WIN6.2C

UniProt ID: P29032
Organism: Populus trichocarpa
Review Status: COMPLETE
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Gene Description

Acidic endochitinase WIN6.2C, a glycoside hydrolase family 19 enzyme that catalyzes the random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Functions as a plant defense protein against chitin-containing fungal pathogens and is induced by wounding. Contains a chitin-binding domain and a catalytic domain. The protein is synthesized as a precursor with a signal peptide and belongs to the chitinase class I subfamily.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0004568 chitinase activity
IEA
GO_REF:0000002
MODIFY
Summary: Correct but not specific enough. The enzyme is specifically an endochitinase.
Proposed replacements: endochitinase activity
Supporting Evidence:
UniProt:P29032
RecName: Full=Acidic endochitinase WIN6.2C
GO:0006032 chitin catabolic process
IEA
GO_REF:0000120
ACCEPT
Summary: Correct annotation representing the core biological process.
Supporting Evidence:
UniProt:P29032
Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
GO:0008061 chitin binding
IEA
GO_REF:0000120
ACCEPT
Summary: Correct annotation supported by domain architecture.
Supporting Evidence:
UniProt:P29032
DOMAIN 23..63 /note="Chitin-binding type-1"
GO:0016998 cell wall macromolecule catabolic process
IEA
GO_REF:0000002
KEEP AS NON CORE
Summary: Correct broader process annotation; chitin is a cell wall macromolecule in fungi.
Supporting Evidence:
UniProt:P29032
Defense against chitin-containing fungal pathogens
GO:0000272 polysaccharide catabolic process
IEA
GO_REF:0000043
KEEP AS NON CORE
Summary: Correct but broad annotation; chitin is a polysaccharide.
Supporting Evidence:
UniProt:P29032
Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
GO:0006952 defense response
IEA
GO_REF:0000043
MODIFY
Summary: Correct but not specific enough. The enzyme provides defense specifically against other organisms.
Supporting Evidence:
UniProt:P29032
Defense against chitin-containing fungal pathogens
GO:0008843 endochitinase activity
IEA
GO_REF:0000003
ACCEPT
Summary: Correct and specific molecular function annotation representing the core enzymatic activity.
Supporting Evidence:
UniProt:P29032
Acidic endochitinase WIN6.2C; EC=3.2.1.14
PMID:1912489
The predicted Win6 proteins have a putative signal peptide, a cysteine-rich 'hevein' domain, a hinge region, and a catalytic domain as described in Shinshi et al. [Plant Mol Biol 14: 357-368].
file:POPTR/WIN6.2C/WIN6.2C-deep-research-openai.md
The protein is in the chitinase/endochitinase activity space, which supports `endochitinase activity` over broader hydrolase labels.
GO:0016787 hydrolase activity
IEA
GO_REF:0000043
KEEP AS NON CORE
Summary: Correct but very general. Chitinases are hydrolases.
Supporting Evidence:
UniProt:P29032
GO; GO:0008843; F:endochitinase activity; IEA:UniProtKB-EC
GO:0016798 hydrolase activity, acting on glycosyl bonds
IEA
GO_REF:0000043
KEEP AS NON CORE
Summary: Correct and more specific than general hydrolase activity.
Supporting Evidence:
UniProt:P29032
Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin
GO:0098542 defense response to other organism
IEA
GO_REF:0000117
ACCEPT
Summary: Correct and specific biological process representing the core defensive function.
Supporting Evidence:
UniProt:P29032
Defense against chitin-containing fungal pathogens
PMID:1912489
Poplar trees have at least two different chitinase genes, win6 and win8, which are systemically wound-inducible and belong to multigene families [Proc Natl Acad Sci USA 86: 7895-7899].

Core Functions

catalyzes the random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins as part of plant defense mechanisms

Supporting Evidence:
  • UniProt:P29032
    Acidic endochitinase WIN6.2C with EC:3.2.1.14 activity catalyzing random endo-hydrolysis of chitin
  • PMID:1912489
    The predicted Win6 proteins have a putative signal peptide, a cysteine-rich 'hevein' domain, a hinge region, and a catalytic domain as described in Shinshi et al. [Plant Mol Biol 14: 357-368].

binds chitin substrates through a specialized chitin-binding type-1 domain to facilitate enzymatic degradation

Molecular Function:
chitin binding
Supporting Evidence:
  • UniProt:P29032
    Contains chitin-binding type-1 domain (residues 23-63)

References

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Suggested Questions for Experts

Q: How does WIN6.2C contribute to plant defense responses and pathogen resistance?

Q: What determines the specificity of WIN6.2C recognition by different pathogen effectors?

Q: How is WIN6.2C expression regulated during pathogen infection and stress responses?

Q: What role does WIN6.2C play in the broader plant immune system and resistance gene networks?

Suggested Experiments

Experiment: Pathogen infection assays to study WIN6.2C function in disease resistance

Experiment: Protein-protein interaction studies to identify WIN6.2C binding partners and downstream signaling components

Experiment: RNA-seq analysis during pathogen infection to study WIN6.2C-dependent transcriptional responses

Experiment: Structural biology approaches to understand WIN6.2C protein structure and function

Deep Research

OpenAI

(WIN6.2C-deep-research-openai.md)

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