CHIC_POPTR
ID CHIC_POPTR Reviewed; 121 AA.
AC P29032;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Acidic endochitinase WIN6.2C;
DE EC=3.2.1.14;
DE Flags: Precursor; Fragment;
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].
RX PubMed=1912489; DOI=10.1007/bf00037049;
RA Davis J.M., Clarke H.R.G., Bradshaw H.D. Jr., Gordon M.P.;
RT "Populus chitinase genes: structure, organization, and similarity of
RT translated sequences to herbaceous plant chitinases.";
RL Plant Mol. Biol. 17:631-639(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nisqually;
RX PubMed=16973872; DOI=10.1126/science.1128691;
RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA Chapman J., Chen G.-L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA dePamphilis C.W., Detter J., Dirks B., Dubchak I., Duplessis S.,
RA Ehlting J., Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J.,
RA Groover A., Gunter L., Hamberger B., Heinze B., Helariutta Y.,
RA Henrissat B., Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J.,
RA Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S., Martin F.,
RA Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA Tsai C.-J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA Rokhsar D.S.;
RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL Science 313:1596-1604(2006).
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; X59995; CAA42614.1; -; Genomic_DNA.
DR EMBL; CM009298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P29032; -.
DR SMR; P29032; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR EnsemblPlants; PNT21326; PNT21326; POPTR_009G141800v3.
DR Gramene; PNT21326; PNT21326; POPTR_009G141800v3.
DR Proteomes; UP000006729; Chromosome 9.
DR ExpressionAtlas; P29032; 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; 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 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.
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.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..>121
FT /note="Acidic endochitinase WIN6.2C"
FT /id="PRO_0000005318"
FT DOMAIN 23..63
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT REGION 78..121
FT /note="Catalytic"
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 NON_TER 121
SQ SEQUENCE 121 AA; 12689 MW; A89DFC96795FE87F CRC64;
MSVWAFFAFF SLFLSLSVRG SAEQCGRQAG DALCPGGLCC SFYGWCGTTV DYCGDGCQSQ
CDGGDGCDGG GGGGGDGDDG YLSDIIPKST FDALLKFRND PRCHAVGFYT YDAFISAAKE
F
