogens.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
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DR   EMBL; Z68123; CAA92207.1; -; mRNA.
DR   RefSeq; NP_001268048.1; NM_001281119.1.
DR   AlphaFoldDB; P51614; -.
DR   SMR; P51614; -.
DR   STRING; 29760.VIT_16s0050g02220.t01; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   PRIDE; P51614; -.
DR   GeneID; 100233088; -.
DR   KEGG; vvi:100233088; -.
DR   eggNOG; KOG4701; Eukaryota.
DR   OrthoDB; 923272at2759; -.
DR   ExpressionAtlas; P51614; differential.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR   InterPro; IPR045321; Cts1-like.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Chitin degradation; Disulfide bond; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..301
FT                   /note="Acidic endochitinase"
FT                   /id="PRO_0000011921"
FT   DOMAIN          26..301
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        152
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   DISULFID        45..92
FT                   /evidence="ECO:0000250"
FT   DISULFID        75..82
FT                   /evidence="ECO:0000250"
FT   DISULFID        187..216
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   301 AA;  32351 MW;  54E3A59E8E2E007B CRC64;
     MARTPQSTPL LISLSVLALL QTSYAGGIAI YWGQNGNEGT LTQTCNTGKY SYVNIAFLNK
     FGNGQTPEIN LAGHCNPASN GCTSVSTGIR NCQNRGIKVM LSIGGGAGSY SLSSSNDAQN
     VANYLWNNFL GGQSSSRPLG DAVLDGIDFD IELGSTLHWD DLARALSRIE FQQERGRKVY
     LTAAPQCPFP DKVPGTALNT GLFDYVWVQF YNNPPCQYSS GNTNNLLNSW NRWTSSINST
     GSFMGLPASS AAAGRGFIPA NVLTSQILPV IKRSPKYGGV MLWSKYYDDQ SGYSSSIKSS
     V