Full text data of PVRL2
PVRL2
(HVEB, PRR2)
[Confidence: high (a blood group or CD marker)]
Poliovirus receptor-related protein 2 (Herpes virus entry mediator B; Herpesvirus entry mediator B; HveB; Nectin-2; CD112; Flags: Precursor)
Poliovirus receptor-related protein 2 (Herpes virus entry mediator B; Herpesvirus entry mediator B; HveB; Nectin-2; CD112; Flags: Precursor)
UniProt
Q92692
ID PVRL2_HUMAN Reviewed; 538 AA.
AC Q92692; O75455; Q6IBI6; Q96J29;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1997, sequence version 1.
DT 22-JAN-2014, entry version 143.
DE RecName: Full=Poliovirus receptor-related protein 2;
DE AltName: Full=Herpes virus entry mediator B;
DE Short=Herpesvirus entry mediator B;
DE Short=HveB;
DE AltName: Full=Nectin-2;
DE AltName: CD_antigen=CD112;
DE Flags: Precursor;
GN Name=PVRL2; Synonyms=HVEB, PRR2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA).
RX PubMed=7622062; DOI=10.1016/0378-1119(95)00180-E;
RA Eberle F., Dubreuil P., Mattei M.-G., Devilard E., Lopez M.;
RT "The human PRR2 gene, related to the human poliovirus receptor gene
RT (PVR), is the true homolog of the murine MPH gene.";
RL Gene 159:267-272(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), AND FUNCTION AS A RECEPTOR
RP FOR MUTANTS OF HHV-1; HHV-2 AND PRV.
RX PubMed=9657005; DOI=10.1006/viro.1998.9218;
RA Warner M.S., Geraghty R.J., Martinez W.M., Montgomery R.I.,
RA Whitbeck J.C., Xu R., Eisenberg R.J., Cohen G.H., Spear P.G.;
RT "A cell surface protein with herpesvirus entry activity (HveB) confers
RT susceptibility to infection by mutants of herpes simplex virus type 1,
RT herpes simplex virus type 2, and pseudorabies virus.";
RL Virology 246:179-189(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-538.
RA Yoshiura K., Murray J.C.;
RT "A transcriptional map in the region of 19q13 derived using direct
RT sequencing and exon trapping.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 449-538.
RX PubMed=10520737;
RA Freitas E.M., Zhang W.J., Lalonde J.P., Tay G.K., Gaudieri S.,
RA Ashworth L.K., Van Bockxmeer F.M., Dawkins R.L.;
RT "Sequencing of 42kb of the APO E-C2 gene cluster reveals a new gene:
RT PEREC1.";
RL DNA Seq. 9:89-100(1998).
RN [8]
RP INTERACTION WITH HHV-1 MUTANT RID1; HHV-2 AND PRV GLYCOPROTEIN D, AND
RP MUTAGENESIS OF MET-89.
RX PubMed=11602758; DOI=10.1128/JVI.75.22.11185-11195.2001;
RA Martinez W.M., Spear P.G.;
RT "Structural features of nectin-2 (HveB) required for herpes simplex
RT virus entry.";
RL J. Virol. 75:11185-11195(2001).
RN [9]
RP INTERACTION WITH CD226.
RX PubMed=15607800; DOI=10.1016/j.molimm.2004.07.028;
RA Pende D., Bottino C., Castriconi R., Cantoni C., Marcenaro S.,
RA Rivera P., Spaggiari G.M., Dondero A., Carnemolla B., Reymond N.,
RA Mingari M.C., Lopez M., Moretta L., Moretta A.;
RT "PVR (CD155) and Nectin-2 (CD112) as ligands of the human DNAM-1
RT (CD226) activating receptor: involvement in tumor cell lysis.";
RL Mol. Immunol. 42:463-469(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP INTERACTION WITH TIGIT.
RX PubMed=19011627; DOI=10.1038/ni.1674;
RA Yu X., Harden K., Gonzalez L.C., Francesco M., Chiang E., Irving B.,
RA Tom I., Ivelja S., Refino C.J., Clark H., Eaton D., Grogan J.L.;
RT "The surface protein TIGIT suppresses T cell activation by promoting
RT the generation of mature immunoregulatory dendritic cells.";
RL Nat. Immunol. 10:48-57(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Probable cell adhesion protein.
