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P15151

- PVR_HUMAN

UniProt

P15151 - PVR_HUMAN

Protein

Poliovirus receptor

Gene

PVR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Mediates NK cell adhesion and triggers NK cell effector functions. Binds two different NK cell receptors: CD96 and CD226. These interactions accumulates at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytoxicity of activated NK cells. May also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Plays a role in mediating tumor cell invasion and migration. Serves as a receptor for poliovirus attachment to target cells. May play a role in axonal transport of poliovirus, by targeting virion-PVR-containing endocytic vesicles to the microtubular network through interaction with DYNLT1. This interaction would drive the virus-containing vesicle to the axonal retrograde transport.2 Publications

    Kineticsi

    1. KM=72 nM for VTN

    GO - Molecular functioni

    1. cell adhesion molecule binding Source: BHF-UCL
    2. protein binding Source: UniProtKB
    3. receptor activity Source: ProtInc
    4. virus receptor activity Source: Ensembl

    GO - Biological processi

    1. adherens junction organization Source: Reactome
    2. cell-cell junction organization Source: Reactome
    3. cell junction assembly Source: Reactome
    4. cell migration Source: Ensembl
    5. positive regulation of natural killer cell mediated cytotoxicity Source: BHF-UCL
    6. positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target Source: BHF-UCL
    7. regulation of immune response Source: Reactome
    8. single organismal cell-cell adhesion Source: Ensembl
    9. susceptibility to natural killer cell mediated cytotoxicity Source: BHF-UCL
    10. susceptibility to T cell mediated cytotoxicity Source: BHF-UCL
    11. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Cell adhesion, Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_19268. Nectin/Necl trans heterodimerization.

    Protein family/group databases

    MEROPSiI43.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Poliovirus receptor
    Alternative name(s):
    Nectin-like protein 5
    Short name:
    NECL-5
    CD_antigen: CD155
    Gene namesi
    Name:PVR
    Synonyms:PVS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9705. PVR.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: BHF-UCL
    2. cytoplasm Source: ProtInc
    3. extracellular space Source: ProtInc
    4. extracellular vesicular exosome Source: UniProt
    5. integral component of membrane Source: BHF-UCL
    6. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi369 – 3724KCSR → ACSA: Partial loss of DYNLT1 binding. 2 Publications

    Organism-specific databases

    MIMi173850. gene+phenotype.
    PharmGKBiPA34050.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 417397Poliovirus receptorPRO_0000015131Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi49 ↔ 1231 PublicationPROSITE-ProRule annotation
    Glycosylationi105 – 1051N-linked (GlcNAc...)
    Glycosylationi120 – 1201N-linked (GlcNAc...) (complex)1 Publication
    Disulfide bondi166 ↔ 221PROSITE-ProRule annotation
    Glycosylationi188 – 1881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi218 – 2181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi237 – 2371N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi266 ↔ 312PROSITE-ProRule annotation
    Glycosylationi278 – 2781N-linked (GlcNAc...)1 Publication
    Glycosylationi307 – 3071N-linked (GlcNAc...)1 Publication
    Glycosylationi313 – 3131N-linked (GlcNAc...)Sequence Analysis
    Modified residuei398 – 3981Phosphotyrosine2 Publications

    Post-translational modificationi

    N-glycosylated. N-glycan at Asn-120: Hex5HexNAc4.3 Publications
    Phosphorylated by Src kinases on tyrosine residues in the ITIM motif upon ligation. Interaction with TIGIT is required for Phosphorylation.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP15151.
    PaxDbiP15151.
    PRIDEiP15151.

    PTM databases

    PhosphoSiteiP15151.

    Expressioni

    Inductioni

    Transcriptionally regulated by SHH.1 Publication

    Gene expression databases

    ArrayExpressiP15151.
    BgeeiP15151.
    CleanExiHS_PVR.
    GenevestigatoriP15151.

    Organism-specific databases

    HPAiHPA012568.

    Interactioni

    Subunit structurei

    Can form trans-heterodimers with PVRL3/nectin-3. The extracellular domain interacts with VTN, CD226 and CD96. The cytoplasmic domain interacts with DYNLT1. Interacts with HHV-5 UL141. Interacts with poliovirus capsid composed of VP1, VP2 and VP3, mainly through VP3. Binds with high affinity to TIGIT.10 Publications

    Protein-protein interaction databases

    BioGridi111775. 13 interactions.
    DIPiDIP-43987N.
    IntActiP15151. 7 interactions.
    MINTiMINT-5224421.
    STRINGi9606.ENSP00000402060.

