Reviewed,
UniProtKB/Swiss-Prot P24091 (CHI2_TOBAC)
Last modified
June 16, 2009.
Version 88.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Endochitinase B Short name=CHN-B EC=3.2.1.14 | ||
| Gene names |
| ||
| Organism | Nicotiana tabacum (Common tobacco) | ||
| Taxonomic identifier | 4097 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Nicotianoideae › Nicotianeae › Nicotiana |
Protein attributes
| Sequence length | 324 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 | Defense against chitin containing fungal pathogens. |
| Catalytic activity | Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. |
| Subcellular location | |
| Induction | By ethylene. |
| Post-translational modification | The 4-hydroxyproline residues are not glycosylated in this plant vacuolar protein. |
| Sequence similarities | Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily. Contains 1 chitin-binding type-1 domain. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 23 | 23 | Ref.3 | ||||||||
| Chain | 24 – 317 | 294 | Endochitinase B | PRO_0000005332 | |||||||
| Propeptide | 318 – 324 | 7 | Removed in mature form Probable | PRO_0000005333 | |||||||
Regions | |||||||||||
| Domain | 24 – 65 | 42 | Chitin-binding type-1 | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 67 | 1 | 4-hydroxyproline Ref.5 | ||||||||
| Modified residue | 69 | 1 | 4-hydroxyproline Ref.5 | ||||||||
| Disulfide bond | 26 ↔ 41 | By similarity | |||||||||
| Disulfide bond | 35 ↔ 47 | By similarity | |||||||||
| Disulfide bond | 40 ↔ 54 | By similarity | |||||||||
| Disulfide bond | 59 ↔ 63 | By similarity | |||||||||
| Disulfide bond | 96 ↔ 158 | By similarity | |||||||||
| Disulfide bond | 170 ↔ 178 | By similarity | |||||||||
| Disulfide bond | 277 ↔ 309 | By similarity | |||||||||
Sequences
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References
| [1] | "Gene structure and expression of a tobacco endochitinase gene in suspension-cultured tobacco cells." Fukuda Y., Ohme M., Shinshi H. Plant Mol. Biol. 16:1-10(1991) [PubMed: 1888889] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Bright Yellow 4. Tissue: Leaf. |
| [2] | "The structure and regulation of homeologous tobacco endochitinase genes of Nicotiana sylvestris and N. tomentosiformis origin." van Buuren M., Neuhaus J.-M., Shinshi H., Ryals J., Meins F. Jr. Mol. Gen. Genet. 232:460-469(1992) [PubMed: 1588915] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Havana 425. Tissue: Leaf. |
| [3] | "Regulation of a plant pathogenesis-related enzyme: inhibition of chitinase and chitinase mRNA accumulation in cultured tobacco tissues by auxin and cytokinin." Shinshi H., Mohnen D., Meins F. Jr. Proc. Natl. Acad. Sci. U.S.A. 84:89-93(1987) [PubMed: 16593796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 15-324, PROTEIN SEQUENCE OF 24-53. Strain: cv. Havana. |
| [4] | "A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole." Neuhaus J.-M., Sticher L., Meins F. Jr., Boller T. Proc. Natl. Acad. Sci. U.S.A. 88:10362-10366(1991) [PubMed: 1946457] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [5] | "Vacuolar chitinases of tobacco: a new class of hydroxyproline-containing proteins." Sticher L., Hofsteenge J., Milani A., Neuhaus J.-M., Meins F. Jr. Science 257:655-657(1992) [PubMed: 1496378] [Abstract] Cited for: HYDROXYLATION AT PRO-67 AND PRO-69, MASS SPECTROMETRY. |
Cross-references
Sequence databases | |
|---|---|
| X51599 Genomic DNA. Translation: CAA35945.1. X64519 Genomic DNA. Translation: CAA45822.1. M15173 mRNA. Translation: AAA34070.1. | |
| PIR | S20981. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1CNS based on UniProtKB P23951. |
| SMR | P24091. Positions 24-315. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | CBM18. Carbohydrate-Binding Module Family 18. GH19. Glycoside Hydrolase Family 19. |
Enzyme and pathway databases | |
| BRENDA | 3.2.1.14. 298. |
Family and domain databases | |
| InterPro | IPR018371. Chitin-binding_1_CS. IPR001002. Chitin_bd_1. IPR016283. Glyco_hydro_19. IPR000726. Glyco_hydro_19_cat. [Graphical view] |
| Gene3D | G3DSA:3.30.60.10. Chitin_bd_1. 1 hit. |
| PANTHER | PTHR22595. Glyco_hydro_19_cat. 1 hit. |
| 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_binding_1. 1 hit. PD354900. Glyco_hydro_19. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00270. ChtBD1. 1 hit. [Graphical view] |
| 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... |
Entry information
| Entry name | CHI2_TOBAC | ||||||||
| Accession | Primary (citable) accession number: P24091 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

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