CC -!- SUBUNIT: Can form trans-heterodimers with PVRL3/nectin-3 (By
CC similarity). Interacts with CD226. Binds with low affinity to
CC TIGIT. Interacts with herpes simplex virus 1 (HHV-1) mutant Rid1,
CC herpes simplex virus 1 (HHV-2) and pseudorabies virus (PRV)
CC envelope glycoprotein D; functions as an entry receptor for these
CC viruses.
CC -!- INTERACTION:
CC Q15762:CD226; NbExp=2; IntAct=EBI-718419, EBI-4314442;
CC P55196:MLLT4; NbExp=2; IntAct=EBI-718419, EBI-365875;
CC Q9NQS3:PVRL3; NbExp=2; IntAct=EBI-718419, EBI-2826725;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Delta;
CC IsoId=Q92692-1; Sequence=Displayed;
CC Name=Alpha;
CC IsoId=Q92692-2; Sequence=VSP_002628, VSP_002629;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the nectin family.
CC -!- SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like)
CC domains.
CC -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC domain.
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DR EMBL; X80038; CAA56342.1; -; mRNA.
DR EMBL; AF058448; AAC23797.1; -; mRNA.
DR EMBL; CR456818; CAG33099.1; -; mRNA.
DR EMBL; CH471126; EAW57298.1; -; Genomic_DNA.
DR EMBL; BC003091; AAH03091.1; -; mRNA.
DR EMBL; AF044968; AAC82348.1; -; Genomic_DNA.
DR EMBL; AF044962; AAC82348.1; JOINED; Genomic_DNA.
DR EMBL; AF044963; AAC82348.1; JOINED; Genomic_DNA.
DR EMBL; AF044964; AAC82348.1; JOINED; Genomic_DNA.
DR EMBL; AF044966; AAC82348.1; JOINED; Genomic_DNA.
DR EMBL; AF044967; AAC82348.1; JOINED; Genomic_DNA.
DR EMBL; AF050154; AAD02503.1; -; Genomic_DNA.
DR PIR; I68093; I68093.
DR RefSeq; NP_001036189.1; NM_001042724.1.
DR RefSeq; NP_002847.1; NM_002856.2.
DR UniGene; Hs.655455; -.
DR PDB; 3R0N; X-ray; 1.30 A; A=32-158.
DR PDB; 4DFH; X-ray; 1.85 A; A/B=32-158.
DR PDB; 4DFI; X-ray; 1.80 A; A=32-158.
DR PDB; 4HZA; X-ray; 1.70 A; A/B=32-158.
DR PDBsum; 3R0N; -.
DR PDBsum; 4DFH; -.
DR PDBsum; 4DFI; -.
DR PDBsum; 4HZA; -.
DR ProteinModelPortal; Q92692; -.
DR SMR; Q92692; 32-350.
DR DIP; DIP-41043N; -.
DR IntAct; Q92692; 15.
DR MINT; MINT-90946; -.
DR STRING; 9606.ENSP00000252483; -.
DR PhosphoSite; Q92692; -.
DR DMDM; 12643789; -.
DR PaxDb; Q92692; -.
DR PRIDE; Q92692; -.
DR DNASU; 5819; -.
DR Ensembl; ENST00000252483; ENSP00000252483; ENSG00000130202.
DR Ensembl; ENST00000252485; ENSP00000252485; ENSG00000130202.
DR GeneID; 5819; -.
DR KEGG; hsa:5819; -.
DR UCSC; uc002ozw.1; human.
DR CTD; 5819; -.
DR GeneCards; GC19P045349; -.
DR HGNC; HGNC:9707; PVRL2.
DR HPA; CAB026138; -.
DR HPA; HPA012759; -.
DR MIM; 600798; gene.
DR neXtProt; NX_Q92692; -.
DR PharmGKB; PA34052; -.
DR eggNOG; NOG149530; -.
DR HOGENOM; HOG000237277; -.
DR HOVERGEN; HBG019169; -.
DR InParanoid; Q92692; -.
DR KO; K06531; -.
DR OMA; REVTWLR; -.
DR OrthoDB; EOG7D59N6; -.
DR PhylomeDB; Q92692; -.
DR Reactome; REACT_111155; Cell-Cell communication.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; PVRL2; human.
DR EvolutionaryTrace; Q92692; -.
