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Poliovirus receptor-related 1

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(Redirected from HveC)

NECTIN1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesNECTIN1, CD111, CLPED1, ED4, HIgR, HV1S, HVEC, OFC7, PRR, PRR1, PVRR, PVRR1, SK-12, nectin-1, PVRL1, nectin cell adhesion molecule 1
External IDsOMIM: 600644; MGI: 1926483; HomoloGene: 2138; GeneCards: NECTIN1; OMA:NECTIN1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_203286
NM_002855
NM_032767
NM_203285

NM_021424

RefSeq (protein)

NP_002846
NP_976030
NP_976031

NP_067399

Location (UCSC)Chr 11: 119.62 – 119.73 MbChr 9: 43.66 – 43.74 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Poliovirus receptor-related 1 (PVRL1), also known as nectin-1 and CD111 (formerly herpesvirus entry mediator C, HVEC) is a human protein of the immunoglobulin superfamily (IgSF), also considered a member of the nectins.[5] 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).

Function

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PVRL1 is an adhesion molecule found in a wide range of tissues where it 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 development as well as in aging brains. 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 players in mediating cellular entry of the Herpes simplex virus by interacting with the viral glycoprotein D (gD).[6]

See also

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Interactions

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PVRL1 has been shown to interact with MLLT4.[7]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000110400Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032012Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Entrez Gene: PVRL1 poliovirus receptor-related 1 (herpesvirus entry mediator C; nectin)".
  6. ^ Cocchi F, Lopez M, Menotti L, Aoubala M, Dubreuil P, Campadelli-Fiume G (1999). "The V domain of herpesvirus Ig-like receptor (HIgR) contains a major functional region in herpes simplex virus-1 entry into cells and interacts physically with the viral glycoprotein D". Proc. Natl. Acad. Sci. U.S.A. 95 (26): 15700–5. doi:10.1073/pnas.95.26.15700. PMC 28107. PMID 9861033.
  7. ^ Takahashi K, Nakanishi H, Miyahara M, Mandai K, Satoh K, Satoh A, Nishioka H, Aoki J, Nomoto A, Mizoguchi A, Takai Y (May 1999). "Nectin/PRR: An Immunoglobulin-like Cell Adhesion Molecule Recruited to Cadherin-based Adherens Junctions through Interaction with Afadin, a PDZ Domain–containing Protein". J. Cell Biol. 145 (3): 539–49. doi:10.1083/jcb.145.3.539. PMC 2185068. PMID 10225955.

Further reading

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