CHI7_ORYSJ
ID CHI7_ORYSJ Reviewed; 340 AA.
AC Q7Y1Z1; A0A0N7KKQ9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Chitinase 7;
DE EC=3.2.1.14 {ECO:0000269|PubMed:10890535};
DE AltName: Full=Class I chitinase d;
DE Short=OsChia1d;
DE AltName: Full=Pathogenesis related (PR)-3 chitinase 7;
DE Flags: Precursor;
GN Name=Cht7; Synonyms=PC; OrderedLocusNames=Os05g0399700, LOC_Os05g33150;
GN ORFNames=OSJNBa0035J16.1, P0605G01.16;
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=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(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 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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=10890535; DOI=10.1023/a:1006401816145;
RA Takakura Y., Ito T., Saito H., Inoue T., Komari T., Kuwata S.;
RT "Flower-predominant expression of a gene encoding a novel class I chitinase
RT in rice (Oryza sativa L.).";
RL Plant Mol. Biol. 42:883-897(2000).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
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 play a role in defense against
CC fungal pathogens containing chitin. {ECO:0000269|PubMed:10890535}.
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 Evidence={ECO:0000269|PubMed:10890535};
CC -!- TISSUE SPECIFICITY: Expressed in pistils, stamens and lodicules.
CC {ECO:0000269|PubMed:10890535}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I subfamily. {ECO:0000305}.
CC -!- CAUTION: Enzyme activity is uncertain. Was shown to have endochitinase
CC activity (in vitro) (PubMed:10890535). Lacks the conserved Glu residue
CC that is essential for catalytic activity, suggesting it lacks enzyme
CC activity. {ECO:0000269|PubMed:10890535, ECO:0000305}.
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DR EMBL; AB096139; BAC76690.1; -; mRNA.
DR EMBL; AC132492; AAU10808.1; -; Genomic_DNA.
DR EMBL; AC135418; AAT85136.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF17392.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS93905.1; -; Genomic_DNA.
DR EMBL; AK071196; BAG92366.1; -; mRNA.
DR RefSeq; XP_015640431.1; XM_015784945.1.
DR AlphaFoldDB; Q7Y1Z1; -.
DR SMR; Q7Y1Z1; -.
DR STRING; 4530.OS05T0399700-01; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PaxDb; Q7Y1Z1; -.
DR PRIDE; Q7Y1Z1; -.
DR EnsemblPlants; Os05t0399700-01; Os05t0399700-01; Os05g0399700.
DR GeneID; 4338720; -.
DR Gramene; Os05t0399700-01; Os05t0399700-01; Os05g0399700.
DR KEGG; osa:4338720; -.
DR eggNOG; KOG4742; Eukaryota.
DR HOGENOM; CLU_045506_1_0_1; -.
DR InParanoid; Q7Y1Z1; -.
DR OMA; CGRSCDH; -.
DR OrthoDB; 1132954at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR ExpressionAtlas; Q7Y1Z1; baseline and differential.
DR Genevisible; Q7Y1Z1; OS.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IBA:GO_Central.
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.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Disulfide bond; Glycosidase; Hydrolase; Plant defense;
KW Polysaccharide degradation; Reference proteome; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..340
FT /note="Chitinase 7"
FT /id="PRO_0000383466"
FT DOMAIN 33..73
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 35..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 44..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 49..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 67..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 118..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 185..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 293..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 340 AA; 35300 MW; 3EC5430B3E9F1515 CRC64;
MIAARAANLQ VAMKALALAV LALAYAAATA RAEQCGRQAG GARCPNRLCC SRWGWCGLTD
DYCKGGCQSQ CRVSRDGGDD DVAAVLLTAP GGGRAGVASV VTSDQFERML PHRDDAACPA
RGFYAYRAFV AAAGAFPAFA ATGDADTRKR EVAAFLAQTS HATSGGPYSW GYCYKEVKGA
TSDFCVPNAR WPCAPGKAYH ARGPMQIAYN YNYGAAGEAI GADLLGNPEL VATDPTVAFK
TALWLWMTAR SPSQPSPHAV VTGQWTPTPA DSAAGRAPGY GLTTNILTGG LQCAGGNGGA
DRVAFYKRYC DVLGVGYGPN LDCFGQAPFD GDIMSASAAK
