Q3KRC6 · LRC8E_RAT

  • Protein
    Volume-regulated anion channel subunit LRRC8E
  • Gene
    Lrrc8e
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes (PubMed:28833202).
The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine (By similarity).
Mediates efflux of amino acids, such as aspartate, in response to osmotic stress (By similarity).
The VRAC channel also mediates transport of immunoreactive cyclic dinucleotide GMP-AMP (2'-3'-cGAMP), an immune messenger produced in response to DNA virus in the cytosol (By similarity).
Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition (PubMed:28833202).
Also plays a role in lysosome homeostasis by forming functional lysosomal VRAC channels in response to low cytoplasmic ionic strength condition: lysosomal VRAC channels are necessary for the formation of large lysosome-derived vacuoles, which store and then expel excess water to maintain cytosolic water homeostasis (By similarity).

Catalytic activity

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentendoplasmic reticulum membrane
Cellular Componentlysosomal membrane
Cellular Componentmonoatomic ion channel complex
Cellular Componentplasma membrane
Molecular Functionvolume-sensitive anion channel activity
Biological Processaspartate transmembrane transport
Biological Processcell volume homeostasis
Biological Processcellular response to osmotic stress
Biological Processcyclic-GMP-AMP transmembrane import across plasma membrane
Biological Processmonoatomic anion transmembrane transport

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Volume-regulated anion channel subunit LRRC8E
  • Alternative names
    • Leucine-rich repeat-containing protein 8E

Gene names

    • Name
      Lrrc8e

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q3KRC6

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Lysosome membrane
; Multi-pass membrane protein
Endoplasmic reticulum membrane
; Multi-pass membrane protein
Note: In the absence of LRRC8A, resides primarily in the endoplasmic reticulum. Requires LRRC8A for localization at the cell membrane or lysosome membrane.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-22Cytoplasmic
Transmembrane23-43Helical
Topological domain44-116Extracellular
Transmembrane117-137Helical
Topological domain138-264Cytoplasmic
Transmembrane265-285Helical
Topological domain286-312Extracellular
Transmembrane313-333Helical
Topological domain334-795Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for chain, disulfide bond, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00000762521-795Volume-regulated anion channel subunit LRRC8E
Disulfide bond54↔300
Glycosylation63N-linked (GlcNAc...) asparagine
Glycosylation301N-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Heterohexamer (Probable). Oligomerizes with other LRRC8 proteins (LRRC8A, LRRC8C, LRRC8D and/or LRRC8B) to form a heterohexamer (PubMed:28833202).
Detected in a channel complex that contains LRRC8A, LRRC8C and LRRC8E (By similarity).
In vivo, the subunit composition may depend primarily on expression levels, and heterooligomeric channels containing various proportions of the different LRRC8 proteins may coexist (Probable)

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for repeat.

TypeIDPosition(s)Description
Repeat535-556LRR 1
Repeat558-578LRR 2
Repeat582-603LRR 3
Repeat605-626LRR 4
Repeat630-651LRR 5
Repeat653-674LRR 6
Repeat676-697LRR 7
Repeat699-720LRR 8
Repeat722-743LRR 9
Repeat745-766LRR 10

Domain

The volume-regulated anion channel (VRAC) channel forms a trimer of dimers, with symmetry mismatch between the pore-forming domain and the cytosolic LRR repeats, a topology similar to gap junction proteins.

Sequence similarities

Belongs to the LRRC8 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    795
  • Mass (Da)
    90,445
  • Last updated
    2005-11-08 v1
  • Checksum
    17F6795B243632DC
MIPVAEFKQFTEQQPAFKVLKPWWDVLAEYLTVAMLMIGVFGCTLQVTQDKIICLPSHESRENSSEAPCQQLLPQGISEQIGGLRELSGLKNNLDLQQYSFINQLCYETALHWYAKYFPYLVVIHTLIFMVCTSFWFKFPGTSSKIEHFISILGKCFDSPWTTRALSEVSGENHKGPAAGRATVTTVTTVGTGTGKVGEGEKEKVLIEPEKVVTEPPAVTLLDKKEGEQAKALFEKVKKFRVHVEEGDILYSMYIRQTVLKVCKFFAILVYNLVYVEKISFLVACRVETSEITGYASFCCNHTKAHLFSKLAFCYISFVCVYGITCLYTLYWLFHRPLKEYSFRSVREETGMNDIPDVRNDFAFMLHLIDQYDSLYSKRFAVFLSEVSESRLKQLNLNHEWTPDKLRQKLQRNARGRLELSLCMLPGLPDTVFELSEVEALRLEAICDISFPPGLSQLVNLQELSLLHSPARLPFSSQIFLRDRLKVICVKFEELREVPLWVFGLRGLEELHLEGLFPPEMARGATLESLRELKQLKVLSLRSNAGKVPASVTDVAGHLQRLSLHNDGARLLALNSLKKLAVLRELELVACGLERIPHAIFSLGALQELDLKDNHLRSIEEILSFQHCRKLVILRLWHNQIAYVPEHVRKLRSLEQLYLSHNKLETLPAQLGQCFGLRLLDVSHNGLRSLPPELGLLQSLQHLALSYNALESLPDELFFCHKLRTLLLGYNHLTQFSPHVAALQALSRLELKGNRLEALPEELGDCKGLKKSGLLVEDTLYEGLPAEVREKMEEE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BC105779
EMBL· GenBank· DDBJ
AAI05780.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp