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Reviewed, UniProtKB/Swiss-Prot P17541 (CHIA_CUCSA)

Last modified September 22, 2009. Version 68. 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:
    Acidic endochitinase
    EC=3.2.1.14
OrganismCucumis sativus (Cucumber)
Taxonomic identifier3659 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids ICucurbitalesCucurbitaceaeCucumis

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

This protein functions as a 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

Secretedextracellular space.

Induction

By salicylate and upon tobacco necrosis virus infection.

Sequence similarities

Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Chitin degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processchitin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncation binding

Inferred from electronic annotation. Source: InterPro

chitinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525
Chain26 – 292267Acidic endochitinase
PRO_0000011916

Sites

Active site1521Proton donor By similarity

Amino acid modifications

Disulfide bond45 ↔ 92 By similarity
Disulfide bond75 ↔ 82 By similarity
Disulfide bond180 ↔ 209 By similarity

Sequences

Sequence LengthMass (Da)Tools
P17541-1 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 2DE39D42BBDB0093

FASTA29230,774
        10         20         30         40         50         60 
MAAHKITTTL SIFFLLSSIF RSSDAAGIAI YWGQNGNEGS LASTCATGNY EFVNIAFLSS 

        70         80         90        100        110        120 
FGSGQAPVLN LAGHCNPDNN GCAFLSDEIN SCKSQNVKVL LSIGGGAGSY SLSSADDAKQ 

       130        140        150        160        170        180 
VANFIWNSYL GGQSDSRPLG AAVLDGVDFD IESGSGQFWD VLAQELKNFG QVILSAAPQC 

       190        200        210        220        230        240 
PIPDAHLDAA IKTGLFDSVW VQFYNNPPCM FADNADNLLS SWNQWTAFPT SKLYMGLPAA 

       250        260        270        280        290 
REAAPSGGFI PADVLISQVL PTIKASSNYG GVMLWSKAFD NGYSDSIKGS IG 

« Hide

References

[1]"Isolation of a complementary DNA encoding a chitinase with structural homology to a bifunctional lysozyme/chitinase."
Metraux J.P., Burkhart W., Moyer M., Dincher S., Middlesteadt W., Williams S., Payne G., Carnes M., Ryals J.
Proc. Natl. Acad. Sci. U.S.A. 86:896-900(1989) [PubMed: 2915985] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: cv. Wisconsin SMR-58.
[2]"Regulation of cucumber class III chitinase gene expression."
Lawton K., Beck J., Potter S., Ward E., Ryals J.
Mol. Plant Microbe Interact. 7:48-57(1994) [PubMed: 8167370] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Tissue: Leaf.

Cross-references

Sequence databases

M24365 mRNA. Translation: AAA33120.1.
M84214 Unassigned DNA. Translation: AAC37395.1.
PIRA31455.

3D structure databases

HSSPHSSP built from PDB template 2HVM based on UniProtKB P23472.
ModBaseSearch...

Protein family/group databases

CAZyGH18. Glycoside Hydrolase Family 18.

Enzyme and pathway databases

BRENDA3.2.1.14. 1241.

Family and domain databases

InterProIPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
PROSITEPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHIA_CUCSA
AccessionPrimary (citable) accession number: P17541
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: September 22, 2009
This is version 68 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