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P15151 (PVR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Poliovirus receptor
Alternative name(s):
Nectin-like protein 5
Short name=NECL-5
CD_antigen=CD155
Gene names
Name:PVR
Synonyms:PVS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.16 Ref.20

Subunit structure

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. Ref.9 Ref.10 Ref.12 Ref.14 Ref.15 Ref.17 Ref.18 Ref.21 Ref.23

Subcellular location

Isoform Alpha: Cell membrane; Single-pass type I membrane protein.

Isoform Delta: Cell membrane; Single-pass type I membrane protein.

Isoform Beta: Secreted.

Isoform Gamma: Secreted.

Induction

Transcriptionally regulated by SHH. Ref.11

Domain

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. Ref.7

Post-translational modification

N-glycosylated. N-glycan at Asn-120: Hex5HexNAc4. Ref.8 Ref.24

Phosphorylated by Src kinases on tyrosine residues in the ITIM motif upon ligation. Interaction with TIGIT is required for Phosphorylation. Ref.13 Ref.27

Miscellaneous

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

Sequence similarities

Belongs to the nectin family.

Contains 2 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Biophysicochemical properties

Kinetic parameters:

KM=72 nM for VTN

Ontologies

Keywords
   Biological processCell adhesion
Host-virus interaction
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadherens junction organization

Traceable author statement. Source: Reactome

cell junction assembly

Traceable author statement. Source: Reactome

cell migration

Inferred from electronic annotation. Source: Ensembl

cell-cell junction organization

Traceable author statement. Source: Reactome

positive regulation of natural killer cell mediated cytotoxicity

Inferred from mutant phenotype PubMed 16304049. Source: BHF-UCL

positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target

Inferred from mutant phenotype PubMed 12913096. Source: BHF-UCL

regulation of immune response

Traceable author statement. Source: Reactome

single organismal cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

susceptibility to T cell mediated cytotoxicity

Inferred from direct assay Ref.14. Source: BHF-UCL

susceptibility to natural killer cell mediated cytotoxicity

Inferred from mutant phenotype PubMed 12913096. Source: BHF-UCL

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell surface

Inferred from direct assay PubMed 16831868. Source: BHF-UCL

cytoplasm

Traceable author statement Ref.3. Source: ProtInc

extracellular space

Traceable author statement Ref.3. Source: ProtInc

integral component of membrane

Inferred from direct assay PubMed 12913096. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functioncell adhesion molecule binding

Inferred from physical interaction PubMed 12913096. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.23. Source: UniProtKB

receptor activity

Traceable author statement Ref.1. Source: ProtInc

virus receptor activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform Alpha (identifier: P15151-1)

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.
Isoform Beta (identifier: P15151-2)

The sequence of this isoform differs from the canonical sequence as follows:
     340-384: Missing.
Note: Glycosylated on Asn-360.
Isoform Gamma (identifier: P15151-3)

The sequence of this isoform differs from the canonical sequence as follows:
     331-331: E → G
     332-384: Missing.
Note: Glycosylated on Asn-352.
Isoform Delta (identifier: P15151-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 417397Poliovirus receptor
PRO_0000015131

Regions

Topological domain21 – 343323Extracellular Potential
Transmembrane344 – 36724Helical; Potential
Topological domain368 – 41750Cytoplasmic Potential
Domain24 – 139116Ig-like V-type
Domain145 – 23793Ig-like C2-type 1
Domain244 – 32885Ig-like C2-type 2
Region368 – 3725DYNLT1 binding
Motif396 – 4016ITIM motif

Amino acid modifications

Modified residue3981Phosphotyrosine Ref.13 Ref.27
Glycosylation1051N-linked (GlcNAc...)
Glycosylation1201N-linked (GlcNAc...) (complex) Ref.24
Glycosylation1881N-linked (GlcNAc...) Potential
Glycosylation2181N-linked (GlcNAc...) Potential
Glycosylation2371N-linked (GlcNAc...) Potential
Glycosylation2781N-linked (GlcNAc...) Ref.19
Glycosylation3071N-linked (GlcNAc...) Ref.22
Glycosylation3131N-linked (GlcNAc...) Potential
Disulfide bond49 ↔ 123 Ref.27
Disulfide bond166 ↔ 221 By similarity
Disulfide bond266 ↔ 312 By similarity

Natural variations

Alternative sequence3311E → G in isoform Gamma.
VSP_002618
Alternative sequence332 – 38453Missing in isoform Gamma.
VSP_002619
Alternative sequence340 – 38445Missing in isoform Beta.
VSP_002617
Alternative sequence385 – 3928TEHASASA → EHHQSCRN in isoform Delta.
VSP_002620
Alternative sequence393 – 41725Missing in isoform Delta.
VSP_002621
Natural variant671A → T.
Corresponds to variant rs1058402 [ dbSNP | Ensembl ].
VAR_003952
Natural variant2951A → T.
Corresponds to variant rs35365841 [ dbSNP | Ensembl ].
VAR_049994
Natural variant3401I → M. Ref.6
Corresponds to variant rs203710 [ dbSNP | Ensembl ].
VAR_011736

Experimental info

Mutagenesis369 – 3724KCSR → ACSA: Partial loss of DYNLT1 binding. Ref.8 Ref.15

Secondary structure

......................... 417
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: D15C012CE853169B

FASTA41745,303
        10         20         30         40         50         60 
MARAMAAAWP LLLVALLVLS WPPPGTGDVV VQAPTQVPGF LGDSVTLPCY LQVPNMEVTH 

