CHI3_ORYSJ
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 03-AUG-2022, entry version 152.
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; 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}.
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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; 4530.OS06T0726100-01; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PaxDb; P24626; -.
DR PRIDE; 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; GNFYSYN; -.
DR OrthoDB; 1132954at2759; -.
DR BRENDA; 3.2.1.14; 4460.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR ExpressionAtlas; P24626; baseline and differential.
DR Genevisible; P24626; OS.
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 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.
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
