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Protein

Heterokaryon incompatibility protein s

Gene

het-s

Organism
Podospora anserina (Pleurage anserina)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Keywords - Molecular functioni

Prion

Protein family/group databases

TCDBi1.C.104.1.1. the heterokaryon incompatibility prion/amyloid protein (het-s) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Heterokaryon incompatibility protein s
Alternative name(s):
Small s protein
Vegetative incompatibility protein s
Gene namesi
Name:het-s
Synonyms:small s
OrganismiPodospora anserina (Pleurage anserina)
Taxonomic identifieri5145 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesLasiosphaeriaceaePodospora

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Amyloid, Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231D → A: Converts its specificity to [Het-S]; when associated with H-33. 1 Publication
Mutagenesisi33 – 331P → H: Converts its specificity to [Het-S]; when associated with A-23. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 289289Heterokaryon incompatibility protein sPRO_0000417569Add
BLAST

Interactioni

Subunit structurei

Homodimer. Forms heterodimers with het-S.

Protein-protein interaction databases

DIPiDIP-58535N.

Structurei

Secondary structure

1
289
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 2411Combined sources
Helixi25 – 273Combined sources
Beta strandi28 – 314Combined sources
Helixi32 – 376Combined sources
Helixi38 – 5821Combined sources
Turni59 – 635Combined sources
Helixi65 – 684Combined sources
Beta strandi69 – 713Combined sources
Helixi75 – 10430Combined sources
Helixi107 – 1104Combined sources
Helixi115 – 1173Combined sources
Helixi120 – 13617Combined sources
Beta strandi148 – 1503Combined sources
Helixi153 – 17220Combined sources
Turni173 – 1753Combined sources
Helixi177 – 18711Combined sources
Helixi194 – 20310Combined sources
Turni204 – 2074Combined sources
Helixi209 – 22012Combined sources
Beta strandi226 – 23611Combined sources
Beta strandi238 – 2458Combined sources
Turni247 – 2493Combined sources
Beta strandi261 – 27212Combined sources
Beta strandi274 – 28310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KJ3NMR-A/B/C218-289[»]
2LBUNMR-A/B/C/D/E218-289[»]
2RNMNMR-A/B/C/D/E218-289[»]
2WVNX-ray2.62A1-227[»]
2WVQX-ray2.00A/B13-221[»]
ProteinModelPortaliQ03689.
SMRiQ03689. Positions 218-289.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03689.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 227227Globular domainAdd
BLAST
Regioni218 – 28972Prion domain (PrD)Add
BLAST

Domaini

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.

Phylogenomic databases

eggNOGiENOG410IZIR. Eukaryota.
ENOG410YM9X. LUCA.

Family and domain databases

InterProiIPR029498. HeLo_dom.
IPR021084. Het-s_prion_dom.
[Graphical view]
PfamiPF14479. HeLo. 1 hit.
PF11558. HET-s_218-289. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03689-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEPFGIVAG ALNVAGLFNN CVDCFEYVQL GRPFGRDYER CQLRLDIAKA
60 70 80 90 100
RLSRWGEAVK INDDPRFHSD APTDKSVQLA KSIVEEILLL FESAQKTSKR
110 120 130 140 150
YELVADQQDL VVFEDKDMKP IGRALHRRLN DLVSRRQKQT SLAKKTAWAL
160 170 180 190 200
YDGKSLEKIV DQVARFVDEL EKAFPIEAVC HKLAEIEIEE VEDEASLTIL
210 220 230 240 250
KDAAGGIDAA MSDAAAQKID AIVGRNSAKD IRTEERARVQ LGNVVTAAAL
260 270 280
HGGIRISDQT TNSVETVVGK GESRVLIGNE YGGKGFWDN
Length:289
Mass (Da):31,978
Last modified:July 5, 2004 - v3
Checksum:iD37468804C3DC793
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38529 Genomic DNA. Translation: AAB94631.1.
PIRiS16556.
S16557.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38529 Genomic DNA. Translation: AAB94631.1.
PIRiS16556.
S16557.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KJ3NMR-A/B/C218-289[»]
2LBUNMR-A/B/C/D/E218-289[»]
2RNMNMR-A/B/C/D/E218-289[»]
2WVNX-ray2.62A1-227[»]
2WVQX-ray2.00A/B13-221[»]
ProteinModelPortaliQ03689.
SMRiQ03689. Positions 218-289.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-58535N.

Protein family/group databases

TCDBi1.C.104.1.1. the heterokaryon incompatibility prion/amyloid protein (het-s) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IZIR. Eukaryota.
ENOG410YM9X. LUCA.

Miscellaneous databases

EvolutionaryTraceiQ03689.

Family and domain databases

InterProiIPR029498. HeLo_dom.
IPR021084. Het-s_prion_dom.
[Graphical view]
PfamiPF14479. HeLo. 1 hit.
PF11558. HET-s_218-289. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Two allelic genes responsible for vegetative incompatibility in the fungus Podospora anserina are not essential for cell viability."
    Turcq B., Deleu C., Denayrolles M., Begueret J.
    Mol. Gen. Genet. 228:265-269(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: s / FGSC 6710.
  2. "A single amino acid difference is sufficient to elicit vegetative incompatibility in the fungus Podospora anserina."
    Deleu C., Clave C., Begueret J.
    Genetics 135:45-52(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF ASP-23 AND PRO-33.
    Strain: A, C, s / FGSC 6710 and V.
  3. "The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog."
    Coustou V., Deleu C., Saupe S., Begueret J.
    Proc. Natl. Acad. Sci. U.S.A. 94:9773-9778(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRION IDENTIFICATION, FUNCTION, INTERACTION WITH HET-S.
  4. Cited for: PRION FORMATION.
  5. "Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina."
    Balguerie A., Dos Reis S., Ritter C., Chaignepain S., Coulary-Salin B., Forge V., Bathany K., Lascu I., Schmitter J.M., Riek R., Saupe S.J.
    EMBO J. 22:2071-2081(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRION FORMATION, DOMAIN.
  6. "The sequences appended to the amyloid core region of the HET-s prion protein determine higher-order aggregate organization in vivo."
    Balguerie A., Dos Reis S., Coulary-Salin B., Chaignepain S., Sabourin M., Schmitter J.M., Saupe S.J.
    J. Cell Sci. 117:2599-2610(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRION FORMATION, DOMAIN.
  7. "Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core."
    Wasmer C., Lange A., Van Melckebeke H., Siemer A.B., Riek R., Meier B.H.
    Science 319:1523-1526(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 218-289.
  8. "Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy."
    Van Melckebeke H., Wasmer C., Lange A., Ab E., Loquet A., Bockmann A., Meier B.H.
    J. Am. Chem. Soc. 132:13765-13775(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 218-289.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 13-221, PRION FORMATION, DOMAIN.
  10. Cited for: STRUCTURE BY NMR OF 218-289.

Entry informationi

Entry nameiHETS_PODAS
AccessioniPrimary (citable) accession number: Q03689
Secondary accession number(s): Q01531
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2012
Last sequence update: July 5, 2004
Last modified: December 9, 2015
This is version 59 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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 cytplasmic element. On vegetative cell fusion with neutral [Het-s*] strains, the prion spreads throuhout 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).2 Publications
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).1 Publication

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.