Gene
aqp3b
- ID
- ZDB-GENE-040724-66
- Name
- aquaporin 3b
- Symbol
- aqp3b Nomenclature History
- Previous Names
-
- aqp3l
- si:dkey-83d9.1
- Type
- protein_coding_gene
- Location
- Chr: 21 Mapping Details/Browsers
- Description
- Enables several functions, including arsenite transmembrane transporter activity; glycerol transmembrane transporter activity; and water transmembrane transporter activity. Predicted to be involved in glycerol transmembrane transport and water transport. Predicted to act upstream of or within transmembrane transport. Predicted to be located in membrane. Predicted to be active in basolateral plasma membrane. Is expressed in eye; gill; integument; muscle; and testis. Orthologous to human AQP3 (aquaporin 3 (Gill blood group)).
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- 4 figures from 4 publications
- Cross-Species Comparison
- High Throughput Data
- Thisse Expression Data
- No data available
Wild Type Expression Summary
- All Phenotype Data
- No data available
- Cross-Species Comparison
- Alliance
Phenotype Summary
Mutations
| Allele | Type | Localization | Consequence | Mutagen | Supplier |
|---|---|---|---|---|---|
| la028309Tg | Transgenic insertion | Unknown | Unknown | DNA | |
| sa37266 | Allele with one point mutation | Unknown | Premature Stop | ENU |
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No data available
Human Disease
| Disease Ontology Term | Multi-Species Data | OMIM Term | OMIM Phenotype ID |
|---|---|---|---|
| [Blood group GIL] | 607457 |
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Domain, Family, and Site Summary
Domain Details Per Protein
| Protein | Additional Resources | Length | Aquaporin 3 | Aquaporin-like | Major intrinsic protein | Major Intrinsic Protein/Aquaporin | Major intrinsic protein, conserved site |
|---|---|---|---|---|---|---|---|
| UniProtKB:D3TI80 | InterPro | 299 |
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- Genome Browsers
Interactions and Pathways
No data available
Plasmids
No data available
No data available
| Relationship | Marker Type | Marker | Accession Numbers | Citations |
|---|---|---|---|---|
| Contained in | BAC | DKEY-83D9 | ||
| Contained in | BAC | DKEY-237I15 | ZFIN Curated Data |
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- Vöcking, O., Famulski, J.K. (2023) A temporal single cell transcriptome atlas of zebrafish anterior segment development. Scientific Reports. 13:56565656
- Goudarzi, M., Boquet-Pujadas, A., Olivo-Marin, J.C., Raz, E. (2019) Fluid dynamics during bleb formation in migrating cells in vivo. PLoS One. 14:e0212699
- Qin, Y., Wang, S., Duan, X., Liu, D. (2019) Expression analysis of the aquaporins during zebrafish embryonic development. Gene expression patterns : GEP. 32:38-43
- Eskova, A., Chauvigné, F., Maischein, H.M., Ammelburg, M., Cerdà, J., Nüsslein-Volhard, C., Irion, U. (2017) Gain-of-function mutations of mau/DrAqp3a influence zebrafish pigment pattern formation through the tissue environment. Development (Cambridge, England). 144(11):2059-2069
- Bedford-Guaus, S.J., Chauvigné, F., Mejía-Ramírez, E., Martí, M., Ventura-Rubio, A., Raya, Á., Cerdà, J., Veiga, A. (2016) Expression of the T85A mutant of zebrafish aquaporin 3b improves post-thaw survival of cryopreserved early mammalian embryos. Zygote (Cambridge, England). 24(6):839-847
- Dong, C., Chen, L., Feng, J., Xu, J., Mahboob, S., Al-Ghanim, K., Li, X., Xu, P. (2016) Genome Wide Identification, Phylogeny, and Expression of Aquaporin Genes in Common Carp (Cyprinus carpio). PLoS One. 11:e0166160
- Horng, J.L., Chao, P.L., Chen, P.Y., Shih, T.H., Lin, L.Y. (2015) Aquaporin 1 Is Involved in Acid Secretion by Ionocytes of Zebrafish Embryos through Facilitating CO2 Transport. PLoS One. 10:e0136440
- Varshney, G.K., Lu, J., Gildea, D., Huang, H., Pei, W., Yang, Z., Huang, S.C., Schoenfeld, D.S., Pho, N., Casero, D., Hirase, T., Mosbrook-Davis, D.M., Zhang, S., Jao, L.E., Zhang, B., Woods, I.G., Zimmerman, S., Schier, A.F., Wolfsberg, T., Pellegrini, M., Burgess, S.M., and Lin, S. (2013) A large-scale zebrafish gene knockout resource for the genome-wide study of gene function. Genome research. 23(4):727-735
- Chauvigné, F., Lubzens, E., and Cerdà, J. (2011) Design and characterization of genetically engineered zebrafish aquaporin-3 mutants highly permeable to the cryoprotectant ethylene glycol. BMC Biotechnology. 11:34
- Zapater, C., Chauvigné, F., Norberg, B., Finn, R.N., and Cerdà, J. (2011) Dual neofunctionalization of a rapidly evolving aquaporin-1 paralog resulted in constrained and relaxed traits controlling channel function during meiosis resumption in teleosts. Mol. Biol. Evol.. 28(11):3151-69
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