    Structurei

    Secondary structure

    1
    417
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi30 – 323
    Beta strandi35 – 406
    Beta strandi45 – 473
    Beta strandi50 – 523
    Beta strandi60 – 689
    Beta strandi75 – 795
    Turni80 – 823
    Beta strandi83 – 864
    Beta strandi90 – 945
    Beta strandi108 – 1103
    Helixi115 – 1173
    Beta strandi119 – 12810
    Beta strandi131 – 14212

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DGIelectron microscopy22.00R28-329[»]
    1NN8electron microscopy15.00R/S/T28-329[»]
    3EPCelectron microscopy8.00R30-242[»]
    3EPDelectron microscopy9.00R30-242[»]
    3EPFelectron microscopy9.00R30-242[»]
    3UDWX-ray2.90C/D28-145[»]
    3UROX-ray3.50R29-243[»]
    4FQPX-ray3.60A28-334[»]
    ProteinModelPortaliP15151.
    SMRiP15151. Positions 28-333.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15151.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 343323ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini368 – 41750CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei344 – 36724HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 139116Ig-like V-typeAdd
    BLAST
    Domaini145 – 23793Ig-like C2-type 1Add
    BLAST
    Domaini244 – 32885Ig-like C2-type 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni368 – 3725DYNLT1 binding

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi396 – 4016ITIM motif

    Domaini

    Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases.1 Publication

    Sequence similaritiesi

    Belongs to the nectin family.Curated

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG147224.
    HOGENOMiHOG000237277.
    HOVERGENiHBG019169.
    InParanoidiP15151.
    KOiK06539.
    OMAiGPPSEHS.
    OrthoDBiEOG7D59N6.
    PhylomeDBiP15151.
    TreeFamiTF331051.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    InterProiIPR013162. CD80_C2-set.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013106. Ig_V-set.
    IPR003596. Ig_V-set_subgr.
    IPR013151. Immunoglobulin.
    [Graphical view]
    PfamiPF08205. C2-set_2. 1 hit.
    PF00047. ig. 1 hit.
    PF07686. V-set. 1 hit.
    [Graphical view]
    SMARTiSM00406. IGv. 1 hit.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 3 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform Alpha (identifier: P15151-1) [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

    MARAMAAAWP LLLVALLVLS WPPPGTGDVV VQAPTQVPGF LGDSVTLPCY    50
    LQVPNMEVTH VSQLTWARHG ESGSMAVFHQ TQGPSYSESK RLEFVAARLG 100
    AELRNASLRM FGLRVEDEGN YTCLFVTFPQ GSRSVDIWLR VLAKPQNTAE 150
    VQKVQLTGEP VPMARCVSTG GRPPAQITWH SDLGGMPNTS QVPGFLSGTV 200
    TVTSLWILVP SSQVDGKNVT CKVEHESFEK PQLLTVNLTV YYPPEVSISG 250
    YDNNWYLGQN EATLTCDARS NPEPTGYNWS TTMGPLPPFA VAQGAQLLIR 300
    PVDKPINTTL ICNVTNALGA RQAELTVQVK EGPPSEHSGI SRNAIIFLVL 350
    GILVFLILLG IGIYFYWSKC SREVLWHCHL CPSSTEHASA SANGHVSYSA 400
    VSRENSSSQD PQTEGTR 417
    Length:417
    Mass (Da):45,303
    Last modified:February 1, 1996 - v2
    Checksum:iD15C012CE853169B
    GO
    Isoform Beta (identifier: P15151-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         340-384: Missing.

    Note: Glycosylated on Asn-360.

    Show »
    Length:372
    Mass (Da):40,125
    Checksum:i7B56B38F949996BE
    GO
    Isoform Gamma (identifier: P15151-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         331-331: E → G
         332-384: Missing.

    Note: Glycosylated on Asn-352.

    Show »
    Length:364
    Mass (Da):39,304
    Checksum:iF63D1B6CF19F2A6F
    GO
    Isoform Delta (identifier: P15151-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         385-392: TEHASASA → EHHQSCRN
         393-417: Missing.

    Show »
    Length:392
    Mass (Da):42,864
    Checksum:i528DFC93B73C7FD8
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti67 – 671A → T.
    Corresponds to variant rs1058402 [ dbSNP | Ensembl ].
    VAR_003952
    Natural varianti295 – 2951A → T.
    Corresponds to variant rs35365841 [ dbSNP | Ensembl ].
    VAR_049994
    Natural varianti340 – 3401I → M.1 Publication
    Corresponds to variant rs203710 [ dbSNP | Ensembl ].
    VAR_011736

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei331 – 3311E → G in isoform Gamma. CuratedVSP_002618
    Alternative sequencei332 – 38453Missing in isoform Gamma. CuratedVSP_002619Add
    BLAST
    Alternative sequencei340 – 38445Missing in isoform Beta. 1 PublicationVSP_002617Add
    BLAST
    Alternative sequencei385 – 3928TEHASASA → EHHQSCRN in isoform Delta. CuratedVSP_002620
    Alternative sequencei393 – 41725Missing in isoform Delta. CuratedVSP_002621Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24407 mRNA. Translation: AAA36461.1.
    M24406 mRNA. Translation: AAA36462.1.
    X64116
    , X64117, X64118, X64119, X64120, X64121, X64122, X64123 Genomic DNA. Translation: CAA45478.1.
    X64116
    , X64117, X64118, X64119, X64120, X64121, X64122, X64123 Genomic DNA. Translation: CAA45479.1.
    X64116
    , X64117, X64118, X64119, X64120, X64122, X64123 Genomic DNA. Translation: CAA45480.1.
    AK300349 mRNA. Translation: BAG62091.1.
    AC068948 Genomic DNA. Translation: AAF69803.1.
    BC015542 mRNA. Translation: AAH15542.1.
    CCDSiCCDS12640.1. [P15151-1]
    CCDS46105.1. [P15151-2]
    CCDS46106.1. [P15151-3]
    CCDS46107.1. [P15151-4]
    PIRiA43024. RWHUPD.
    S12048. RWHUPA.
    RefSeqiNP_001129240.1. NM_001135768.2. [P15151-2]
    NP_001129241.1. NM_001135769.2. [P15151-3]
    NP_001129242.2. NM_001135770.3.
    NP_006496.4. NM_006505.4.
    UniGeneiHs.171844.

    Genome annotation databases

    EnsembliENST00000344956; ENSP00000340870; ENSG00000073008. [P15151-3]
    ENST00000403059; ENSP00000385344; ENSG00000073008. [P15151-2]
    ENST00000406449; ENSP00000383907; ENSG00000073008. [P15151-4]
    ENST00000425690; ENSP00000402060; ENSG00000073008. [P15151-1]
    GeneIDi5817.
    KEGGihsa:5817.
    UCSCiuc002ozm.3. human. [P15151-1]
    uc010ejs.3. human. [P15151-4]
    uc010xxb.2. human. [P15151-3]
    uc010xxc.2. human. [P15151-2]

    Polymorphism databases

    DMDMi1346922.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    The accidental crippler - Issue 75 of October 2006

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24407 mRNA. Translation: AAA36461.1 .
    M24406 mRNA. Translation: AAA36462.1 .
    X64116
    , X64117 , X64118 , X64119 , X64120 , X64121 , X64122 , X64123 Genomic DNA. Translation: CAA45478.1 .
    X64116
    , X64117 , X64118 , X64119 , X64120 , X64121 , X64122 , X64123 Genomic DNA. Translation: CAA45479.1 .
    X64116
    , X64117 , X64118 , X64119 , X64120 , X64122 , X64123 Genomic DNA. Translation: CAA45480.1 .
    AK300349 mRNA. Translation: BAG62091.1 .
    AC068948 Genomic DNA. Translation: AAF69803.1 .
    BC015542 mRNA. Translation: AAH15542.1 .
    CCDSi CCDS12640.1. [P15151-1 ]
    CCDS46105.1. [P15151-2 ]
    CCDS46106.1. [P15151-3 ]
    CCDS46107.1. [P15151-4 ]
    PIRi A43024. RWHUPD.
    S12048. RWHUPA.
    RefSeqi NP_001129240.1. NM_001135768.2. [P15151-2 ]
    NP_001129241.1. NM_001135769.2. [P15151-3 ]
    NP_001129242.2. NM_001135770.3.
    NP_006496.4. NM_006505.4.
    UniGenei Hs.171844.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DGI electron microscopy 22.00 R 28-329 [» ]
    1NN8 electron microscopy 15.00 R/S/T 28-329 [» ]
    3EPC electron microscopy 8.00 R 30-242 [» ]
    3EPD electron microscopy 9.00 R 30-242 [» ]
    3EPF electron microscopy 9.00 R 30-242 [» ]
    3UDW X-ray 2.90 C/D 28-145 [» ]
    3URO X-ray 3.50 R 29-243 [» ]
    4FQP X-ray 3.60 A 28-334 [» ]
    ProteinModelPortali P15151.
    SMRi P15151. Positions 28-333.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111775. 13 interactions.
    DIPi DIP-43987N.
    IntActi P15151. 7 interactions.
    MINTi MINT-5224421.
    STRINGi 9606.ENSP00000402060.

