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Q15223

- PVRL1_HUMAN

UniProt

Q15223 - PVRL1_HUMAN

Protein

Nectin-1

Gene

PVRL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 3 (26 Sep 2001)
      Previous versions | rss
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    Functioni

    Promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between PVRL1/nectin-1 and PVRL3/nectin-3 and between PVRL1/nectin-1 and PVRL4/nectin-4. Functions as an entry receptor for herpes simplex virus and pseudorabies virus. Has some neurite outgrowth-promoting activity.2 Publications

    GO - Molecular functioni

    1. carbohydrate binding Source: Ensembl
    2. cell adhesion molecule binding Source: BHF-UCL
    3. coreceptor activity Source: ProtInc
    4. protein binding Source: IntAct
    5. protein homodimerization activity Source: HGNC
    6. virion binding Source: Ensembl
    7. virus receptor activity Source: UniProtKB-KW

    GO - Biological processi

    1. adherens junction organization Source: Reactome
    2. axon guidance Source: Ensembl
    3. cell adhesion Source: UniProtKB
    4. cell-cell junction organization Source: Reactome
    5. cell junction assembly Source: Reactome
    6. desmosome organization Source: Ensembl
    7. enamel mineralization Source: Ensembl
    8. heterophilic cell-cell adhesion Source: HGNC
    9. homophilic cell adhesion Source: HGNC
    10. immune response Source: UniProtKB
    11. iron ion transport Source: Ensembl
    12. lens morphogenesis in camera-type eye Source: Ensembl
    13. regulation of synapse assembly Source: Ensembl
    14. retina development in camera-type eye Source: Ensembl
    15. signal transduction Source: GOC
    16. single organismal cell-cell adhesion Source: UniProtKB
    17. viral entry into host cell Source: UniProtKB

    Keywords - Molecular functioni

    Host cell receptor for virus entry, Receptor

    Keywords - Biological processi

    Cell adhesion, Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_19195. Adherens junctions interactions.
    REACT_19268. Nectin/Necl trans heterodimerization.

    Protein family/group databases

    MEROPSiI43.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nectin-1
    Alternative name(s):
    Herpes virus entry mediator C
    Short name:
    Herpesvirus entry mediator C
    Short name:
    HveC
    Herpesvirus Ig-like receptor
    Short name:
    HIgR
    Poliovirus receptor-related protein 1
    CD_antigen: CD111
    Gene namesi
    Name:PVRL1
    Synonyms:HVEC, PRR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:9706. PVRL1.

    Subcellular locationi

    GO - Cellular componenti

    1. adherens junction Source: UniProtKB
    2. axon Source: Ensembl
    3. cell-cell adherens junction Source: BHF-UCL
    4. extracellular region Source: UniProtKB-SubCell
    5. growth cone membrane Source: Ensembl
    6. integral component of membrane Source: UniProtKB
    7. intracellular membrane-bounded organelle Source: Ensembl
    8. membrane Source: ProtInc
    9. plasma membrane Source: Reactome
    10. presynaptic membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Secreted, Synapse

    Pathology & Biotechi

    Involvement in diseasei

    Ectodermal dysplasia, Margarita Island type (EDMI) [MIM:225060]: An autosomal recessive form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. It is a syndrome characterized by the association of cleft lip/palate, ectodermal dysplasia (sparse short and dry scalp hair, sparse eyebrows and eyelashes), and partial syndactyly of the fingers and/or toes. Two thirds of the patients do not manifest oral cleft but present with abnormal teeth and nails.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Non-syndromic orofacial cleft 7 (OFC7) [MIM:225060]: A birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi82 – 821N → Y: Impairs interaction with herpes simplex glycoprotein D. Decreases susceptibility to infection by herpes simplex virus. 1 Publication
    Mutagenesisi84 – 841S → Y: Impairs interaction with herpes simplex glycoprotein D. Decreases susceptibility to infection by herpes simplex virus. 1 Publication
    Mutagenesisi129 – 1291F → A or S: Impairs interaction with herpes simplex glycoprotein D. Decreases susceptibility to infection by herpes simplex virus. 1 Publication

    Keywords - Diseasei

    Ectodermal dysplasia

    Organism-specific databases

    MIMi225060. phenotype.
    Orphaneti1991. Cleft lip with or without cleft palate.
    3253. Zlotogora-Ogur syndrome.
    PharmGKBiPA34051.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 517487Nectin-1PRO_0000015133Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi36 – 361N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi51 ↔ 124
    Glycosylationi72 – 721N-linked (GlcNAc...)1 Publication
    Glycosylationi139 – 1391N-linked (GlcNAc...)1 Publication
    Disulfide bondi172 ↔ 226
    Glycosylationi202 – 2021N-linked (GlcNAc...) (complex)4 Publications
    Disulfide bondi269 ↔ 316
    Glycosylationi286 – 2861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi307 – 3071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi332 – 3321N-linked (GlcNAc...)1 Publication
    Modified residuei422 – 4221Phosphoserine1 Publication
    Modified residuei434 – 4341Phosphoserine1 Publication
    Modified residuei435 – 4351PhosphoserineBy similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ15223.
    PaxDbiQ15223.
    PeptideAtlasiQ15223.
    PRIDEiQ15223.

