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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)DescriptionActionsGraphical viewLength
Mutagenesisi23D → A: Converts its specificity to [Het-S]; when associated with H-33. 1 Publication1
Mutagenesisi33P → H: Converts its specificity to [Het-S]; when associated with A-23. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004175691 – 289Heterokaryon incompatibility protein sAdd BLAST289

Interactioni

Subunit structurei

Homodimer. Forms heterodimers with het-S.

Protein-protein interaction databases

DIPiDIP-58535N.

Structurei

Secondary structure

1289
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 24Combined sources11
Helixi25 – 27Combined sources3
Beta strandi28 – 31Combined sources4
Helixi32 – 37Combined sources6
Helixi38 – 58Combined sources21
Turni59 – 63Combined sources5
Helixi65 – 68Combined sources4
Beta strandi69 – 71Combined sources3
Helixi75 – 104Combined sources30
Helixi107 – 110Combined sources4
Helixi115 – 117Combined sources3
Helixi120 – 136Combined sources17
Beta strandi148 – 150Combined sources3
Helixi153 – 172Combined sources20
Turni173 – 175Combined sources3
Helixi177 – 187Combined sources11
Helixi194 – 203Combined sources10
Turni204 – 207Combined sources4
Helixi209 – 220Combined sources12
Beta strandi226 – 236Combined sources11
Beta strandi238 – 245Combined sources8
Turni247 – 249Combined sources3
Beta strandi261 – 272Combined sources12
Beta strandi274 – 283Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03689.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 227Globular domainAdd BLAST227
Regioni218 – 289Prion domain (PrD)Add BLAST72

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
PDB 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.
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...

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: November 2, 2016
This is version 61 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.