        70         80         90        100        110        120 
VSQLTWARHG ESGSMAVFHQ TQGPSYSESK RLEFVAARLG AELRNASLRM FGLRVEDEGN 

       130        140        150        160        170        180 
YTCLFVTFPQ GSRSVDIWLR VLAKPQNTAE VQKVQLTGEP VPMARCVSTG GRPPAQITWH 

       190        200        210        220        230        240 
SDLGGMPNTS QVPGFLSGTV TVTSLWILVP SSQVDGKNVT CKVEHESFEK PQLLTVNLTV 

       250        260        270        280        290        300 
YYPPEVSISG YDNNWYLGQN EATLTCDARS NPEPTGYNWS TTMGPLPPFA VAQGAQLLIR 

       310        320        330        340        350        360 
PVDKPINTTL ICNVTNALGA RQAELTVQVK EGPPSEHSGI SRNAIIFLVL GILVFLILLG 

       370        380        390        400        410 
IGIYFYWSKC SREVLWHCHL CPSSTEHASA SANGHVSYSA VSRENSSSQD PQTEGTR 

« Hide

Isoform Beta [UniParc].

Checksum: 7B56B38F949996BE
Show »

FASTA37240,125
Isoform Gamma [UniParc].

Checksum: F63D1B6CF19F2A6F
Show »

FASTA36439,304
Isoform Delta [UniParc].

Checksum: 528DFC93B73C7FD8
Show »

FASTA39242,864

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Functional domains of the poliovirus receptor."
Koike S., Ise I., Nomoto A.
Proc. Natl. Acad. Sci. U.S.A. 88:4104-4108(1991) [PubMed] [Europe PMC] [Abstract]
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]"Downregulation of natural killer cell-activating ligand CD155 by human cytomegalovirus UL141."
Tomasec P., Wang E.C., Davison A.J., Vojtesek B., Armstrong M., Griffin C., McSharry B.P., Morris R.J., Llewellyn-Lacey S., Rickards C., Nomoto A., Sinzger C., Wilkinson G.W.
Nat. Immunol. 6:181-188(2005) [PubMed] [Europe PMC] [Abstract]
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]"Interaction of the poliovirus receptor with poliovirus."
He Y., Bowman V.D., Mueller S., Bator C.M., Bella J., Peng X., Baker T.S., Wimmer E., Kuhn R.J., Rossmann M.G.
Proc. Natl. Acad. Sci. U.S.A. 97:79-84(2000) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Protein Spotlight

The accidental crippler - Issue 75 of October 2006

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24407 mRNA. Translation: AAA36461.1.
M24406 mRNA. Translation: AAA36462.1.
X64116 expand/collapse EMBL AC list , X64117, X64118, X64119, X64120, X64121, X64122, X64123 Genomic DNA. Translation: CAA45478.1.
X64116 expand/collapse EMBL AC list , X64117, X64118, X64119, X64120, X64121, X64122, X64123 Genomic DNA. Translation: CAA45479.1.
X64116 expand/collapse EMBL AC list , 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.
CCDSCCDS46105.1. [P15151-2]
CCDS46106.1. [P15151-3]
PIRRWHUPD. A43024.
RWHUPA. S12048.
RefSeqNP_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.
UniGeneHs.171844.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP15151.
SMRP15151. Positions 28-333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111775. 13 interactions.
DIPDIP-43987N.
IntActP15151. 7 interactions.
MINTMINT-5224421.
STRING9606.ENSP00000402060.

Protein family/group databases

MEROPSI43.001.

PTM databases

PhosphoSiteP15151.

Polymorphism databases

DMDM1346922.

Proteomic databases

MaxQBP15151.
PaxDbP15151.
PRIDEP15151.

Protocols and materials databases

DNASU5817.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344956; ENSP00000340870; ENSG00000073008. [P15151-3]
ENST00000403059; ENSP00000385344; ENSG00000073008. [P15151-2]
ENST00000406449; ENSP00000383907; ENSG00000073008. [P15151-4]
ENST00000425690; ENSP00000402060; ENSG00000073008. [P15151-1]
GeneID5817.
KEGGhsa:5817.
UCSCuc002ozm.3. human. [P15151-1]
uc010ejs.3. human. [P15151-4]
uc010xxb.2. human. [P15151-3]
uc010xxc.2. human. [P15151-2]

Organism-specific databases

CTD5817.
GeneCardsGC19P045147.
HGNCHGNC:9705. PVR.
HPAHPA012568.
MIM173850. gene+phenotype.
neXtProtNX_P15151.
PharmGKBPA34050.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG147224.
HOGENOMHOG000237277.
HOVERGENHBG019169.
InParanoidP15151.
KOK06539.
OMAGPPSEHS.
OrthoDBEOG7D59N6.
PhylomeDBP15151.
TreeFamTF331051.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP15151.
BgeeP15151.
CleanExHS_PVR.
GenevestigatorP15151.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013106. Ig_V-set.
IPR003596. Ig_V-set_subgr.
IPR013151. Immunoglobulin.
[Graphical view]
PfamPF08205. C2-set_2. 1 hit.
PF00047. ig. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTSM00406. IGv. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15151.
GeneWikiCD155.
GenomeRNAi5817.
NextBio22654.
PROP15151.
SOURCESearch...

Entry information

Entry namePVR_HUMAN
AccessionPrimary (citable) accession number: P15151
Secondary accession number(s): B4DTS9 expand/collapse secondary AC list , P15152, Q15267, Q15268, Q96BJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries