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Reviewed, UniProtKB/Swiss-Prot P24091 (CHI2_TOBAC)

Last modified June 16, 2009. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Endochitinase B
      Short name=CHN-B
    EC=3.2.1.14
Gene names
Name: CHN50
OrganismNicotiana tabacum (Common tobacco)
Taxonomic identifier4097 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Vacuole. Note: Vacuolar and protoplast. Ref.4

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.3
Chain24 – 317294Endochitinase B
PRO_0000005332
Propeptide318 – 3247Removed in mature form Probable
PRO_0000005333

Regions

Domain24 – 6542Chitin-binding type-1

Amino acid modifications

Modified residue6714-hydroxyproline Ref.5
Modified residue6914-hydroxyproline Ref.5
Disulfide bond26 ↔ 41 By similarity
Disulfide bond35 ↔ 47 By similarity
Disulfide bond40 ↔ 54 By similarity
Disulfide bond59 ↔ 63 By similarity
Disulfide bond96 ↔ 158 By similarity
Disulfide bond170 ↔ 178 By similarity
Disulfide bond277 ↔ 309 By similarity

Sequences

Sequence LengthMass (Da)Tools
P24091-1 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: FA65DC2113B33EB6

FASTA32434,721
        10         20         30         40         50         60 
MRLREFTALS SLLFSLLLLS ASAEQCGSQA GGARCASGLC CSKFGWCGNT NDYCGPGNCQ 

        70         80         90        100        110        120 
SQCPGGPTPP GGGDLGSIIS SSMFDQMLKH RNDNACQGKG FYSYNAFINA ARSFPGFGTS 

       130        140        150        160        170        180 
GDTTARKREI AAFFAQTSHE TTGGWATAPD GPYAWGYCWL REQGSPGDYC TPSGQWPCAP 

       190        200        210        220        230        240 
GRKYFGRGPI QISHNYNYGP CGRAIGVDLL NNPDLVATDP VISFKSALWF WMTPQSPKPS 

       250        260        270        280        290        300 
CHDVIIGRWQ PSSADRAANR LPGFGVITNI INGGLECGRG TDSRVQDRIG FYRRYCSILG 

       310        320 
VSPGDNLDCG NQRSFGNGLL VDTM 

« Hide

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.
PIRS20981.

3D structure databases

HSSPHSSP built from PDB template 1CNS based on UniProtKB P23951.
SMRP24091. Positions 24-315.
ModBaseSearch...

Protein family/group databases

CAZyCBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Enzyme and pathway databases

BRENDA3.2.1.14. 298.

Family and domain databases

InterProIPR018371. Chitin-binding_1_CS.
IPR001002. Chitin_bd_1.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
[Graphical view]
Gene3DG3DSA:3.30.60.10. Chitin_bd_1. 1 hit.
PANTHERPTHR22595. Glyco_hydro_19_cat. 1 hit.
PfamPF00187. Chitin_bind_1. 1 hit.
PF00182. Glyco_hydro_19. 1 hit.
[Graphical view]
PIRSFPIRSF001060. Endochitinase. 1 hit.
PRINTSPR00451. CHITINBINDNG.
ProDomPD000609. Chitin_binding_1. 1 hit.
PD354900. Glyco_hydro_19. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00270. ChtBD1. 1 hit.
[Graphical view]
PROSITEPS00026. 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]
ProtoNetSearch...

Entry information

Entry nameCHI2_TOBAC
AccessionPrimary (citable) accession number: P24091
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: June 16, 2009
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents