ID   CHI3_SOLTU              Reviewed;         318 AA.
AC   P52405; Q43179;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Endochitinase 3;
DE            EC=3.2.1.14;
DE   Flags: Precursor; Fragment;
GN   Name=CHTB3;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Datura; TISSUE=Leaf;
RX   PubMed=8111037; DOI=10.1007/bf00020173;
RA   Beerhues L., Kombrink E.;
RT   "Primary structure and expression of mRNAs encoding basic chitinase and
RT   1,3-beta-glucanase in potato.";
RL   Plant Mol. Biol. 24:353-367(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-318.
RX   PubMed=2519115; DOI=10.1007/bf00016142;
RA   Laflamme D., Roxby R.;
RT   "Isolation and nucleotide sequence of cDNA clones encoding potato chitinase
RT   genes.";
RL   Plant Mol. Biol. 13:249-250(1989).
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   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}. Note=Vacuolar and
CC       protoplast. {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Highest levels in younger leaves or stems segments
CC       and in older ones. Leaves and stems of intermediate age show a
CC       decreased expression. Appreciable amounts are also found in old root
CC       segments, and carpels.
CC   -!- INDUCTION: In response to infection, elicitor, ethylene, wounding.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily. {ECO:0000305}.
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DR   EMBL; U02607; AAA17409.1; -; mRNA.
DR   EMBL; X14133; CAA32351.1; -; mRNA.
DR   PIR; S43317; S43317.
DR   AlphaFoldDB; P52405; -.
DR   SMR; P52405; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   InParanoid; P52405; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P52405; baseline.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Disulfide bond; Glycosidase; Hydrolase; Plant defense;
KW   Polysaccharide degradation; Reference proteome; Signal; Vacuole.
FT   SIGNAL          <1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..311
FT                   /note="Endochitinase 3"
FT                   /id="PRO_0000005324"
FT   PROPEP          312..318
FT                   /note="Removed in mature form, vacuolar targeting"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000005325"
FT   DOMAIN          19..60
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   ACT_SITE        134
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   DISULFID        21..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        30..42
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        35..49
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        54..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        89..152
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        164..172
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        271..303
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   CONFLICT        18..27
FT                   /note="AEQCGSQAGG -> GSNVVHRPD (in Ref. 2; CAA32351)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   318 AA;  33799 MW;  BF587A8515534E71 CRC64;
     EFTIFSLLFS LLLLNASAEQ CGSQAGGALC APGLCCSKFG WCGNTNDYCG PGNCQSQCPG
     GPGPSGDLGG VISNSMFDQM LNHRNDNACQ GKNNFYSYNA FISAAGSFPG FGTTGDITAR
     KREIAAFLAQ TSHETTGGWP SAPDGPYAWG YCFLREQGSP GDYCTPSSQW PCAPGRKYFG
     RGPIQISHNY NYGPCGRAIG VDLLNNPDLV ATDSVISFKS AIWFWMTPQS PKPSCHDVIT
     GRWQPSGADQ AANRVPGFGV ITNIINGGLE CGHGSDSRVQ DRIGFYRRYC GILGVSPGDN
     LDCGNQRSFG NGLLVDTV