Poliovirus receptor-related 1

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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. 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).

NECTIN1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3ALP, 3SKU, 3U83, 4FMF, 4MYW
Identifiers
Aliases	NECTIN1, CD111, CLPED1, ED4, HIgR, HV1S, HVEC, OFC7, PRR, PRR1, PVRR, PVRR1, SK-12, nectin-1, PVRL1, nectin cell adhesion molecule 1
External IDs	OMIM: 600644; MGI: 1926483; HomoloGene: 2138; GeneCards: NECTIN1; OMA:NECTIN1 - orthologs
Gene location (Human) Chr. Chromosome 11 (human) Band 11q23.3 Start 119,623,408 bp End 119,729,200 bp
Gene location (Mouse) Chr. Chromosome 9 (mouse) Band 9|9 A5.1 Start 43,655,281 bp End 43,743,955 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in skin of abdomen skin of leg nipple mucosa of pharynx body of tongue gingival epithelium lateral nuclear group of thalamus subthalamic nucleus vulva external globus pallidus Top expressed in lip neural layer of retina molar dentate gyrus of hippocampal formation granule cell visual cortex epiblast primary visual cortex decidua genital tubercle cerebellar cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein homodimerization activity coreceptor activity virus receptor activity protein binding protein heterodimerization activity virion binding signaling receptor binding carbohydrate binding cell adhesion molecule binding identical protein binding signaling receptor activity Cellular component integral component of membrane membrane intracellular membrane-bounded organelle plasma membrane growth cone membrane synapse integral component of plasma membrane extracellular region axon cell junction neuron projection catenin complex presynaptic membrane apical junction complex cell-cell contact zone cell-cell junction adherens junction dendrite hippocampal mossy fiber to CA3 synapse integral component of presynaptic active zone membrane Biological process heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules cell recognition desmosome organization regulation of synapse assembly axon guidance cell adhesion iron ion transport lens morphogenesis in camera-type eye retina development in camera-type eye immune response viral entry into host cell enamel mineralization viral process adherens junction organization camera-type eye morphogenesis homophilic cell adhesion via plasma membrane adhesion molecules signal transduction protein localization to cell junction cell-cell adhesion virion attachment to host cell Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5818 58235 Ensembl ENSG00000110400 ENSMUSG00000032012 UniProt Q15223 Q9JKF6 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 Mb Chr 9: 43.66 – 43.74 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Function

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).

See also

• Cluster of differentiation

Interactions

PVRL1 has been shown to interact with MLLT4.

