ID   CHI12_ORYSJ             Reviewed;         326 AA.
AC   P25765; A0A0P0VYS9; Q0DR51; Q7Y1K8;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   02-SEP-2026, entry version 165.
DE   RecName: Full=Chitinase 12;
DE            EC=3.2.1.14;
DE   AltName: Full=Basic endochitinase 2;
DE   AltName: Full=Pathogenesis related (PR)-3 chitinase 12;
DE   Flags: Precursor;
GN   Name=Cht12; Synonyms=RCH10;
GN   OrderedLocusNames=Os03g0418000, LOC_Os03g30470;
GN   ORFNames=OSJNBb0028K20.4, OSJNBb0056B16.17;
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 [MRNA].
RX   PubMed=2034221; DOI=10.1007/bf00273615;
RA   Zhu Q., Lamb C.J.;
RT   "Isolation and characterization of a rice gene encoding a basic
RT   chitinase.";
RL   Mol. Gen. Genet. 226:289-296(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
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=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   [5]
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   [6]
RP   FUNCTION.
RX   PubMed=12885168; DOI=10.1023/a:1024276127001;
RA   Kim J.-K., Jang I.-C., Wu R., Zuo W.-N., Boston R.S., Lee Y.-H., Ahn I.-P.,
RA   Nahm B.H.;
RT   "Co-expression of a modified maize ribosome-inactivating protein and a rice
RT   basic chitinase gene in transgenic rice plants confers enhanced resistance
RT   to sheath blight.";
RL   Transgenic Res. 12:475-484(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).
CC   -!- FUNCTION: Hydrolyzes chitin and plays a role in defense against fungal
CC       pathogens containing chitin. Its overexpression confers enhanced
CC       resistance to sheath blight pathogen (R.solani).
CC       {ECO:0000269|PubMed:12885168}.
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 in meristems and at lower levels in roots
CC       and sheaths. {ECO:0000269|PubMed:16936841}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=Ref.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=Ref.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR   EMBL; AC137992; AAP44624.1; -; Genomic_DNA.
DR   EMBL; AC145386; AAR01697.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF96639.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF12287.2; -; Genomic_DNA.
DR   EMBL; AP014959; BAS84717.1; -; Genomic_DNA.
DR   PIR; S15997; S15997.
DR   AlphaFoldDB; P25765; -.
DR   SMR; P25765; -.
DR   FunCoup; P25765; 263.
DR   STRING; 39947.P25765; -.
DR   PaxDb; 39947-P25765; -.
DR   EnsemblPlants; Os03t0418000-00; Os03t0418000-00; Os03g0418000.
DR   Gramene; Os03t0418000-00; Os03t0418000-00; Os03g0418000.
DR   KEGG; dosa:Os03g0418000; -.
DR   eggNOG; KOG4742; Eukaryota.
DR   HOGENOM; CLU_045506_1_0_1; -.
DR   InParanoid; P25765; -.
DR   OMA; INGGHEC; -.
DR   OrthoDB; 5985073at2759; -.
DR   Proteomes; UP000059680; Chromosome 3.
DR   GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IDA: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; IDA:Gramene.
DR   GO; GO:0006040; P:amino sugar metabolic process; IDA:Gramene.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:InterPro.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR   CDD; cd00325; chitinase_GH19; 1.
DR   CDD; cd06921; ChtBD1_GH19_hevein; 1.
DR   FunFam; 3.30.60.10:FF:000001; Basic endochitinase; 1.
DR   FunFam; 3.30.20.10:FF:000001; Endochitinase (Chitinase); 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; CHITINASE 12; 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.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..326
FT                   /note="Chitinase 12"
FT                   /id="PRO_0000005306"
FT   DOMAIN          22..62
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   ACT_SITE        147
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   DISULFID        24..39
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        33..45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        36..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        38..52
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        56..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        102..165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        179..187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        286..318
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   326 AA;  33636 MW;  41E748706FAFEDC1 CRC64;
     MRALAVVAMV ATAFLAAAVH AEQCGSQAGG AVCPNCLCCS QFGWCGSTSD YCGAGCQSQC
     SAAGCGGGGP TPPSGSGGSG VASIVSRSLF DQMLLHRNDA ACPASNFYTY DAFVAAASAF
     PGFAAAGGDA DTNKREVAAF LAQTSHETTG GWATAPDGPY AWGYCFKEEN GGAAGPDYCQ
     QSAQWPCAAG KKYYGRGPIQ LSYNFNYGPA GQAIGADLLG DPDLVASDAT VSFDTAFWFW
     MTPQSPKPSC HAVATGQWTP SADDQAAGRV PGYGVITNII NGGLECGHGE DDRVADRIGF
     YKRYCDILGV SYDANLDCYS QRPFGS
//