Poliovirus receptor-related 1

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)
End	119,729,200 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	43,743,955 bp
RNA expression pattern
	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
	; ; ; ;
	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
	5818
	58235
	ENSG00000110400
	ENSMUSG00000032012
	Q15223
	Q9JKF6
	NM_203286; NM_002855; NM_032767; NM_203285
	NM_021424
	NP_002846; NP_976030; NP_976031
	NP_067399
	Wikidata
View/Edit Human	View/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

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]

Interactions

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

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000110400 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000032012 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Entrez Gene: PVRL1 poliovirus receptor-related 1 (herpesvirus entry mediator C; nectin)".
^ 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 (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.

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.

This membrane protein–related article is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000110400 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000032012 – Ensembl, 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.

[entrez-5] "Entrez Gene: PVRL1 poliovirus receptor-related 1 (herpesvirus entry mediator C; nectin)".

[pmid9861033-6] 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.

[pmid10225955-7] 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.

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v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1–50	CD1 a-c 1A 1B 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50
51–100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 - CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100
101–150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150
151–200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200
201–250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249
251–300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299
301–350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD327 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

Poliovirus receptor-related 1

Function

See also

Interactions

References

Further reading

External links