    Protein family/group databases

    MEROPSi I43.001.

    PTM databases

    PhosphoSitei P15151.

    Polymorphism databases

    DMDMi 1346922.

    Proteomic databases

    MaxQBi P15151.
    PaxDbi P15151.
    PRIDEi P15151.

    Protocols and materials databases

    DNASUi 5817.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000344956 ; ENSP00000340870 ; ENSG00000073008 . [P15151-3 ]
    ENST00000403059 ; ENSP00000385344 ; ENSG00000073008 . [P15151-2 ]
    ENST00000406449 ; ENSP00000383907 ; ENSG00000073008 . [P15151-4 ]
    ENST00000425690 ; ENSP00000402060 ; ENSG00000073008 . [P15151-1 ]
    GeneIDi 5817.
    KEGGi hsa:5817.
    UCSCi uc002ozm.3. human. [P15151-1 ]
    uc010ejs.3. human. [P15151-4 ]
    uc010xxb.2. human. [P15151-3 ]
    uc010xxc.2. human. [P15151-2 ]

    Organism-specific databases

    CTDi 5817.
    GeneCardsi GC19P045147.
    HGNCi HGNC:9705. PVR.
    HPAi HPA012568.
    MIMi 173850. gene+phenotype.
    neXtProti NX_P15151.
    PharmGKBi PA34050.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG147224.
    HOGENOMi HOG000237277.
    HOVERGENi HBG019169.
    InParanoidi P15151.
    KOi K06539.
    OMAi GPPSEHS.
    OrthoDBi EOG7D59N6.
    PhylomeDBi P15151.
    TreeFami TF331051.

    Enzyme and pathway databases

    Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_19268. Nectin/Necl trans heterodimerization.

