P25367 · RNQ1_YEAST
- Protein[PIN+] prion protein RNQ1
- GeneRNQ1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids405 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Transferable epigenetic modifier which forms a prion responsible for the non-Mendelian trait [PIN+]. The native function of the soluble protein is unknown.
Miscellaneous
[PIN+], also known as [RNQ+], is the prion form of RNQ1 (PubMed:10678178).
[PIN+] is the result of a conformational change of the cellular RNQ1 protein that becomes self-propagating and infectious. This conformational change generates a form of RNQ1 that assembles into amyloid fibrils (PubMed:17097676).
[PIN+] promotes de novo [PSI+] formation upon SUP35 overproduction (cross-seeding) (PubMed:11511345).
[PIN+] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [PIN+] propagation (PubMed:10678178).
[PIN+] is the result of a conformational change of the cellular RNQ1 protein that becomes self-propagating and infectious. This conformational change generates a form of RNQ1 that assembles into amyloid fibrils (PubMed:17097676).
[PIN+] promotes de novo [PSI+] formation upon SUP35 overproduction (cross-seeding) (PubMed:11511345).
[PIN+] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [PIN+] propagation (PubMed:10678178).
Present with 1140 molecules/cell in log phase SD medium.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | identical protein binding |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name[PIN+] prion protein RNQ1
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP25367
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 166-169 | in strain: SCI7.2/b, SCI11.5/a and SCI11.5/c | ||||
Sequence: Missing | ||||||
Natural variant | 171-172 | in strain: SCI7.2/a, SCI7.2/d, SCI11.5/b and SCI11.5/d | ||||
Sequence: Missing | ||||||
Natural variant | 289-299 | in strain: SCI7.2/b, SCI7.2/d and SCI11.5/c | ||||
Sequence: Missing | ||||||
Natural variant | 293-303 | in strain: SCI9 | ||||
Sequence: Missing | ||||||
Natural variant | 360 | in strain: SCI3, SCI4, SCI7.2/a, SCI7.2/b, SCI7.2/d, SCI11.5/a, SCI11.5/b, SCI11.5/c and SCI11.5/d | ||||
Sequence: Q → H | ||||||
Natural variant | 372 | in strain: SCI7.2/b, SCI7.2/d and SCI11.5/c | ||||
Sequence: P → PQHNGQQQSNEYGRP | ||||||
Natural variant | 383 | in strain: SCI7.2/b,SCI7.2/d and SCI11.5/c | ||||
Sequence: Q → H | ||||||
Natural variant | 387 | in strain: SCI4 | ||||
Sequence: F → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 16 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, cross-link, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000097390 | 1-405 | [PIN+] prion protein RNQ1 | |||
Sequence: MDTDKLISEAESHFSQGNHAEAVAKLTSAAQSNPNDEQMSTIESLIQKIAGYVMDNRSGGSDASQDRAAGGGSSFMNTLMADSKGSSQTQLGKLALLATVMTHSSNKGSSNRGFDVGTVMSMLSGSGGGSQSMGASGLAALASQFFKSGNNSQGQGQGQGQGQGQGQGQGQGSFTALASLASSFMNSNNNNQQGQNQSSGGSSFGALASMASSFMHSNNNQNSNNSQQGYNQSYQNGNQNSQGYNNQQYQGGNGGYQQQQGQSGGAFSSLASMAQSYLGGGQTQSNQQQYNQQGQNNQQQYQQQGQNYQHQQQGQQQQQGHSSSFSALASMASSYLGNNSNSNSSYGGQQQANEYGRPQQNGQQQSNEYGRPQYGGNQNSNGQHESFNFSGNFSQQNNNGNQNRY | ||||||
Cross-link | 5 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 84 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 143 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P25367 | RNQ1 P25367 | 6 | EBI-21708, EBI-21708 | |
BINARY | P25367 | SIS1 P25294 | 3 | EBI-21708, EBI-17244 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 149-172 | Disordered | ||||
Sequence: GNNSQGQGQGQGQGQGQGQGQGQG | ||||||
Region | 153-402 | Prion domain (PrD) | ||||
Sequence: QGQGQGQGQGQGQGQGQGQGSFTALASLASSFMNSNNNNQQGQNQSSGGSSFGALASMASSFMHSNNNQNSNNSQQGYNQSYQNGNQNSQGYNNQQYQGGNGGYQQQQGQSGGAFSSLASMAQSYLGGGQTQSNQQQYNQQGQNNQQQYQQQGQNYQHQQQGQQQQQGHSSSFSALASMASSYLGNNSNSNSSYGGQQQANEYGRPQQNGQQQSNEYGRPQYGGNQNSNGQHESFNFSGNFSQQNNNGNQ | ||||||
Region | 185-405 | Disordered | ||||
Sequence: MNSNNNNQQGQNQSSGGSSFGALASMASSFMHSNNNQNSNNSQQGYNQSYQNGNQNSQGYNNQQYQGGNGGYQQQQGQSGGAFSSLASMAQSYLGGGQTQSNQQQYNQQGQNNQQQYQQQGQNYQHQQQGQQQQQGHSSSFSALASMASSYLGNNSNSNSSYGGQQQANEYGRPQQNGQQQSNEYGRPQYGGNQNSNGQHESFNFSGNFSQQNNNGNQNRY |
Domain
The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is unstructured in its native, soluble form, and which forms a parallel in-register beta-sheet in its amyloid form.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length405
- Mass (Da)42,580
- Last updated2004-04-26 v2
- Checksum8ED9C40A7DF70F7F
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 181 | in Ref. 1; AAA34615 | ||||
Sequence: A → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M16717 EMBL· GenBank· DDBJ | AAA34615.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
X59720 EMBL· GenBank· DDBJ | CAC42958.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY028674 EMBL· GenBank· DDBJ | AAK26208.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY028675 EMBL· GenBank· DDBJ | AAK26209.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY028676 EMBL· GenBank· DDBJ | AAK26210.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY028677 EMBL· GenBank· DDBJ | AAK26211.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY028678 EMBL· GenBank· DDBJ | AAK26212.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY028679 EMBL· GenBank· DDBJ | AAK26213.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY028680 EMBL· GenBank· DDBJ | AAK26214.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY028681 EMBL· GenBank· DDBJ | AAK26215.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY028682 EMBL· GenBank· DDBJ | AAK26216.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY028683 EMBL· GenBank· DDBJ | AAK26217.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY028684 EMBL· GenBank· DDBJ | AAK26218.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY028685 EMBL· GenBank· DDBJ | AAK26219.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006937 EMBL· GenBank· DDBJ | DAA07456.1 EMBL· GenBank· DDBJ | Genomic DNA |