Gene
prnpb
- ID
- ZDB-GENE-041221-2
- Name
- prion protein b
- Symbol
- prnpb Nomenclature History
- Previous Names
- Type
- protein_coding_gene
- Location
- Chr: 10 Mapping Details/Browsers
- Description
- Predicted to enable calcium-dependent phospholipid binding activity and phosphatidylserine binding activity. Acts upstream of or within several processes, including calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; epiboly involved in gastrulation with mouth forming second; and homophilic cell adhesion via plasma membrane adhesion molecules. Located in cell surface and plasma membrane. Is expressed in cranial ganglion; eye; floor plate; and forebrain.
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- 4 figures from 3 publications
- Cross-Species Comparison
- High Throughput Data
- Thisse Expression Data
- No data available
Wild Type Expression Summary
- All Phenotype Data
- 14 figures from 5 publications
- Cross-Species Comparison
- Alliance
Phenotype Summary
Mutations
| Targeting Reagent | Created Alleles | Citations |
|---|---|---|
| CRISPR1-prnpb | Zebrafish Nomenclature Committee | |
| MO1-prnpb | N/A | (4) |
| MO2-prnpb | N/A | (2) |
| TALEN1-prnpb | (4) |
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Human Disease
Domain, Family, and Site Summary
| Type | InterPro ID | Name |
|---|---|---|
| Homologous_superfamily | IPR036924 | Prion/Doppel beta-ribbon domain superfamily |
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Domain Details Per Protein
| Protein | Additional Resources | Length | Prion/Doppel beta-ribbon domain superfamily |
|---|---|---|---|
| UniProtKB:Q3BDW0 | InterPro | 606 |
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Interactions and Pathways
No data available
| Name | Type | Antigen Genes | Isotype | Host Organism | Assay | Source | Citations |
|---|---|---|---|---|---|---|---|
| Ab1-prnp | monoclonal | IgG1 , k | Mouse |
|
Prionics AG
|
3 |
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Plasmids
No data available
No data available
| Relationship | Marker Type | Marker | Accession Numbers | Citations |
|---|---|---|---|---|
| Contained in | BAC | DKEY-81J8 | ZFIN Curated Data | |
| Encodes | cDNA | MGC:123004 | ZFIN Curated Data |
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| Type | Accession # | Sequence | Length (nt/aa) | Analysis |
|---|---|---|---|---|
| RNA | RefSeq:NM_001013297 (1) | 2399 nt | ||
| Genomic | GenBank:BX640477 (1) | 258048 nt | ||
| Polypeptide | UniProtKB:Q3BDW0 (1) | 606 aa |
- Zebrafish Nomenclature Committee (2024) Nomenclature Data Curation (2024). Nomenclature Committee Submission.
- Pollock, N.M., Leighton, P., Neil, G., Allison, W.T. (2021) Transcriptomic analysis of zebrafish prion protein mutants supports conserved cross-species function of the cellular prion protein. Prion. 15:70-81
- Kanyo, R., Leighton, P.L.A., Neil, G.J., Locskai, L.F., Allison, W.T. (2020) Amyloid-β precursor protein mutant zebrafish exhibit seizure susceptibility that depends on prion protein. Experimental neurology. 328:113283
- Özcan, G.G., Lim, S., Leighton, P., Allison, W.T., Rihel, J. (2020) Sleep is bi-directionally modified by amyloid beta oligomers. eLIFE. 9:
- Leighton, P.L.A., Kanyo, R., Neil, G.J., Pollock, N.M., Allison, W.T. (2018) Prion gene paralogs are dispensable for early zebrafish development but have non-additive roles in seizure susceptibility. The Journal of biological chemistry. 293(32):12576-12592
- Sempou, E., Biasini, E., Pinzón-Olejua, A., Harris, D.A., Málaga-Trillo, E. (2016) Activation of zebrafish Src family kinases by the prion protein is an amyloid-β-sensitive signal that prevents the endocytosis and degradation of E-cadherin/β-catenin complexes in vivo. Molecular neurodegeneration. 11:18
- Halliez, S., Passet, B., Martin-Lannerée, S., Hernandez-Rapp, J., Laude, H., Mouillet-Richard, S., Vilotte, J.L., Béringue, V. (2014) To develop with or without the prion protein. Frontiers in cell and developmental biology. 2:58
- Fleisch, V.C., Leighton, P.L., Wang, H., Pillay, L.M., Ritzel, R.G., Bhinder, G., Roy, B., Tierney, K.B., Ali, D.W., Waskiewicz, A.J., and Allison, W.T. (2013) Targeted Mutation of the Gene Encoding Prion Protein in Zebrafish reveals a Conserved Role in Neuron Excitability. Neurobiology of disease. 55:11-25
- Solis, G.P., Radon, Y., Sempou, E., Jechow, K., Stuermer, C.A., and Málaga-Trillo, E. (2013) Conserved roles of the prion protein domains on subcellular localization and cell-cell adhesion. PLoS One. 8(7):e70327
- Kaiser, D.M., Acharya, M., Leighton, P.L., Wang, H., Daude, N., Wohlgemuth, S., Shi, B., and Allison, W.T. (2012) Amyloid Beta precursor protein and prion protein have a conserved interaction affecting cell adhesion and CNS development. PLoS One. 7(12):e51305
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