Aqp6 aquaporin 6 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Aqp6provided by RGD
Official Full Name: aquaporin 6provided by RGD
Primary source: RGD:71100
See related: EnsemblRapid:ENSRNOG00000063448 AllianceGenome:RGD:71100
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Summary: Enables carbon dioxide transmembrane transporter activity; channel activity; and nitrate transmembrane transporter activity. Involved in nitrate transmembrane transport. Located in cytoplasmic vesicle membrane. Orthologous to human AQP6 (aquaporin 6). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Restricted expression toward (RPKM 99.8) See more
Orthologs: human mouse all
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Genomic context

Location:: 7q36

Exon count:: 4

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	7	NC_086025.1 (132611069..132614004)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	7	NC_051342.1 (130732216..130735149)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	7	NC_005106.4 (141258585..141261518)

Chromosome 7 - NC_086025.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
BioProject: PRJNA238328
Publication: PMID 24510058
Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

A region within the third extracellular loop of rat Aquaporin 6 precludes trafficking to plasma membrane in a heterologous cell line.
Title: A region within the third extracellular loop of rat Aquaporin 6 precludes trafficking to plasma membrane in a heterologous cell line.
confirmed AQP6 expression in retinal ganglion cells and Muller cells in vitro
Title: Expression of Aquaporin-6 in Rat Retinal Ganglion Cells.
AQP6 is involved in osmoregulation to maintain both the acid-base and osmotic balance of parotid secretory granules.
Title: Involvement of AQP6 in the Mercury-sensitive osmotic lysis of rat parotid secretory granules.
AQP6 labeling of the outer plexiform layer was decreased in retinal slices from diabetic rats in comparison to slices from control rats.
Title: Expression of aquaporins in the retina of diabetic rats.
Aquaporin 6 is localized in glial membranes that surround the ribbon synapses in the outer plexiform layer of retina.
Title: Immunolocalization of aquaporin-6 in the rat retina.
aquaporin-6 is distributed throughout the gastrointestinal tract. Its localization at the apical pole of superficial epithelial cells and its upregulation by feeding suggest it may be involved in movements of water and anions through villi epithelium.
Title: Aquaporin-6 is expressed along the rat gastrointestinal tract and upregulated by feeding in the small intestine.
The results suggest that AQP6 participates in water and anion transport in plasma membranes near tight junctions and in secretory granule membranes in rat parotid acinar cells.
Title: Presence and localization of aquaporin-6 in rat parotid acinar cells.
Data show that a single residue substitution totally eliminates the anion permeability of aquaporin 6 when expressed in Xenopus oocytes, but these oocytes exhibit significantly higher osmotic water permeability under basal conditions.
Title: Conversion of aquaporin 6 from an anion channel to a water-selective channel by a single amino acid substitution.
the primary role of AQP6 may be in cellular regulation
Title: Characterization of aquaporin-6 as a nitrate channel in mammalian cells. Requirement of pore-lining residue threonine 63.
AQP1 and AQP6, and the heterotrimeric Go protein are associated with SVs and participate in their swelling
Title: Involvement of water channels in synaptic vesicle swelling.

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General gene information

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Markers

Aqp6 (e-PCR), detects polymorphism
- UniSTS:186495

Aqp6 (e-PCR), detects polymorphism
- UniSTS:209567

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables ammonium channel activity	IDA Inferred from Direct Assay more info	PubMed
enables carbon dioxide transmembrane transporter activity	IDA Inferred from Direct Assay more info	PubMed
enables channel activity	IEA Inferred from Electronic Annotation more info
enables monoatomic anion channel activity	IDA Inferred from Direct Assay more info	PubMed
enables monoatomic anion channel activity	TAS Traceable Author Statement more info
enables nitrate transmembrane transporter activity	IBA Inferred from Biological aspect of Ancestor more info
enables nitrate transmembrane transporter activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables pH-gated chloride channel activity	IDA Inferred from Direct Assay more info	PubMed
enables water channel activity	IBA Inferred from Biological aspect of Ancestor more info
NOT enables water channel activity	IDA Inferred from Direct Assay more info	PubMed
enables water channel activity	IDA Inferred from Direct Assay more info	PubMed
enables water channel activity	ISO Inferred from Sequence Orthology more info
enables water channel activity	ISS Inferred from Sequence or Structural Similarity more info

Process	Evidence Code	Pubs
involved_in ammonium transmembrane transport	IEA Inferred from Electronic Annotation more info
involved_in carbon dioxide transmembrane transport	IEA Inferred from Electronic Annotation more info
involved_in carbon dioxide transport	IBA Inferred from Biological aspect of Ancestor more info
involved_in chloride transmembrane transport	IEA Inferred from Electronic Annotation more info
involved_in nitrate transmembrane transport	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in odontogenesis	ISO Inferred from Sequence Orthology more info
involved_in renal water transport	ISO Inferred from Sequence Orthology more info
involved_in renal water transport	ISS Inferred from Sequence or Structural Similarity more info
involved_in transmembrane transport	IEA Inferred from Electronic Annotation more info
involved_in water transport	IBA Inferred from Biological aspect of Ancestor more info

Component	Evidence Code	Pubs
is_active_in apical plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasmic vesicle membrane	IDA Inferred from Direct Assay more info	PubMed
located_in membrane	IEA Inferred from Electronic Annotation more info
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in transport vesicle membrane	TAS Traceable Author Statement more info

General protein information

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Preferred Names: aquaporin-6

Names: AQP-6; aquaporin 6, kidney specific

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_022181.2 → NP_071517.1 aquaporin-6

See identical proteins and their annotated locations for NP_071517.1

Status: PROVISIONAL

Source sequence(s)

JAXUCZ010000007

UniProtKB/Swiss-Prot

Q9WTY0

UniProtKB/TrEMBL

A0A8I6AGD2, A6KCG3

Related

ENSRNOP00000092300.1, ENSRNOT00000098480.3

Conserved Domains (1) summary

cl00200
Location:22 → 228

MIP; Major intrinsic protein (MIP) superfamily. Members of the MIP superfamily function as membrane channels that selectively transport water, small neutral molecules, and ions out of and between cells. The channel proteins share a common fold: the N-terminal ...