Further reading

• Bustos T, Simosa V, Pinto-Cisternas J, Abramovits W, Jolay L, Rodriguez L, Fernandez L, Ramela M (1992). "Autosomal recessive ectodermal dysplasia: I. An undescribed dysplasia/malformation syndrome". Am. J. Med. Genet. 41 (4): 398–404. doi:10.1002/ajmg.1320410403. PMID 1776626.
• Lopez M, Eberlé F, Mattei MG, Gabert J, Birg F, Bardin F, Maroc C, Dubreuil P (1995). "Complementary DNA characterization and chromosomal localization of a human gene related to the poliovirus receptor-encoding gene". Gene. 155 (2): 261–5. doi:10.1016/0378-1119(94)00842-G. PMID 7721102.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Geraghty RJ, Krummenacher C, Cohen GH, Eisenberg RJ, Spear PG (1998). "Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor". Science. 280 (5369): 1618–20. Bibcode:1998Sci...280.1618G. doi:10.1126/science.280.5369.1618. PMID 9616127.
• Suzuki K, Bustos T, Spritz RA (1998). "Linkage disequilibrium mapping of the gene for Margarita Island ectodermal dysplasia (ED4) to 11q23". Am. J. Hum. Genet. 63 (4): 1102–7. doi:10.1086/302072. PMC 1377504. PMID 9758630.
• Cocchi F, Menotti L, Mirandola P, Lopez M, Campadelli-Fiume G (1998). "The Ectodomain of a Novel Member of the Immunoglobulin Subfamily Related to the Poliovirus Receptor Has the Attributes of a Bona Fide Receptor for Herpes Simplex Virus Types 1 and 2 in Human Cells". J. Virol. 72 (12): 9992–10002. doi:10.1128/JVI.72.12.9992-10002.1998. PMC 110516. PMID 9811737.
• 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.
• Takahashi K, Nakanishi H, Miyahara M, Mandai K, Satoh K, Satoh A, Nishioka H, Aoki J, Nomoto A, Mizoguchi A, Takai Y (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.
• Miyahara M, Nakanishi H, Takahashi K, Satoh-Horikawa K, Tachibana K, Takai Y (2000). "Interaction of nectin with afadin is necessary for its clustering at cell–cell contact sites but not for its cis dimerization or trans interaction". J. Biol. Chem. 275 (1): 613–8. doi:10.1074/jbc.275.1.613. PMID 10617658.
• Suzuki K, Hu D, Bustos T, Zlotogora J, Richieri-Costa A, Helms JA, Spritz RA (2000). "Mutations of PVRL1, encoding a cell–cell adhesion molecule/herpesvirus receptor, in cleft lip/palate-ectodermal dysplasia". Nat. Genet. 25 (4): 427–30. doi:10.1038/78119. PMID 10932188. S2CID 6169893.
• Lopez M, Cocchi F, Avitabile E, Leclerc A, Adelaide J, Campadelli-Fiume G, Dubreuil P (2001). "Novel, Soluble Isoform of the Herpes Simplex Virus (HSV) Receptor Nectin1 (or PRR1-HIgR-HveC) Modulates Positively and Negatively Susceptibility to HSV Infection". J. Virol. 75 (12): 5684–91. doi:10.1128/JVI.75.12.5684-5691.2001. PMC 114282. PMID 11356977.
• Sözen MA, Suzuki K, Tolarova MM, Bustos T, Fernández Iglesias JE, Spritz RA (2001). "Mutation of PVRL1 is associated with sporadic, non-syndromic cleft lip/palate in northern Venezuela". Nat. Genet. 29 (2): 141–2. doi:10.1038/ng740. PMID 11559849. S2CID 8641206.
• Struyf F, Posavad CM, Keyaerts E, Van Ranst M, Corey L, Spear PG (2002). "Search for polymorphisms in the genes for herpesvirus entry mediator, nectin-1, and nectin-2 in immune seronegative individuals". J. Infect. Dis. 185 (1): 36–44. doi:10.1086/338116. PMID 11756979.
• Fabre S, Reymond N, Cocchi F, Menotti L, Dubreuil P, Campadelli-Fiume G, Lopez M (2002). "Prominent role of the Ig-like V domain in trans-interactions of nectins. Nectin3 and nectin 4 bind to the predicted C-C'-C"-D beta-strands of the nectin1 V domain". J. Biol. Chem. 277 (30): 27006–13. doi:10.1074/jbc.M203228200. PMID 12011057.
• Yoon M, Spear PG (2002). "Disruption of Adherens Junctions Liberates Nectin-1 To Serve as Receptor for Herpes Simplex Virus and Pseudorabies Virus Entry". J. Virol. 76 (14): 7203–8. doi:10.1128/JVI.76.14.7203-7208.2002. PMC 136315. PMID 12072519.
• Struyf F, Martinez WM, Spear PG (2002). "Mutations in the N-Terminal Domains of Nectin-1 and Nectin-2 Reveal Differences in Requirements for Entry of Various Alphaherpesviruses and for Nectin-Nectin Interactions". J. Virol. 76 (24): 12940–50. doi:10.1128/JVI.76.24.12940-12950.2002. PMC 136698. PMID 12438620.
• Takekuni K, Ikeda W, Fujito T, Morimoto K, Takeuchi M, Monden M, Takai Y (2003). "Direct binding of cell polarity protein PAR-3 to cell–cell adhesion molecule nectin at neuroepithelial cells of developing mouse". J. Biol. Chem. 278 (8): 5497–500. doi:10.1074/jbc.C200707200. PMID 12515806.
• Krummenacher C, Baribaud I, Eisenberg RJ, Cohen GH (2003). "Cellular Localization of Nectin-1 and Glycoprotein D during Herpes Simplex Virus Infection". J. Virol. 77 (16): 8985–99. doi:10.1128/JVI.77.16.8985-8999.2003. PMC 167240. PMID 12885915.
• Bender FC, Whitbeck JC, Ponce de Leon M, Lou H, Eisenberg RJ, Cohen GH (2003). "Specific Association of Glycoprotein B with Lipid Rafts during Herpes Simplex Virus Entry". J. Virol. 77 (17): 9542–52. doi:10.1128/JVI.77.17.9542-9552.2003. PMC 187402. PMID 12915568.

External links

• PVRL1+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

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