ID   CHI2_TAXBA              Reviewed;          19 AA.
AC   P85338;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Endochitinase 2;
DE            EC=3.2.1.14;
DE   Flags: Fragment;
OS   Taxus baccata (English yew).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Taxaceae;
OC   Taxus.
OX   NCBI_TaxID=25629;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   STRAIN=PC-1008 {ECO:0000269|PubMed:19157640};
RC   TISSUE=Callus {ECO:0000269|PubMed:19157640};
RX   PubMed=19157640; DOI=10.1016/j.jplph.2008.11.009;
RA   Uzal E.N., Gomez-Ros L.V., Hernandez J.A., Pedreno M.A., Cuello J.,
RA   Ros Barcelo A.;
RT   "Analysis of the soluble cell wall proteome of gymnosperms.";
RL   J. Plant Physiol. 166:831-843(2009).
CC   -!- FUNCTION: Defense against chitin-containing fungal pathogens.
CC       {ECO:0000305}.
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: Secreted, cell wall
CC       {ECO:0000269|PubMed:19157640}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily. {ECO:0000255}.
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DR   AlphaFoldDB; P85338; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
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.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cell wall; Chitin degradation;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Plant defense; Polysaccharide degradation; Secreted.
FT   CHAIN           <1..>19
FT                   /note="Endochitinase 2"
FT                   /id="PRO_0000314646"
FT   DISULFID        17..?
FT                   /evidence="ECO:0000250|UniProtKB:Q39785"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:19157640"
FT   NON_TER         19
FT                   /evidence="ECO:0000303|PubMed:19157640"
SQ   SEQUENCE   19 AA;  1898 MW;  DBC4347B85B4A1B9 CRC64;
     TAGFGVFTNI INGGLECGK