    PTM databases

    PhosphoSiteiQ15223.

    Miscellaneous databases

    PMAP-CutDBQ15223.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15223.
    BgeeiQ15223.
    CleanExiHS_PVRL1.
    GenevestigatoriQ15223.

    Organism-specific databases

    HPAiCAB016135.
    HPA026846.

    Interactioni

    Subunit structurei

    Interacts (via Ig-like C2-type domain 2) with FGFR1, FGFR2 and FGFR3 By similarity. Cis- and trans-homodimer. Can form trans-heterodimers with PVRL3/nectin-3 and with PVRL4/nectin-4. Interaction between PVRL1 and PVRL3 on the pre- and postsynaptic sites, respectively, initiates the formation of puncta adherentia junctions between axons and dendrites. Interacts (via cytoplasmic domain) with MLLT4/afadin (via PDZ domain); this interaction recruits PVRL1 to cadherin-based adherens junctions and provides a connection with the actin cytoskeleton. Interacts with integrin alphaV/beta3. Interacts with herpes simplex virus 1 (HHV-1), herpes simplex virus 2 (HHV-2), and pseudorabies virus (PRV) envelope glycoprotein D; functions as an entry receptor for these viruses.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PVRL3Q9NQS32EBI-1771314,EBI-2826725
    PVRL4Q96NY82EBI-1771314,EBI-4314784

    Protein-protein interaction databases

    BioGridi111776. 5 interactions.
    DIPiDIP-40302N.
    IntActiQ15223. 2 interactions.
    MINTiMINT-90873.
    STRINGi9606.ENSP00000264025.

    Structurei

    Secondary structure

    1
    517
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi37 – 426
    Beta strandi47 – 493
    Beta strandi61 – 7111
    Beta strandi74 – 829
    Turni83 – 853
    Beta strandi86 – 894
    Turni94 – 963
    Beta strandi97 – 1015
    Beta strandi103 – 1064
    Beta strandi109 – 1113
    Helixi116 – 1183
    Beta strandi120 – 12910
    Beta strandi132 – 14413
    Beta strandi147 – 1526
    Beta strandi157 – 1593
    Beta strandi167 – 17913
    Beta strandi182 – 1898
    Beta strandi192 – 1998
    Beta strandi205 – 2139
    Helixi217 – 2193
    Beta strandi223 – 2308
    Beta strandi233 – 2408
    Beta strandi243 – 25210
    Beta strandi265 – 27511
    Beta strandi279 – 2846
    Beta strandi293 – 2964
    Beta strandi299 – 3024
    Helixi308 – 3103
    Beta strandi312 – 3209
    Beta strandi323 – 3319

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ALPX-ray2.80A/B30-335[»]
    3SKUX-ray4.00D/E/F31-345[»]
    3U82X-ray3.16B30-335[»]
    3U83X-ray2.50A30-335[»]
    4FMFX-ray3.20A/B/C/D31-337[»]
    ProteinModelPortaliQ15223.
    SMRiQ15223. Positions 33-335.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15223.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini31 – 355325ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini377 – 517141CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei356 – 37621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 141111Ig-like V-typeAdd
    BLAST
    Domaini149 – 23890Ig-like C2-type 1Add
    BLAST
    Domaini247 – 33488Ig-like C2-type 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni282 – 29918Interaction with FGFRBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi437 – 4448Poly-Glu
    Compositional biasi445 – 4495Poly-Gly

    Domaini

    Ig-like C2-type 2 mediates neurite outgrowth through binding, induction of phosphorylation, and activation of FGFR.By similarity

