ID   CHI3_ORYSJ              Reviewed;         320 AA.
AC   P24626; Q42994;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=Chitinase 3;
DE            EC=3.2.1.14;
DE   AltName: Full=Basic endochitinase 1;
DE   AltName: Full=Class I chitinase c;
DE            Short=OsChia1c;
DE   AltName: Full=Pathogenesis related (PR)-3 chitinase 3;
DE   Flags: Precursor;
GN   Name=Cht3; Synonyms=CH6;
GN   OrderedLocusNames=Os06g0726100, LOC_Os06g51050;
GN   ORFNames=P0017G10.2, P0548E04.22;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Seedling;
RX   PubMed=1893114; DOI=10.1007/bf00023999;
RA   Huang J.K., Wen L., Swegle M., Tran H.C., Thin T.H., Naylor H.M.,
RA   Muthukrishnan S., Reeck G.R.;
RT   "Nucleotide sequence of a rice genomic clone that encodes a class I
RT   endochitinase.";
RL   Plant Mol. Biol. 16:479-480(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7901749; DOI=10.1007/bf00280194;
RA   Nishizawa Y., Kishimoto N., Saito A., Hibi T.;
RT   "Sequence variation, differential expression and chromosomal location of
RT   rice chitinase genes.";
RL   Mol. Gen. Genet. 241:1-10(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [6]
RP   FUNCTION.
RX   PubMed=12834284; DOI=10.1271/bbb.67.1063;
RA   Truong N.-H., Park S.-M., Nishizawa Y., Watanabe T., Sasaki T., Itoh Y.;
RT   "Structure, heterologous expression, and properties of rice (Oryza sativa
RT   L.) family 19 chitinases.";
RL   Biosci. Biotechnol. Biochem. 67:1063-1070(2003).
RN   [7]
RP   GENE FAMILY, NOMENCLATURE, AND TISSUE SPECIFICITY.
RX   PubMed=16936841; DOI=10.1139/g06-020;
RA   Nakazaki T., Tsukiyama T., Okumoto Y., Kageyama D., Naito K., Inouye K.,
RA   Tanisaka T.;
RT   "Distribution, structure, organ-specific expression, and phylogenic
RT   analysis of the pathogenesis-related protein-3 chitinase gene family in
RT   rice (Oryza sativa L.).";
RL   Genome 49:619-630(2006).
RN   [8]
RP   FUNCTION.
RX   PubMed=18211919; DOI=10.1093/jb/mvn004;
RA   Mizuno R., Fukamizo T., Sugiyama S., Nishizawa Y., Kezuka Y., Nonaka T.,
RA   Suzuki K., Watanabe T.;
RT   "Role of the loop structure of the catalytic domain in rice class I
RT   chitinase.";
RL   J. Biochem. 143:487-495(2008).
CC   -!- FUNCTION: Hydrolyzes chitin and plays a role in defense against fungal
CC       pathogens containing chitin. Inhibits the growth of T.reesei fungus on
CC       plate assay. {ECO:0000269|PubMed:12834284,
CC       ECO:0000269|PubMed:18211919}.
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   -!- TISSUE SPECIFICITY: Expressed at low levels in roots, leaves, sheaths
CC       and meristems. {ECO:0000269|PubMed:16936841}.
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; X54367; CAA38249.1; -; Genomic_DNA.
DR   EMBL; D16223; BAA03751.1; -; Genomic_DNA.
DR   EMBL; AP003685; BAD61708.1; -; Genomic_DNA.
DR   EMBL; AP004685; BAD61800.1; -; Genomic_DNA.
DR   EMBL; AP014962; BAS99595.1; -; Genomic_DNA.
DR   EMBL; AK061280; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; S14948; S14948.
DR   RefSeq; XP_015643569.1; XM_015788083.1.
DR   AlphaFoldDB; P24626; -.
DR   SMR; P24626; -.
DR   STRING; 39947.P24626; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   PaxDb; 39947-P24626; -.
DR   EnsemblPlants; Os06t0726100-01; Os06t0726100-01; Os06g0726100.
DR   GeneID; 4342114; -.
DR   Gramene; Os06t0726100-01; Os06t0726100-01; Os06g0726100.
DR   KEGG; osa:4342114; -.
DR   eggNOG; KOG4742; Eukaryota.
DR   HOGENOM; CLU_045506_1_0_1; -.
DR   InParanoid; P24626; -.
DR   OMA; DSRCKAN; -.
DR   OrthoDB; 997724at2759; -.
DR   BRENDA; 3.2.1.14; 4460.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
DR   ExpressionAtlas; P24626; baseline and differential.
DR   GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; ISS:Gramene.
DR   GO; GO:0008061; F:chitin binding; ISS:Gramene.
DR   GO; GO:0004568; F:chitinase activity; IDA:UniProtKB.
DR   GO; GO:0008843; F:endochitinase activity; ISS:Gramene.
DR   GO; GO:0006040; P:amino sugar metabolic process; ISS:Gramene.
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; IDA:UniProtKB.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00325; chitinase_GH19; 1.
DR   CDD; cd06921; ChtBD1_GH19_hevein; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.30.20.10; Endochitinase, domain 2; 1.
DR   Gene3D; 3.30.60.10; Endochitinase-like; 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   PANTHER; PTHR22595:SF79; BASIC ENDOCHITINASE B; 1.
DR   PANTHER; PTHR22595; CHITINASE-RELATED; 1.
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; Lysozyme-like; 1.
DR   SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 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.
DR   Genevisible; P24626; OS.
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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..320
FT                   /note="Chitinase 3"
FT                   /id="PRO_0000005305"
FT   DOMAIN          19..59
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   ACT_SITE        141
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        33..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        35..49
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        53..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        97..159
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        172..180
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        279..311
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   CONFLICT        98
FT                   /note="A -> R (in Ref. 1; CAA38249)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        122
FT                   /note="G -> R (in Ref. 1; CAA38249)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183
FT                   /note="G -> A (in Ref. 1; CAA38249)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        202..206
FT                   /note="PAGQA -> RGAG (in Ref. 1; CAA38249)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        223
FT                   /note="Missing (in Ref. 1; CAA38249)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   320 AA;  33681 MW;  D7331BF4A6B592E3 CRC64;
     MRALALAVVA MAVVAVRGEQ CGSQAGGALC PNCLCCSQYG WCGSTSDYCG AGCQSQCSGG
     CGGGPTPPSS GGGSGVASII SPSLFDQMLL HRNDQACAAK GFYTYDAFVA AANAYPDFAT
     TGDADTCKRE VAAFLAQTSH ETTGGWPTAP DGPYSWGYCF KEENNGNAPT YCEPKPEWPC
     AAGKKYYGRG PIQITYNYNY GPAGQAIGSD LLNNPDLVAS DATVSFKTAF WFWMTPQSPK
     PSCHAVITGQ WTPSADDQAA GRVPGYGEIT NIINGGVECG HGADDKVADR IGFYKRYCDM
     LGVSYGDNLD CYNQRPYPPS
//