Q7DNA1 (CHI2_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chitinase 2
EC=3.2.1.14

Alternative name(s):
Class I chitinase b
Short name=OsChia1b
Pathogenesis related (PR)-3 chitinase 2

Gene names

Name:	Cht2
Synonyms:	RC7
Ordered Locus Names:	Os05g0399300, LOC_Os05g33130
ORF Names:	OsJ_18467

Organism

Oryza sativa subsp. japonica (Rice) [Reference proteome]

Taxonomic identifier

39947 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Liliopsida › commelinids › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza › Oryza sativa

Protein attributes

Sequence length	340 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes chitin and plays a role in defense against fungal pathogens containing chitin. Its overexpression confers enhanced resistance to sheath blight pathogen (R.solani). Ref.5 Ref.7 Ref.8
Catalytic activity	Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Tissue specificity	Expressed in roots, sheaths and meristems. Ref.6
Sequence similarities	Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily. Contains 1 chitin-binding type-1 domain.
Sequence caution	The sequence BAF17390.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Chitin degradation Plant defense Polysaccharide degradation
Domain	Signal
Ligand	Chitin-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW defense response to fungus Inferred from direct assay Ref.7. Source: UniProtKB jasmonic acid and ethylene-dependent systemic resistance, ethylene mediated signaling pathway Inferred from electronic annotation. Source: EnsemblPlants/Gramene polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW response to cadmium ion Inferred from electronic annotation. Source: EnsemblPlants/Gramene
Cellular_component	plasma membrane Inferred from electronic annotation. Source: EnsemblPlants/Gramene vacuole Inferred from electronic annotation. Source: EnsemblPlants/Gramene
Molecular_function	chitin binding Inferred from electronic annotation. Source: UniProtKB-KW chitinase activity Inferred from direct assay Ref.8Ref.7. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

32

Potential

Chain

33 – 340

308

Chitinase 2

PRO_5000139669

Regions

Domain

33 – 73

41

Chitin-binding type-1

Amino acid modifications

Disulfide bond

35 ↔ 50

Ref.9

Disulfide bond

44 ↔ 56

Ref.9

Disulfide bond

47 ↔ 74

Ref.9

Disulfide bond

49 ↔ 63

Ref.9

Disulfide bond

67 ↔ 71

Ref.9

Disulfide bond

110 ↔ 172

Ref.9

Disulfide bond

184 ↔ 192

Ref.9

Disulfide bond

291 ↔ 323

Ref.9

Experimental info

Mutagenesis

159

1

W → A: Increased activity. Ref.8

Secondary structure

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340

Helix Strand Turn

Details...

