ID   CHI4_SOLTU              Reviewed;         302 AA.
AC   P52406;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Endochitinase 4;
DE            EC=3.2.1.14;
DE   Flags: Precursor; Fragment;
GN   Name=CHTB4;
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).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U02608; AAA17410.1; -; mRNA.
DR   PIR; S65021; S65021.
DR   AlphaFoldDB; P52406; -.
DR   SMR; P52406; -.
DR   STRING; 4113.PGSC0003DMT400069034; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   PRIDE; P52406; -.
DR   EnsemblPlants; RHC10H1G1776.2.1; RHC10H1G1776.2.1; RHC10H1G1776.2.
DR   Gramene; RHC10H1G1776.2.1; RHC10H1G1776.2.1; RHC10H1G1776.2.
DR   eggNOG; KOG4742; Eukaryota.
DR   InParanoid; P52406; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P52406; 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..>302
FT                   /note="Endochitinase 4"
FT                   /id="PRO_0000005326"
FT   DOMAIN          19..60
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   REGION          59..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        144
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        162..182
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   NON_TER         1
FT   NON_TER         302
SQ   SEQUENCE   302 AA;  32317 MW;  B1E2F0D643B08284 CRC64;
     EFTALSLLFS LLLLTASAEQ CGKQAGGARC AAGLCCSNFG WCGNTNDYCG PGKCQSQCPS
     GPSPKPPTPG PGPSGGDIGS VISNSMFDQM LKHRNDNACQ GKNNFYSYNA FINAARSFGG
     FGTTGDTTAR KREIAAFFAQ TSHETTGGWP TAPDGPYAWG YCFLREQGSP GDYCTPSGQW
     PCAPGRKYFG RGPIQISHNY NYGPCGRAIG VDLLNNPDLV ATDPVISFKS AIWFWMTPQS
     PKPSCHDVII GRWQPSAADR AANRLPGFGV ITNIINGGLE CGRGSDSRVQ DRIGFYRRYC
     GI