CHI8_ORYSJ
ID CHI8_ORYSJ Reviewed; 261 AA.
AC Q7XCK6; A0A0P0XX79; O80423; Q9FWE9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Chitinase 8;
DE EC=3.2.1.14;
DE AltName: Full=Class II chitinase a;
DE Short=OsChia2a;
DE AltName: Full=Pathogenesis related (PR)-3 chitinase 8;
DE Flags: Precursor;
GN Name=Cht8; Synonyms=Cht2; OrderedLocusNames=Os10g0542900, LOC_Os10g39680;
GN ORFNames=OsJ_32330, OSJNBb0015I11.14;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
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 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 [7]
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 [8]
RP INDUCTION.
RX PubMed=9617819; DOI=10.1023/a:1005960313459;
RA Kim C.Y., Gal S.W., Choe M.S., Jeong S.Y., Lee S.I., Cheong Y.H., Lee S.H.,
RA Choi Y.J., Han C.-D., Kang K.Y., Cho M.J.;
RT "A new class II rice chitinase, Rcht2, whose induction by fungal elicitor
RT is abolished by protein phosphatase 1 and 2A inhibitor.";
RL Plant Mol. Biol. 37:523-534(1998).
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 -!- 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 roots, leaves, sheaths and meristems.
CC {ECO:0000269|PubMed:16936841}.
CC -!- INDUCTION: By glycol chitin and fungal elicitor in suspension cell
CC culture and ethephon in leaves. {ECO:0000269|PubMed:9617819}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class II subfamily. {ECO:0000305}.
CC -!- CAUTION: Lacks the chitin binding type-1 domain wich is one of the
CC conserved features of the chitinase class I and class IV subfamilies.
CC {ECO:0000305}.
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DR EMBL; AB016497; BAA31997.1; -; mRNA.
DR EMBL; AC051633; AAG13608.1; -; Genomic_DNA.
DR EMBL; DP000086; AAP54865.1; -; Genomic_DNA.
DR EMBL; AP008216; BAF27110.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT11881.1; -; Genomic_DNA.
DR EMBL; CM000147; EAZ16856.1; -; Genomic_DNA.
DR EMBL; AK070067; BAG91751.1; -; mRNA.
DR RefSeq; XP_015614506.1; XM_015759020.1.
DR AlphaFoldDB; Q7XCK6; -.
DR SMR; Q7XCK6; -.
DR STRING; 4530.OS10T0542900-01; -.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PaxDb; Q7XCK6; -.
DR PRIDE; Q7XCK6; -.
DR EnsemblPlants; Os10t0542900-01; Os10t0542900-01; Os10g0542900.
DR GeneID; 4349267; -.
DR Gramene; Os10t0542900-01; Os10t0542900-01; Os10g0542900.
DR KEGG; osa:4349267; -.
DR eggNOG; KOG4742; Eukaryota.
DR HOGENOM; CLU_045506_1_0_1; -.
DR InParanoid; Q7XCK6; -.
DR OMA; PIQLTHQ; -.
DR OrthoDB; 1132954at2759; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000007752; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR Genevisible; Q7XCK6; OS.
DR GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR016283; Glyco_hydro_19.
DR InterPro; IPR000726; Glyco_hydro_19_cat.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR Pfam; PF00182; Glyco_hydro_19; 1.
DR PIRSF; PIRSF001060; Endochitinase; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS00773; CHITINASE_19_1; 1.
DR PROSITE; PS00774; CHITINASE_19_2; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Disulfide bond; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..261
FT /note="Chitinase 8"
FT /id="PRO_0000383468"
FT ACT_SITE 98
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT DISULFID 53..115
FT /evidence="ECO:0000250"
FT DISULFID 221..253
FT /evidence="ECO:0000250"
FT CONFLICT 199..200
FT /note="DT -> EH (in Ref. 1; BAA31997)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 261 AA; 27552 MW; 773133E7813DFDBE CRC64;
MTTTTTRFVQ LAACAAASLL AVAASGAAAQ GVGSVITQAV FNSMLPNRDN SQCPARGFYT
YDAFIAAANS FPAFGTSGGS AELIRRELAA FFGQTSHETT GGTRGSSDQF QWGYCFKEEI
NKATSPPYYG RGPIQLTGQS NYQAAGNALG LDLVGNPDLV STDAVVSFKT AIWFWMTAQG
NKPSCHDVIL GRWTPSAADT AAGRVPGYGV ITNIINGGIE CGVGQNDANV DRIGYYKRYC
DMLGAGYGSN LDCYNQRNFA S
