ID   CHI6_POPTR              Reviewed;         340 AA.
AC   P16579;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Acidic endochitinase WIN6;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=WIN6;
OS   Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS   trichocarpa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=3694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=H11-11; TISSUE=Leaf;
RX   PubMed=8075397; DOI=10.1007/bf00028875;
RA   Clarke H.R., Davis J.M., Wilbert S.M., Bradshaw H.D. Jr., Gordon M.P.;
RT   "Wound-induced and developmental activation of a poplar tree chitinase gene
RT   promoter in transgenic tobacco.";
RL   Plant Mol. Biol. 25:799-815(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 127-340.
RX   PubMed=2813366; DOI=10.1073/pnas.86.20.7895;
RA   Parsons T.J., Bradshaw H.D. Jr., Gordon M.P.;
RT   "Systemic accumulation of specific mRNAs in response to wounding in poplar
RT   trees.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:7895-7899(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   -!- INDUCTION: By wounding.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily. {ECO:0000305}.
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DR   EMBL; U01661; AAA57278.1; -; Genomic_DNA.
DR   EMBL; U01660; AAA57277.1; -; mRNA.
DR   EMBL; M25336; AAA96701.1; -; mRNA.
DR   PIR; B33985; B33985.
DR   AlphaFoldDB; P16579; -.
DR   SMR; P16579; -.
DR   STRING; 3694.POPTR_0009s14390.1; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   eggNOG; KOG4742; Eukaryota.
DR   ExpressionAtlas; P16579; differential.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
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:0006952; P:defense response; IEA:UniProtKB-KW.
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; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..340
FT                   /note="Acidic endochitinase WIN6"
FT                   /id="PRO_0000005316"
FT   DOMAIN          23..63
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   REGION          64..85
FT                   /note="Spacer"
FT   REGION          86..340
FT                   /note="Chitinase"
FT   ACT_SITE        154
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   DISULFID        25..40
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        34..46
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        39..53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        57..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        110..172
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        183..191
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        290..323
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   340 AA;  36410 MW;  C4E96473BEAA55C5 CRC64;
     MSVWALFAFF SLFLSLSVRG SAEQCGRQAG DALCPGGLCC SSYGWCGTTV DYCGIGCQSQ
     CDGGGGGDGG DDGCDGGDDG GGDGDDGYLS DIIPKSKFDA LLKFRNDARC PAAGFYTYNA
     FISAAKEFPD FGNTGDDLMR KREIAAFLGQ TSHETTGGWP DAPCGPYAWG YCYLKEINCQ
     PYCDPSSNYQ CVAGKQYCGR GPIQLSWNYN YGLCGDDLKL PLLQEPELVE TDPVISFKTA
     IWFWMKPQSP KPSCHAVITG NWTPSAADLE AGRVPGYGVI TNIINGGIEC GQGGPNAANE
     DRIGFYKKYC DSLGTTYGSN LDCYQQRPFG YGLSGLKDTM