Q03689 · HETS_PODAS
- ProteinHeterokaryon incompatibility protein s
- Genehet-s
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids289 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Responsible for heterokaryon incompatibility, a process that ensures that during spontaneous, vegetative cell fusion only compatible cells from the same colony survive (non-self-recognition). Forms a prion for the non-Mendelian trait [het-s]. Interacts with het-S from incompatible cells to trigger a lethal reaction that prevents the formation of viable heterokaryons. It is unknown if the native, soluble protein has a cellular function.
Miscellaneous
[Het-s] is the prion form of het-s (PubMed:9275200).
[Het-s] is the result of a conformational change of the cellular het-s protein that becomes self-propagating and infectious. This conformational change generates a form of het-S that assembles into amyloid fibrils (PubMed:12032295).
[Het-s] is transmitted as a non-Mendelian cytoplasmic element. On vegetative cell fusion with neutral [Het-s*] strains, the prion spreads throughout the cellular network and converts the non-prion form of het-s to a prion state, making the strains acquire the [het-s] phenotype (PubMed:9275200).
Interacts with het-S to trigger incompatibility (PubMed:12032295).
The protein present in [Het-s] strains is more resistant to proteinase K than that present in [Het-s*] mycelium (PubMed:9275200).
[Het-s] is the result of a conformational change of the cellular het-s protein that becomes self-propagating and infectious. This conformational change generates a form of het-S that assembles into amyloid fibrils (PubMed:12032295).
[Het-s] is transmitted as a non-Mendelian cytoplasmic element. On vegetative cell fusion with neutral [Het-s*] strains, the prion spreads throughout the cellular network and converts the non-prion form of het-s to a prion state, making the strains acquire the [het-s] phenotype (PubMed:9275200).
Interacts with het-S to trigger incompatibility (PubMed:12032295).
The protein present in [Het-s] strains is more resistant to proteinase K than that present in [Het-s*] mycelium (PubMed:9275200).
In P.anserina, the het-s locus exists as 2 incompatible alleles, het-s and het-S. Strains of het-s genotype (e.g. A, C, s, and V) can display 2 distinct phenoypes, the neutral (prion-free) [Het-s*], which is compatible with het-S strains (e.g. D, S, U, and X), and the reactive [Het-s] phenotype, which causes rapid cell death in het-S strains. Although the two alleles het-s and het-S differ from each other by 14 amino acids, vegetative incompatibility between s and S strains can be attributed to a single amino acid difference in the proteins encoded by the het-s locus (PubMed:8224826).
A sequence for the het-S allele can be found in strain S (AC B2ACC7).
A sequence for the het-S allele can be found in strain S (AC B2ACC7).
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | identical protein binding |
Keywords
- Molecular function
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameHeterokaryon incompatibility protein s
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Sordariomycetidae > Sordariales > Podosporaceae > Podospora
Accessions
- Primary accessionQ03689
- Secondary accessions
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 23 | Converts its specificity to [Het-S]; when associated with H-33. | ||||
Sequence: D → A | ||||||
Mutagenesis | 33 | Converts its specificity to [Het-S]; when associated with A-23. | ||||
Sequence: P → H |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000417569 | 1-289 | Heterokaryon incompatibility protein s | |||
Sequence: MSEPFGIVAGALNVAGLFNNCVDCFEYVQLGRPFGRDYERCQLRLDIAKARLSRWGEAVKINDDPRFHSDAPTDKSVQLAKSIVEEILLLFESAQKTSKRYELVADQQDLVVFEDKDMKPIGRALHRRLNDLVSRRQKQTSLAKKTAWALYDGKSLEKIVDQVARFVDELEKAFPIEAVCHKLAEIEIEEVEDEASLTILKDAAGGIDAAMSDAAAQKIDAIVGRNSAKDIRTEERARVQLGNVVTAAALHGGIRISDQTTNSVETVVGKGESRVLIGNEYGGKGFWDN |
Interaction
Subunit
Homodimer. Forms heterodimers with het-S.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q03689 | het-s Q03689 | 3 | EBI-15800884, EBI-15800884 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-227 | Globular domain | ||||
Sequence: MSEPFGIVAGALNVAGLFNNCVDCFEYVQLGRPFGRDYERCQLRLDIAKARLSRWGEAVKINDDPRFHSDAPTDKSVQLAKSIVEEILLLFESAQKTSKRYELVADQQDLVVFEDKDMKPIGRALHRRLNDLVSRRQKQTSLAKKTAWALYDGKSLEKIVDQVARFVDELEKAFPIEAVCHKLAEIEIEEVEDEASLTILKDAAGGIDAAMSDAAAQKIDAIVGRNS | ||||||
Region | 218-289 | Prion domain (PrD) | ||||
Sequence: KIDAIVGRNSAKDIRTEERARVQLGNVVTAAALHGGIRISDQTTNSVETVVGKGESRVLIGNEYGGKGFWDN |
Domain
The globular domain is dispensable for prion formation and incompatibility function. However, the het-S globular domain, but not the het-s globular domain, is essential for programmed cell death.
The prion domain (PrD) is unstructured in its native, soluble form, and forms a form a beta solenoid with a hydrophobic core in its amyloid form. It is both necessary and sufficient for amyloid formation and prion propagation.
Family and domain databases
Sequence
- Sequence statusComplete
- Length289
- Mass (Da)31,978
- Last updated2004-07-05 v3
- ChecksumD37468804C3DC793
Keywords
- Technical term