P15151 (PVR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Poliovirus receptor

Alternative name(s):
Nectin-like protein 5
Short name=NECL-5
CD_antigen=CD155

Gene names

Name:	PVR
Synonyms:	PVS

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	417 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.15 Ref.19
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.13 Ref.14 Ref.16 Ref.17 Ref.20 Ref.22
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
Post-translational modification	N-glycosylated. N-glycan at Asn-120: Hex5HexNAc4. Ref.8 Ref.23
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 process	Cell adhesion Host-virus interaction
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adherens junction organization Traceable author statement. Source: Reactome cell junction assembly Traceable author statement. Source: Reactome cell migration Inferred from electronic annotation. Source: Compara cell-cell adhesion Inferred from electronic annotation. Source: Compara positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target Inferred from mutant phenotype PubMed 12913096. Source: BHF-UCL susceptibility to T cell mediated cytotoxicity Inferred from direct assay Ref.13. Source: BHF-UCL susceptibility to natural killer cell mediated cytotoxicity Inferred from mutant phenotype PubMed 12913096. Source: BHF-UCL virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell junction Inferred from direct assay. Source: HPA cell 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 to membrane Inferred from direct assay PubMed 12913096. Source: BHF-UCL nucleus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA
Molecular_function	receptor activity Traceable author statement Ref.1. Source: ProtInc
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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Potential

Chain

21 – 417

397

Poliovirus receptor

PRO_0000015131

Regions

Topological domain

21 – 343

323

Extracellular Potential

Transmembrane

344 – 367

24

Helical; Potential

Topological domain

368 – 417

50

Cytoplasmic Potential

Domain

24 – 139

116

Ig-like V-type

Domain

145 – 237

93

Ig-like C2-type 1

Domain

244 – 328

85

Ig-like C2-type 2

Region

368 – 372

5

DYNLT1 binding

Amino acid modifications

Glycosylation

105

1

N-linked (GlcNAc...)

Glycosylation

120

1

N-linked (GlcNAc...) (complex) Ref.23

Glycosylation

188

1

N-linked (GlcNAc...) Potential

Glycosylation

218

1

N-linked (GlcNAc...) Potential

Glycosylation

237

1

N-linked (GlcNAc...) Potential

Glycosylation

278

1

N-linked (GlcNAc...) Ref.18

Glycosylation

307

1

N-linked (GlcNAc...) Ref.21

Glycosylation

313

1

N-linked (GlcNAc...) Potential

Disulfide bond

49 ↔ 123

By similarity

Disulfide bond

166 ↔ 221

By similarity

Disulfide bond

266 ↔ 312

By similarity

Natural variations

Alternative sequence

331

1

E → G in isoform Gamma.

VSP_002618

Alternative sequence

332 – 384

53

Missing in isoform Gamma.

VSP_002619

Alternative sequence

340 – 384

45

Missing in isoform Beta.

VSP_002617

Alternative sequence

385 – 392

8

TEHASASA → EHHQSCRN in isoform Delta.

VSP_002620

Alternative sequence

393 – 417

25

Missing in isoform Delta.

VSP_002621

Natural variant

67

1

A → T.
Corresponds to variant rs1058402 [ dbSNP | Ensembl ].

VAR_003952

Natural variant

295

1

A → T.
Corresponds to variant rs35365841 [ dbSNP | Ensembl ].

VAR_049994

Natural variant

340

1

I → M. Ref.6
Corresponds to variant rs203710 [ dbSNP | Ensembl ].

VAR_011736

Experimental info

Mutagenesis

369 – 372

4

KCSR → ACSA: Partial loss of DYNLT1 binding. Ref.8 Ref.14

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

417

Helix Strand Turn

Details...

