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P15151

- PVR_HUMAN

UniProt

P15151 - PVR_HUMAN

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Protein

Poliovirus receptor

Gene

PVR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. receptor activity Source: ProtInc

GO - Biological processi

  1. adherens junction organization Source: Reactome
  2. cell adhesion Source: UniProtKB-KW
  3. cell-cell junction organization Source: Reactome
  4. cell junction assembly Source: Reactome
  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. susceptibility to natural killer cell mediated cytotoxicity Source: BHF-UCL
  9. susceptibility to T cell mediated cytotoxicity Source: BHF-UCL
  10. viral process Source: UniProtKB-KW
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 343323ExtracellularSequence AnalysisAdd
BLAST
Transmembranei344 – 36724HelicalSequence AnalysisAdd
BLAST
Topological domaini368 – 41750CytoplasmicSequence AnalysisAdd
BLAST

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. focal adhesion Source: UniProtKB
  6. integral component of membrane Source: BHF-UCL
  7. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi369 – 3724KCSR → ACSA: Partial loss of DYNLT1 binding. 1 Publication

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

BgeeiP15151.
CleanExiHS_PVR.
ExpressionAtlasiP15151. baseline and differential.
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. 14 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 – 323Combined sources
Beta strandi35 – 406Combined sources
Beta strandi45 – 473Combined sources
Beta strandi50 – 523Combined sources
Beta strandi60 – 689Combined sources
Beta strandi75 – 795Combined sources
Turni80 – 823Combined sources
Beta strandi83 – 864Combined sources
Beta strandi90 – 945Combined sources
Beta strandi108 – 1103Combined sources
Helixi115 – 1173Combined sources
Beta strandi119 – 12810Combined sources
Beta strandi131 – 14212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
GeneTreeiENSGT00770000120512.
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

        10         20         30         40         50
MARAMAAAWP LLLVALLVLS WPPPGTGDVV VQAPTQVPGF LGDSVTLPCY
60 70 80 90 100
LQVPNMEVTH VSQLTWARHG ESGSMAVFHQ TQGPSYSESK RLEFVAARLG
110 120 130 140 150
AELRNASLRM FGLRVEDEGN YTCLFVTFPQ GSRSVDIWLR VLAKPQNTAE
160 170 180 190 200
VQKVQLTGEP VPMARCVSTG GRPPAQITWH SDLGGMPNTS QVPGFLSGTV
210 220 230 240 250
TVTSLWILVP SSQVDGKNVT CKVEHESFEK PQLLTVNLTV YYPPEVSISG
260 270 280 290 300
YDNNWYLGQN EATLTCDARS NPEPTGYNWS TTMGPLPPFA VAQGAQLLIR
310 320 330 340 350
PVDKPINTTL ICNVTNALGA RQAELTVQVK EGPPSEHSGI SRNAIIFLVL
360 370 380 390 400
GILVFLILLG IGIYFYWSKC SREVLWHCHL CPSSTEHASA SANGHVSYSA
410
VSRENSSSQD PQTEGTR
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:
EMBLi
GenBanki
DDBJi
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]
ENST00000425690; ENSP00000402060; ENSG00000073008.
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 14 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 ]
ENST00000425690 ; ENSP00000402060 ; ENSG00000073008 .
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.
GeneTreei ENSGT00770000120512.
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

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

Gene expression databases

Bgeei P15151.
CleanExi HS_PVR.
ExpressionAtlasi P15151. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 162 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