ID   CHI4_ORYSJ              Reviewed;         285 AA.
AC   O04138; Q7XU64;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=Chitinase 4;
DE            EC=3.2.1.14;
DE   AltName: Full=OsChia2b;
DE   AltName: Full=Pathogenesis related (PR)-3 chitinase 4;
DE   Flags: Precursor;
GN   Name=Cht4; OrderedLocusNames=Os04g0493400, LOC_Os04g41620;
GN   ORFNames=OsJ_15306, OSJNBb0091E11.8;
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   STRAIN=cv. Nipponbare;
RA   Nakazaki T., Ikehashi H.;
RT   "Genomic sequence and polymorphisms of a rice chitinase gene, Cht4.";
RL   Breed. Sci. 48:371-376(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
RC   STRAIN=cv. Nipponbare;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447439; DOI=10.1038/nature01183;
RA   Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA   Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA   Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA   Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA   Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA   Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA   Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA   Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA   Li J., Hong G., Xue Y., Han B.;
RT   "Sequence and analysis of rice chromosome 4.";
RL   Nature 420:316-320(2002).
RN   [4]
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   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [9]
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).
CC   -!- FUNCTION: Hydrolyzes chitin and may function in reproductive organs
CC       during embryogenesis and seed maturation.
CC       {ECO:0000269|PubMed:12834284}.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O04138-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O04138-2; Sequence=VSP_037998, VSP_037999;
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in leaves, sheaths and
CC       meristems. {ECO:0000269|PubMed:16936841}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class IV subfamily. {ECO:0000305}.
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DR   EMBL; AB054687; BAB21374.1; -; Genomic_DNA.
DR   EMBL; AB003194; BAA19793.1; -; mRNA.
DR   EMBL; AL606629; CAD41540.2; -; Genomic_DNA.
DR   EMBL; AP008210; BAF15098.1; -; Genomic_DNA.
DR   EMBL; AP014960; BAS89866.1; -; Genomic_DNA.
DR   EMBL; CM000141; EAZ31206.1; -; Genomic_DNA.
DR   EMBL; AK060363; BAG87422.1; -; mRNA.
DR   EMBL; AK099973; BAG94383.1; -; mRNA.
DR   PIR; T03405; T03405.
DR   AlphaFoldDB; O04138; -.
DR   SMR; O04138; -.
DR   STRING; 39947.O04138; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   PaxDb; 39947-O04138; -.
DR   EnsemblPlants; Os04t0493400-01; Os04t0493400-01; Os04g0493400. [O04138-2]
DR   Gramene; Os04t0493400-01; Os04t0493400-01; Os04g0493400. [O04138-2]
DR   eggNOG; KOG4742; Eukaryota.
DR   InParanoid; O04138; -.
DR   OMA; KCHSAIT; -.
DR   Proteomes; UP000000763; Chromosome 4.
DR   Proteomes; UP000007752; Chromosome 4.
DR   Proteomes; UP000059680; Chromosome 4.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004568; F:chitinase activity; IDA:UniProtKB.
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   CDD; cd00325; chitinase_GH19; 1.
DR   CDD; cd00035; ChtBD1; 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; CHITINASE-RELATED; 1.
DR   PANTHER; PTHR22595:SF147; ENDOCHITINASE CHI; 1.
DR   Pfam; PF00187; Chitin_bind_1; 1.
DR   Pfam; PF00182; Glyco_hydro_19; 2.
DR   PIRSF; PIRSF001060; Endochitinase; 1.
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.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Carbohydrate metabolism; Chitin degradation;
KW   Chitin-binding; Disulfide bond; Glycosidase; Hydrolase; Plant defense;
KW   Polysaccharide degradation; Reference proteome; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..285
FT                   /note="Chitinase 4"
FT                   /id="PRO_0000383463"
FT   DOMAIN          28..62
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   ACT_SITE        148
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   DISULFID        30..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        32..44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        37..51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        55..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        104..153
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        166..175
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        253..285
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   VAR_SEQ         1..56
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12834284,
FT                   ECO:0000303|PubMed:12869764"
FT                   /id="VSP_037998"
FT   VAR_SEQ         57..80
FT                   /note="SGPCWGSGGEAAAGMAGRKAGAGA -> MANSPTLTMLVFLAIGLSLVLSAA
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12834284,
FT                   ECO:0000303|PubMed:12869764"
FT                   /id="VSP_037999"
SQ   SEQUENCE   285 AA;  30451 MW;  289A6A44CB5EBFCE CRC64;
     MAAKMATMVA LVFGLALLLS AAAPAAAQNC GCQDGYCCSQ WGYCGTTEAY CGQGCQSGPC
     WGSGGEAAAG MAGRKAGAGA GVSVESVVTE AFFNGIKNQA PNGCAGKSFY TRQSFLNAAR
     SYSGFANDRT NDDSKREIAA FFAHVTHETG HMCYINEING ANMDYCDKSN KQWPCQPGKK
     YYGRGPLQIS WNFNYGPAGK NIGFDGLRDP DKVAQDPTIS FKTALWFWMN NVHQVMSQGF
     GATIRAINGA LECNGKNPGA VNARVNYYKD YCRQFGVSPG GNLYC
//