Beta strand

30 – 32

3

Beta strand

35 – 40

6

Beta strand

45 – 47

3

Beta strand

50 – 52

3

Beta strand

60 – 68

9

Beta strand

75 – 79

5

Turn

80 – 82

3

Beta strand

83 – 86

4

Beta strand

90 – 94

5

Beta strand

108 – 110

3

Helix

115 – 117

3

Beta strand

119 – 128

10

Beta strand

131 – 142

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha [UniParc]. Last modified February 1, 1996. Version 2. Checksum: D15C012CE853169B	FASTA	417	45,303
	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
	Isoform Beta [UniParc]. Checksum: 7B56B38F949996BE	FASTA	372	40,125
	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 EGPPSEHSGT EHASASANGH VSYSAVSREN 370 SSSQDPQTEG TR
	Isoform Gamma [UniParc]. Checksum: F63D1B6CF19F2A6F	FASTA	364	39,304
	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 GTEHASASAN GHVSYSAVSR ENSSSQDPQT EGTR
	Isoform Delta [UniParc]. Checksum: 528DFC93B73C7FD8	FASTA	392	42,864
	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 IGIYFYWSKC SREVLWHCHL CPSSEHHQSC RN

References

	« Hide 'large scale' referencesShow '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. , 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]	"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]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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), MASS SPECTROMETRY. Tissue: Plasma.
[19]	"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.
[20]	"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.
[21]	"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, MASS SPECTROMETRY. Tissue: Liver.
[22]	"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.
[23]	"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, MASS SPECTROMETRY.
[24]	"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.
[25]	"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.
+	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 , 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.

IPI

IPI00219425.
IPI00219426.
IPI00219427.
IPI00299158.

PIR

RWHUPD. A43024.
RWHUPA. S12048.

RefSeq

NP_001129240.1. NM_001135768.1.
NP_001129241.1. NM_001135769.1.
NP_001129242.1. NM_001135770.1.
NP_006496.3. NM_006505.3.

UniGene

Hs.171844.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P15151.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-43987N.

IntAct

P15151. 4 interactions.

MINT

MINT-5224421.

STRING

9606.ENSP00000402060.

Protein family/group databases

MEROPS

I43.001.

PTM databases

PhosphoSite

P15151.

Polymorphism databases

DMDM

1346922.

Proteomic databases

PaxDb

P15151.

PRIDE

P15151.

Protocols and materials databases

DNASU

5817.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000344956; ENSP00000340870; ENSG00000073008.
ENST00000403059; ENSP00000385344; ENSG00000073008.
ENST00000406449; ENSP00000383907; ENSG00000073008.
ENST00000425690; ENSP00000402060; ENSG00000073008.

GeneID

5817.

KEGG

hsa:5817.

UCSC

uc002ozm.3. human.
uc010ejs.3. human.
uc010xxb.2. human.
uc010xxc.2. human.

Organism-specific databases

CTD

5817.

GeneCards

GC19P045147.

HGNC

HGNC:9705. PVR.

HPA

HPA012568.

MIM

173850. gene+phenotype.

neXtProt

NX_P15151.

PharmGKB

PA34050.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG147224.

HOGENOM

HOG000237277.

HOVERGEN

HBG019169.

InParanoid

P15151.

KO

K06539.

OMA

GPPSEHS.

OrthoDB

EOG4PK281.

PhylomeDB

P15151.

Enzyme and pathway databases

Reactome

REACT_111155. Cell-Cell communication.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P15151.

Bgee

P15151.

CleanEx

HS_PVR.

Genevestigator

P15151.

GermOnline

ENSG00000073008. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 3 hits.

InterPro

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]

Pfam

PF08205. C2-set_2. 1 hit.
PF00047. ig. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]

SMART

SM00406. IGv. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P15151.

GenomeRNAi

5817.

NextBio

22654.

SOURCE

Search...

Entry information

Entry name

PVR_HUMAN

Accession

Primary (citable) accession number: P15151
Secondary accession number(s): B4DTS9 , P15152, Q15267, Q15268, Q96BJ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 146 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.