    Sequence similaritiesi

    Belongs to the nectin family.Curated

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG147558.
    HOGENOMiHOG000115804.
    HOVERGENiHBG100542.
    InParanoidiQ15223.
    KOiK06081.
    OMAiMARMGHA.
    OrthoDBiEOG73RBB5.
    PhylomeDBiQ15223.
    TreeFamiTF331051.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    InterProiIPR013162. CD80_C2-set.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR013106. Ig_V-set.
    IPR003596. Ig_V-set_subgr.
    [Graphical view]
    PfamiPF08205. C2-set_2. 1 hit.
    PF07686. V-set. 1 hit.
    [Graphical view]
    SMARTiSM00409. IG. 1 hit.
    SM00406. IGv. 1 hit.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform Delta (identifier: Q15223-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MARMGLAGAA GRWWGLALGL TAFFLPGVHS QVVQVNDSMY GFIGTDVVLH    50
    CSFANPLPSV KITQVTWQKS TNGSKQNVAI YNPSMGVSVL APYRERVEFL 100
    RPSFTDGTIR LSRLELEDEG VYICEFATFP TGNRESQLNL TVMAKPTNWI 150
    EGTQAVLRAK KGQDDKVLVA TCTSANGKPP SVVSWETRLK GEAEYQEIRN 200
    PNGTVTVISR YRLVPSREAH QQSLACIVNY HMDRFKESLT LNVQYEPEVT 250
    IEGFDGNWYL QRMDVKLTCK ADANPPATEY HWTTLNGSLP KGVEAQNRTL 300
    FFKGPINYSL AGTYICEATN PIGTRSGQVE VNITEFPYTP SPPEHGRRAG 350
    PVPTAIIGGV AGSILLVLIV VGGIVVALRR RRHTFKGDYS TKKHVYGNGY 400
    SKAGIPQHHP PMAQNLQYPD DSDDEKKAGP LGGSSYEEEE EEEEGGGGGE 450
    RKVGGPHPKY DEDAKRPYFT VDEAEARQDG YGDRTLGYQY DPEQLDLAEN 500
    MVSQNDGSFI SKKEWYV 517
    Length:517
    Mass (Da):57,158
    Last modified:September 26, 2001 - v3
    Checksum:iDF34C8AEC893EE6D
    GO
    Isoform Alpha (identifier: Q15223-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         336-458: FPYTPSPPEH...GERKVGGPHP → KPRPQRGLGS...RTTEPRGECP
         459-517: Missing.

    Show »
    Length:458
    Mass (Da):50,721
    Checksum:iAB507515F86D7B45
    GO
    Isoform Gamma (identifier: Q15223-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         335-352: EFPYTPSPPEHGRRAGPV → AFCQLIYPGKGRTRARMF
         353-517: Missing.

    Show »
    Length:352
    Mass (Da):39,150
    Checksum:i2FB60588FA752D99
    GO

    Sequence cautioni

    The sequence CAA53980.2 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei335 – 35218EFPYT…RAGPV → AFCQLIYPGKGRTRARMF in isoform Gamma. 1 PublicationVSP_002624Add
    BLAST
    Alternative sequencei336 – 458123FPYTP…GGPHP → KPRPQRGLGSAARLLAGTVA VFLILVAVLTVFFLYNRQQK SPPETDGAGTDQPLSQKPEP SPSRQSSLVPEDIQVVHLDP GRQQQQEEEDLQKLSLQPPY YDLGVSPSYHPSVRTTEPRG ECP in isoform Alpha. CuratedVSP_002626Add
    BLAST
    Alternative sequencei353 – 517165Missing in isoform Gamma. 1 PublicationVSP_002625Add
    BLAST
    Alternative sequencei459 – 51759Missing in isoform Alpha. CuratedVSP_002627Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76400 mRNA. Translation: CAA53980.2. Different initiation.
    AF060231 mRNA. Translation: AAC23798.1.
    AY029539 mRNA. Translation: AAK33124.1.
    BC104948 mRNA. Translation: AAI04949.1.
    BC113471 mRNA. Translation: AAI13472.1.
    AF252867
    , AF196768, AF196769, AF196770, AF196771 Genomic DNA. Translation: AAG16648.1.
    AF196774
    , AF196768, AF196769, AF196770, AF196771, AF196772, AF196773 Genomic DNA. Translation: AAG16649.1.
    CCDSiCCDS8425.1. [Q15223-2]
    CCDS8426.1. [Q15223-1]
    CCDS8427.1. [Q15223-3]
    PIRiJC4024.
    RefSeqiNP_002846.3. NM_002855.4. [Q15223-1]
    NP_976030.1. NM_203285.1. [Q15223-2]
    NP_976031.1. NM_203286.1. [Q15223-3]
    UniGeneiHs.334846.