    Miscellaneous databases

    EvolutionaryTracei P15151.
    GeneWikii CD155.
    GenomeRNAii 5817.
    NextBioi 22654.
    PROi P15151.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15151.
    Bgeei P15151.
    CleanExi HS_PVR.
    Genevestigatori P15151.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    InterProi IPR013162. CD80_C2-set.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013106. Ig_V-set.
    IPR003596. Ig_V-set_subgr.
    IPR013151. Immunoglobulin.
    [Graphical view ]
    Pfami PF08205. C2-set_2. 1 hit.
    PF00047. ig. 1 hit.
    PF07686. V-set. 1 hit.
    [Graphical view ]
    SMARTi SM00406. IGv. 1 hit.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cellular receptor for poliovirus: molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily."
      Mendelsohn C.L., Wimmer E., Racaniello V.R.
      Cell 56:855-865(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Racaniello V.R.
      Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "The poliovirus receptor protein is produced both as membrane-bound and secreted forms."
      Koike S., Horie H., Ise I., Okitsu A., Yoshida M., Iizuka N., Takeuchi K., Takegami T., Nomoto A.
      EMBO J. 9:3217-3224(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
      Tissue: Placenta.
    5. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 ALPHA), VARIANT MET-340.
      Tissue: Pancreas.
    7. Cited for: DOMAINS.
    8. "N glycosylation of the virus binding domain is not essential for function of the human poliovirus receptor."
      Zibert A., Wimmer E.
      J. Virol. 66:7368-7373(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLYCOSYLATION SITES.
    9. "The poliovirus receptor CD155 mediates cell-to-matrix contacts by specifically binding to vitronectin."
      Lange R., Peng X., Wimmer E., Lipp M., Bernhardt G.
      Virology 285:218-227(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VTN.
    10. "Interaction of the poliovirus receptor CD155 with the dynein light chain Tctex-1 and its implication for poliovirus pathogenesis."
      Mueller S., Cao X., Welker R., Wimmer E.
      J. Biol. Chem. 277:7897-7904(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DYNLT1.
    11. "Expression of the human poliovirus receptor/CD155 gene is activated by sonic hedgehog."
      Solecki D.J., Gromeier M., Mueller S., Bernhardt G., Wimmer E.
      J. Biol. Chem. 277:25697-25702(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRANSCRIPTIONAL REGULATION BY SHH.
    12. "Recruitment of nectin-3 to cell-cell junctions through trans-heterophilic interaction with CD155, a vitronectin and poliovirus receptor that localizes to alpha(v)beta3 integrin-containing membrane microdomains."
      Mueller S., Wimmer E.
      J. Biol. Chem. 278:31251-31260(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PVRL3.
    13. "Ligand stimulation of CD155alpha inhibits cell adhesion and enhances cell migration in fibroblasts."
      Oda T., Ohka S., Nomoto A.
      Biochem. Biophys. Res. Commun. 319:1253-1264(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ITIM MOTIF, PHOSPHORYLATION AT TYR-398.
    14. "Functional characterization of DNAM-1 (CD226) interaction with its ligands PVR (CD155) and nectin-2 (PRR-2/CD112)."
      Tahara-Hanaoka S., Shibuya K., Onoda Y., Zhang H., Yamazaki S., Miyamoto A., Honda S., Lanier L.L., Shibuya A.
      Int. Immunol. 16:533-538(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD226.
    15. "Receptor (CD155)-dependent endocytosis of poliovirus and retrograde axonal transport of the endosome."
      Ohka S., Matsuda N., Tohyama K., Oda T., Morikawa M., Kuge S., Nomoto A.
      J. Virol. 78:7186-7198(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DYNLT1, MUTAGENESIS OF 369-LYS--ARG-372.
    16. "CD155/PVR plays a key role in cell motility during tumor cell invasion and migration."
      Sloan K.E., Eustace B.K., Stewart J.K., Zehetmeier C., Torella C., Simeone M., Roy J.E., Unger C., Louis D.N., Ilag L.L., Jay D.G.
      BMC Cancer 4:73-73(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Inhibition of cell movement and proliferation by cell-cell contact-induced interaction of Necl-5 with nectin-3."
      Fujito T., Ikeda W., Kakunaga S., Minami Y., Kajita M., Sakamoto Y., Monden M., Takai Y.
      J. Cell Biol. 171:165-173(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PVRL3.
    18. "CD96 (tactile) promotes NK cell-target cell adhesion by interacting with the poliovirus receptor (CD155)."
      Fuchs A., Cella M., Giurisato E., Shaw A.S., Colonna M.
      J. Immunol. 172:3994-3998(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD96.
    19. "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-278, GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-360 (ISOFORM BETA).
      Tissue: Plasma.
    20. "PVR (CD155) and Nectin-2 (CD112) as ligands of the human DNAM-1 (CD226) activating receptor: involvement in tumor cell lysis."
      Pende D., Bottino C., Castriconi R., Cantoni C., Marcenaro S., Rivera P., Spaggiari G.M., Dondero A., Carnemolla B., Reymond N., Mingari M.C., Lopez M., Moretta L., Moretta A.
      Mol. Immunol. 42:463-469(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. Cited for: INTERACTION WITH HHV-5 UL141.
    22. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-307.
      Tissue: Liver.
    23. "The surface protein TIGIT suppresses T cell activation by promoting the generation of mature immunoregulatory dendritic cells."
      Yu X., Harden K., Gonzalez L.C., Francesco M., Chiang E., Irving B., Tom I., Ivelja S., Refino C.J., Clark H., Eaton D., Grogan J.L.
      Nat. Immunol. 10:48-57(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIGIT.
    24. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
      Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
      Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-120, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
    25. Cited for: X-RAY CRYSTALLOGRAPHY (22.0 ANGSTROMS) OF 28-329.
    26. "Complexes of poliovirus serotypes with their common cellular receptor, CD155."
      He Y., Mueller S., Chipman P.R., Bator C.M., Peng X., Bowman V.D., Mukhopadhyay S., Wimmer E., Kuhn R.J., Rossmann M.G.
      J. Virol. 77:4827-4835(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (15.0 ANGSTROMS) OF 28-329.
    27. "Structure of TIGIT immunoreceptor bound to poliovirus receptor reveals a cell-cell adhesion and signaling mechanism that requires cis-trans receptor clustering."
      Stengel K.F., Harden-Bowles K., Yu X., Rouge L., Yin J., Comps-Agrar L., Wiesmann C., Bazan J.F., Eaton D.L., Grogan J.L.
      Proc. Natl. Acad. Sci. U.S.A. 109:5399-5404(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 28-145 IN COMPLEX WITH TIGIT, DISULFIDE BOND, PHOSPHORYLATION AT TYR-398.

    Entry informationi

    Entry nameiPVR_HUMAN
    AccessioniPrimary (citable) accession number: P15151
    Secondary accession number(s): B4DTS9
    , P15152, Q15267, Q15268, Q96BJ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 160 of the entry and version 2 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

    Miscellaneous

    The V-type domain is necessary and sufficient for virus binding and uptake.

    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 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    8. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3