DR GeneWiki; PVRL2; -.
DR GenomeRNAi; 5819; -.
DR NextBio; 22666; -.
DR PRO; PR:Q92692; -.
DR ArrayExpress; Q92692; -.
DR Bgee; Q92692; -.
DR CleanEx; HS_PVRL2; -.
DR Genevestigator; Q92692; -.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0016021; C:integral to membrane; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005915; C:zonula adherens; ISS:BHF-UCL.
DR GO; GO:0015026; F:coreceptor activity; TAS:ProtInc.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0001675; P:acrosome assembly; IEA:Ensembl.
DR GO; GO:0034332; P:adherens junction organization; TAS:Reactome.
DR GO; GO:0051856; P:adhesion to symbiont; IDA:BHF-UCL.
DR GO; GO:0034329; P:cell junction assembly; TAS:Reactome.
DR GO; GO:0032990; P:cell part morphogenesis; IEA:Ensembl.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0051654; P:establishment of mitochondrion localization; IEA:Ensembl.
DR GO; GO:0009566; P:fertilization; IEA:Ensembl.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IDA:BHF-UCL.
DR GO; GO:0007156; P:homophilic cell adhesion; IDA:BHF-UCL.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0002891; P:positive regulation of immunoglobulin mediated immune response; IMP:BHF-UCL.
DR GO; GO:0033005; P:positive regulation of mast cell activation; IMP:BHF-UCL.
DR GO; GO:0002860; P:positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; IMP:BHF-UCL.
DR GO; GO:0009615; P:response to virus; IEA:GOC.
DR GO; GO:0030382; P:sperm mitochondrion organization; IEA:Ensembl.
DR GO; GO:0007286; P:spermatid development; ISS:BHF-UCL.
DR GO; GO:0007289; P:spermatid nucleus differentiation; IEA:Ensembl.
DR GO; GO:0042271; P:susceptibility to natural killer cell mediated cytotoxicity; IMP:BHF-UCL.
DR GO; GO:0060370; P:susceptibility to T cell mediated cytotoxicity; IDA:BHF-UCL.
DR GO; GO:0046814; P:virion attachment, binding of host cell surface coreceptor; IDA:BHF-UCL.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Complete proteome; Disulfide bond; Glycoprotein;
KW Host cell receptor for virus entry; Host-virus interaction;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 31 Potential.
FT CHAIN 32 538 Poliovirus receptor-related protein 2.
FT /FTId=PRO_0000015136.
FT TOPO_DOM 32 360 Extracellular (Potential).
FT TRANSMEM 361 381 Helical; (Potential).
FT TOPO_DOM 382 538 Cytoplasmic (Potential).
FT DOMAIN 32 156 Ig-like V-type.
FT DOMAIN 162 256 Ig-like C2-type 1.
FT DOMAIN 261 345 Ig-like C2-type 2.
FT MOD_RES 433 433 Phosphoserine.
FT CARBOHYD 137 137 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 324 324 N-linked (GlcNAc...) (Potential).
FT DISULFID 54 140 By similarity.
FT DISULFID 183 238 By similarity.
FT DISULFID 283 329 By similarity.
FT VAR_SEQ 351 479 NTAGAGATGGIIGGIIAAIIATAVAATGILICRQQRKEQTL
FT QGAEEDEDLEGPPSYKPPTPKAKLEAQEMPSQLFTLGASEH
FT SPLKTPYFDAGASCTEQEMPRYHELPTLEERSGPLHPGATS
FT LGSPIP -> RASPRDVGPLVWGAVGGTLLVLLLLAGGSLA
FT FILLRVRRRRKSPGGAGGGASGDGGFYDPKAQVLGNGDPVF
FT WTPVVPGPMEPDGKDEEEEEEEEKAEKGLMLPPPPALEDDM
FT ESQLDGSLISRRAVYV (in isoform Alpha).
FT /FTId=VSP_002628.
FT VAR_SEQ 480 538 Missing (in isoform Alpha).
FT /FTId=VSP_002629.
FT MUTAGEN 89 89 M->F: Loss of entry of HHV-1/Rid1 and
FT HSV-2. No effect on PRV entry.
FT MUTAGEN 89 89 M->I: Increased entry of HHV-1/Rid1 and
FT HSV-2.