    Genome annotation databases

    EnsembliENST00000264025; ENSP00000264025; ENSG00000110400. [Q15223-1]
    ENST00000340882; ENSP00000345289; ENSG00000110400. [Q15223-3]
    ENST00000341398; ENSP00000344974; ENSG00000110400. [Q15223-2]
    GeneIDi5818.
    KEGGihsa:5818.
    UCSCiuc001pwu.1. human. [Q15223-2]
    uc001pwv.3. human. [Q15223-1]
    uc001pww.3. human. [Q15223-3]

    Polymorphism databases

    DMDMi18202503.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76400 mRNA. Translation: CAA53980.2 . Different initiation.
    AF060231 mRNA. Translation: AAC23798.1 .
    AY029539 mRNA. Translation: AAK33124.1 .
    BC104948 mRNA. Translation: AAI04949.1 .
    BC113471 mRNA. Translation: AAI13472.1 .
    AF252867
    , AF196768 , AF196769 , AF196770 , AF196771 Genomic DNA. Translation: AAG16648.1 .
    AF196774
    , AF196768 , AF196769 , AF196770 , AF196771 , AF196772 , AF196773 Genomic DNA. Translation: AAG16649.1 .
    CCDSi CCDS8425.1. [Q15223-2 ]
    CCDS8426.1. [Q15223-1 ]
    CCDS8427.1. [Q15223-3 ]
    PIRi JC4024.
    RefSeqi NP_002846.3. NM_002855.4. [Q15223-1 ]
    NP_976030.1. NM_203285.1. [Q15223-2 ]
    NP_976031.1. NM_203286.1. [Q15223-3 ]
    UniGenei Hs.334846.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ALP X-ray 2.80 A/B 30-335 [» ]
    3SKU X-ray 4.00 D/E/F 31-345 [» ]
    3U82 X-ray 3.16 B 30-335 [» ]
    3U83 X-ray 2.50 A 30-335 [» ]
    4FMF X-ray 3.20 A/B/C/D 31-337 [» ]
    ProteinModelPortali Q15223.
    SMRi Q15223. Positions 33-335.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111776. 5 interactions.
    DIPi DIP-40302N.
    IntActi Q15223. 2 interactions.
    MINTi MINT-90873.
    STRINGi 9606.ENSP00000264025.

    Protein family/group databases

    MEROPSi I43.001.

    PTM databases

    PhosphoSitei Q15223.

    Polymorphism databases

    DMDMi 18202503.

    Proteomic databases

    MaxQBi Q15223.
    PaxDbi Q15223.
    PeptideAtlasi Q15223.
    PRIDEi Q15223.

    Protocols and materials databases

    DNASUi 5818.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264025 ; ENSP00000264025 ; ENSG00000110400 . [Q15223-1 ]
    ENST00000340882 ; ENSP00000345289 ; ENSG00000110400 . [Q15223-3 ]
    ENST00000341398 ; ENSP00000344974 ; ENSG00000110400 . [Q15223-2 ]
    GeneIDi 5818.
    KEGGi hsa:5818.
    UCSCi uc001pwu.1. human. [Q15223-2 ]
    uc001pwv.3. human. [Q15223-1 ]
    uc001pww.3. human. [Q15223-3 ]

    Organism-specific databases

    CTDi 5818.
    GeneCardsi GC11M119542.
    HGNCi HGNC:9706. PVRL1.
    HPAi CAB016135.
    HPA026846.
    MIMi 225060. phenotype.
    600644. gene.
    neXtProti NX_Q15223.
    Orphaneti 1991. Cleft lip with or without cleft palate.
    3253. Zlotogora-Ogur syndrome.
    PharmGKBi PA34051.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG147558.
    HOGENOMi HOG000115804.
    HOVERGENi HBG100542.
    InParanoidi Q15223.
    KOi K06081.
    OMAi MARMGHA.
    OrthoDBi EOG73RBB5.
    PhylomeDBi Q15223.
    TreeFami TF331051.

    Enzyme and pathway databases

    Reactomei REACT_19195. Adherens junctions interactions.
    REACT_19268. Nectin/Necl trans heterodimerization.