Turn

37 – 41

5

Helix

45 – 47

3

Beta strand

54 – 59

6

Helix

60 – 63

4

Helix

89 – 91

3

Helix

95 – 101

7

Turn

102 – 106

5

Turn

111 – 114

4

Helix

118 – 126

9

Turn

129 – 132

4

Beta strand

134 – 136

3

Helix

137 – 155

19

Helix

166 – 168

3

Beta strand

188 – 190

3

Turn

202 – 205

4

Helix

209 – 219

11

Turn

223 – 225

3

Helix

229 – 232

4

Helix

234 – 246

13

Helix

255 – 259

5

Helix

267 – 271

5

Helix

278 – 290

13

Beta strand

291 – 294

4

Helix

297 – 312

16

Sequences

	Sequence		Length	Mass (Da)
	Q7DNA1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 642F13E3928CA7BE	FASTA	340	35,587
	10 20 30 40 50 60 MSTPRAAASL AKKAALVALA VLAAALATAA RAEQCGAQAG GARCPNCLCC SRWGWCGTTS 70 80 90 100 110 120 DFCGDGCQSQ CSGCGPTPTP TPPSPSDGVG SIVPRDLFER LLLHRNDGAC PARGFYTYEA 130 140 150 160 170 180 FLAAAAAFPA FGGTGNTETR KREVAAFLGQ TSHETTGGWP TAPDGPFSWG YCFKQEQNPP 190 200 210 220 230 240 SDYCQPSPEW PCAPGRKYYG RGPIQLSFNF NYGPAGRAIG VDLLSNPDLV ATDATVSFKT 250 260 270 280 290 300 ALWFWMTPQG NKPSSHDVIT GRWAPSPADA AAGRAPGYGV ITNIVNGGLE CGHGPDDRVA 310 320 330 340 NRIGFYQRYC GAFGIGTGGN LDCYNQRPFN SGSSVGLAEQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence variation, differential expression and chromosomal location of rice chitinase genes." Nishizawa Y., Kishimoto N., Saito A., Hibi T. Mol. Gen. Genet. 241:1-10(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: cv. Nipponbare.
[2]	"The map-based sequence of the rice genome." International rice genome sequencing project (IRGSP) Nature 436:793-800(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[3]	"The rice annotation project database (RAP-DB): 2008 update." The rice annotation project (RAP) Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: cv. Nipponbare.
[4]	"The genomes of Oryza sativa: a history of duplications." Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H. PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[5]	"Enhanced resistance to sheath blight by constitutive expression of infection-related rice chitinase in transgenic elite indica rice cultivars." Datta K., Tu J., Oliva N., Ona I., Velazhahan R., Mew T.W., Muthukrishnan S., Datta S.K. Plant Sci. 160:405-414(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Distribution, structure, organ-specific expression, and phylogenic analysis of the pathogenesis-related protein-3 chitinase gene family in rice (Oryza sativa L.)." Nakazaki T., Tsukiyama T., Okumoto Y., Kageyama D., Naito K., Inouye K., Tanisaka T. Genome 49:619-630(2006) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY.
[7]	"Purification and characterization of a rice class I chitinase, OsChia1b, produced in Esherichia coli." Mizuno R., Itoh Y., Nishizawa Y., Kezuka Y., Suzuki K., Nonaka T., Watanabe T. Biosci. Biotechnol. Biochem. 72:893-895(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Role of the loop structure of the catalytic domain in rice class I chitinase." Mizuno R., Fukamizo T., Sugiyama S., Nishizawa Y., Kezuka Y., Nonaka T., Suzuki K., Watanabe T. J. Biochem. 143:487-495(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF TRP-159.
[9]	"Crystallization and preliminary X-ray analysis of plant class I chitinase from rice." Kezuka Y., Kitazaki K., Itoh Y., Watanabe J., Takaha O., Watanabe T., Nishizawa Y., Nonaka T. Protein Pept. Lett. 11:401-405(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 33-340, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D16222 Genomic DNA. Translation: BAA03750.1.
X56787 mRNA. Translation: CAA40107.1.
AP008211 Genomic DNA. Translation: BAF17390.1. Sequence problems.
CM000142 Genomic DNA. Translation: EEE63650.1.

PIR

S39979.
S40414.

RefSeq

NP_001055476.1. NM_001062011.1.

UniGene

Os.3374.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DKV	X-ray	2.00	A	33-340	[»]
3IWR	X-ray	2.57	A/B	33-340	[»]

ProteinModelPortal

Q7DNA1.

ModBase

Search...

Protein family/group databases

CAZy

CBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

LOC_Os05g33130.1; LOC_Os05g33130.1; LOC_Os05g33130.

GeneID

4338718.

KEGG

dosa:Os05t0399300-01.
osa:4338718.

Organism-specific databases

Gramene

Q7DNA1.

Phylogenomic databases

HOGENOM

HOG000231411.

KO

K01183.

OMA

PEWPCAP.

ProtClustDB

CLSN2919583.

Family and domain databases

Gene3D

3.30.60.10. 1 hit.

InterPro

IPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view]

Pfam

PF00187. Chitin_bind_1. 1 hit.
PF00182. Glyco_hydro_19. 1 hit.
[Graphical view]

PIRSF

PIRSF001060. Endochitinase. 1 hit.

PRINTS

PR00451. CHITINBINDNG.

ProDom

PD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00270. ChtBD1. 1 hit.
[Graphical view]

SUPFAM

SSF57016. Chitin_bd_1. 1 hit.
SSF53955. SSF53955. 1 hit.

PROSITE

PS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 1 hit.
PS00773. CHITINASE_19_1. 1 hit.
PS00774. CHITINASE_19_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q7DNA1.

Entry information

Entry name

CHI2_ORYSJ

Accession

Primary (citable) accession number: Q7DNA1
Secondary accession number(s): Q0DID3, Q43294

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	July 5, 2004
Last modified:	April 3, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program