PVRL1

From Wikipedia, the free encyclopedia
Poliovirus receptor-related 1 (herpesvirus entry mediator C)
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsPVRL1; CD111; CLPED1; ED4; HIgR; HVEC; OFC7; PRR; PRR1; PVRR; PVRR1; SK-12; nectin-1
External IDsOMIM: 600644 MGI: 1926483 HomoloGene: 2138 GeneCards: PVRL1 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez581858235
EnsemblENSG00000110400ENSMUSG00000032012
UniProtQ15223Q9JKF6
RefSeq (mRNA)NM_002855NM_021424
RefSeq (protein)NP_002846NP_067399
Location (UCSC)Chr 11:
119.49 – 119.6 Mb
Chr 9:
43.74 – 43.81 Mb
PubMed search

Poliovirus receptor-related 1 (herpesvirus entry mediator C; nectin-1; CD111), also known as PVRL1, is a human gene that encodes a protein of immunoglobulin superfamily (IgSF) also considered a member of the nectins.[1] It is a membrane protein with three extracellular immunoglobulin domains, a single transmembrane helix and a cytoplasmic tail. The protein can mediate Ca2+-independent cellular adhesion further characterizing it as IgSF cell adhesion molecule (IgSF CAM).

PVRL1 is adhesion molecule found in a wide range of tissues where is localizes in various junctions such as the adherens junction of epithelial tissue or the chemical synapse of neurons. The cytoplasmic tail of PVRL1 can bind the protein afadin which is a scaffolding protein that binds actin.

In the chemical synapse PVRL1 interacts with PVRL3 (nectin-3) and both proteins can be found in neuronal tissue already in early stages of brain developmen as well as in aging brains. Inerestingly the two proteins have been found to localize asymmetrically along the chemical synapse, with PVRL1 primarily on the axonal side and PVRL3 on the dendritic side.

The protein has been revealed as one of the key playerse in mediating cellular entry of the Herpes simplex virus by interacting with the viral glycoprotein D (gD).[2]

See also

Interactions

PVRL1 has been shown to interact with MLLT4.[3]

References

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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