CHI12_ORYSJ
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 03-AUG-2022, entry version 152.
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; 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 RefSeq; XP_015629397.1; XM_015773911.1.
DR AlphaFoldDB; P25765; -.
DR SMR; P25765; -.
DR STRING; 4530.OS03T0418000-00; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PaxDb; P25765; -.
DR PRIDE; P25765; -.
DR EnsemblPlants; Os03t0418000-00; Os03t0418000-00; Os03g0418000.
DR GeneID; 4333121; -.
DR Gramene; Os03t0418000-00; Os03t0418000-00; Os03g0418000.
DR KEGG; osa:4333121; -.
DR eggNOG; KOG4742; Eukaryota.
DR HOGENOM; CLU_045506_1_0_1; -.
DR InParanoid; P25765; -.
DR OMA; CQQSAQW; -.
DR OrthoDB; 1132954at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
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: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..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