    Miscellaneous databases

    ChiTaRSi PVRL1. human.
    EvolutionaryTracei Q15223.
    GeneWikii PVRL1.
    GenomeRNAii 5818.
    NextBioi 22658.
    PMAP-CutDB Q15223.
    PROi Q15223.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15223.
    Bgeei Q15223.
    CleanExi HS_PVRL1.
    Genevestigatori Q15223.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    InterProi IPR013162. CD80_C2-set.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR013106. Ig_V-set.
    IPR003596. Ig_V-set_subgr.
    [Graphical view ]
    Pfami PF08205. C2-set_2. 1 hit.
    PF07686. V-set. 1 hit.
    [Graphical view ]
    SMARTi SM00409. IG. 1 hit.
    SM00406. IGv. 1 hit.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA characterization and chromosomal localization of a gene related to the poliovirus receptor gene."
      Lopez M., Eberle F., Mattei M.-G., Gabert J., Bardin F., Maroc C., Dubreuil P.
      Gene 155:261-265(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA), FUNCTION AS A RECEPTOR FOR HHV-1; HHV-2 AND PRV.
    2. "Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor."
      Geraghty R.J., Krummenacher C., Cohen G.H., Eisenberg R.J., Spear P.G.
      Science 280:1618-1620(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA).
    3. "Novel, soluble isoform of the herpes simplex virus (HSV) receptor nectin1 (or prr1-HIgR-Hvec) modulates positively and negatively susceptibility to hsv infection."
      Lopez M., Cocchi F., Avitabile E., Leclerc A., Adelaide J., Campadelli-Fjume G., Dubreuil P.
      J. Virol. 75:5684-5691(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA).
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DELTA).
      Tissue: Brain.
    5. "Mutations of PVRL1, encoding a cell-cell adhesion molecule/herpesvirus receptor, in cleft lip/palate-ectodermal dysplasia."
      Suzuki K., Hu D., Bustos T., Zlotogora J., Richieri-Costa A., Helms J.A., Spritz R.A.
      Nat. Genet. 25:427-430(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-517 (ISOFORMS ALPHA AND DELTA), DISEASE.
    6. "Herpes simplex virus glycoprotein D can bind to poliovirus receptor-related protein 1 or herpesvirus entry mediator, two structurally unrelated mediators of virus entry."
      Krummenacher C., Nicola A.V., Whitbeck J.C., Lou H., Hou W., Lambris J.D., Geraghty R.J., Spear P.G., Cohen G.H., Eisenberg R.J.
      J. Virol. 72:7064-7074(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HHV-1 AND HHV-2 GLYCOPROTEIN D.
    7. "Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein."
      Takahashi K., Nakanishi H., Miyahara M., Mandai K., Satoh K., Satoh A., Nishioka H., Aoki J., Nomoto A., Mizoguchi A., Takai Y.
      J. Cell Biol. 145:539-549(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AFADIN.
    8. "Nectin4/PRR4, a new afadin-associated member of the nectin family that trans-interacts with nectin1/PRR1 through V domain interaction."
      Reymond N., Fabre S., Lecocq E., Adelaide J., Dubreuil P., Lopez M.
      J. Biol. Chem. 276:43205-43215(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PVRL3 AND PVRL4.
    9. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202.
      Tissue: Plasma.
    10. "Interaction of integrin alpha(v)beta3 with nectin. Implication in cross-talk between cell-matrix and cell-cell junctions."
      Sakamoto Y., Ogita H., Hirota T., Kawakatsu T., Fukuyama T., Yasumi M., Kanzaki N., Ozaki M., Takai Y.
      J. Biol. Chem. 281:19631-19644(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INTEGRIN ITGAV/ITGB3.
    11. Cited for: GLYCOSYLATION AT ASN-202.
    12. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-332.
      Tissue: Leukemic T-cell.
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422 AND SER-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion."
      Zhang N., Yan J., Lu G., Guo Z., Fan Z., Wang J., Shi Y., Qi J., Gao G.F.
      Nat. Commun. 2:577-577(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 30-335 IN COMPLEX WITH HERPES SIMPLEX VIRUS GLYCOPROTEIN D, SUBUNIT, DISULFIDE BONDS.
    16. "Structure of herpes simplex virus glycoprotein D bound to the human receptor nectin-1."
      Di Giovine P., Settembre E.C., Bhargava A.K., Luftig M.A., Lou H., Cohen G.H., Eisenberg R.J., Krummenacher C., Carfi A.
      PLoS Pathog. 7:E1002277-E1002277(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 31-345 IN COMPLEX WITH HERPES SIMPLEX VIRUS GLYCOPROTEIN D, FUNCTION, SUBUNIT, MUTAGENESIS OF ASN-82; SER-84 AND PHE-129, DISULFIDE BONDS, GLYCOSYLATION AT ASN-72; ASN-139 AND ASN-202.
    17. Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 31-337, SUBUNIT, GLYCOSYLATION AT ASN-202, DISULFIDE BONDS, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiPVRL1_HUMAN
    AccessioniPrimary (citable) accession number: Q15223
    Secondary accession number(s): O75465
    , Q2M3D3, Q9HBE6, Q9HBW2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: September 26, 2001
    Last modified: October 1, 2014
    This is version 141 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3