FT STRAND 35 37
FT STRAND 40 43
FT STRAND 50 52
FT STRAND 55 58
FT STRAND 64 71
FT HELIX 77 79
FT STRAND 81 86
FT TURN 87 89
FT STRAND 90 92
FT STRAND 95 98
FT HELIX 100 102
FT STRAND 103 107
FT TURN 113 115
FT STRAND 125 127
FT HELIX 132 134
FT STRAND 136 145
FT STRAND 148 157
SQ SEQUENCE 538 AA; 57742 MW; 3AE4F83E92F6F624 CRC64;
MARAAALLPS RSPPTPLLWP LLLLLLLETG AQDVRVQVLP EVRGQLGGTV ELPCHLLPPV
PGLYISLVTW QRPDAPANHQ NVAAFHPKMG PSFPSPKPGS ERLSFVSAKQ STGQDTEAEL
QDATLALHGL TVEDEGNYTC EFATFPKGSV RGMTWLRVIA KPKNQAEAQK VTFSQDPTTV
ALCISKEGRP PARISWLSSL DWEAKETQVS GTLAGTVTVT SRFTLVPSGR ADGVTVTCKV
EHESFEEPAL IPVTLSVRYP PEVSISGYDD NWYLGRTDAT LSCDVRSNPE PTGYDWSTTS
GTFPTSAVAQ GSQLVIHAVD SLFNTTFVCT VTNAVGMGRA EQVIFVRETP NTAGAGATGG
IIGGIIAAII ATAVAATGIL ICRQQRKEQT LQGAEEDEDL EGPPSYKPPT PKAKLEAQEM
PSQLFTLGAS EHSPLKTPYF DAGASCTEQE MPRYHELPTL EERSGPLHPG ATSLGSPIPV
PPGPPAVEDV SLDLEDEEGE EEEEYLDKIN PIYDALSYSS PSDSYQGKGF VMSRAMYV
//
ID PVRL2_HUMAN Reviewed; 538 AA.
AC Q92692; O75455; Q6IBI6; Q96J29;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1997, sequence version 1.
DT 22-JAN-2014, entry version 143.
DE RecName: Full=Poliovirus receptor-related protein 2;
DE AltName: Full=Herpes virus entry mediator B;
DE Short=Herpesvirus entry mediator B;
DE Short=HveB;
DE AltName: Full=Nectin-2;
DE AltName: CD_antigen=CD112;
DE Flags: Precursor;
GN Name=PVRL2; Synonyms=HVEB, PRR2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA).
RX PubMed=7622062; DOI=10.1016/0378-1119(95)00180-E;
RA Eberle F., Dubreuil P., Mattei M.-G., Devilard E., Lopez M.;
RT "The human PRR2 gene, related to the human poliovirus receptor gene
RT (PVR), is the true homolog of the murine MPH gene.";
RL Gene 159:267-272(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), AND FUNCTION AS A RECEPTOR
RP FOR MUTANTS OF HHV-1; HHV-2 AND PRV.
RX PubMed=9657005; DOI=10.1006/viro.1998.9218;
RA Warner M.S., Geraghty R.J., Martinez W.M., Montgomery R.I.,
RA Whitbeck J.C., Xu R., Eisenberg R.J., Cohen G.H., Spear P.G.;
RT "A cell surface protein with herpesvirus entry activity (HveB) confers
RT susceptibility to infection by mutants of herpes simplex virus type 1,
RT herpes simplex virus type 2, and pseudorabies virus.";
RL Virology 246:179-189(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-538.
RA Yoshiura K., Murray J.C.;
RT "A transcriptional map in the region of 19q13 derived using direct
RT sequencing and exon trapping.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 449-538.
RX PubMed=10520737;
RA Freitas E.M., Zhang W.J., Lalonde J.P., Tay G.K., Gaudieri S.,
RA Ashworth L.K., Van Bockxmeer F.M., Dawkins R.L.;
RT "Sequencing of 42kb of the APO E-C2 gene cluster reveals a new gene:
RT PEREC1.";
RL DNA Seq. 9:89-100(1998).
RN [8]
RP INTERACTION WITH HHV-1 MUTANT RID1; HHV-2 AND PRV GLYCOPROTEIN D, AND
RP MUTAGENESIS OF MET-89.
RX PubMed=11602758; DOI=10.1128/JVI.75.22.11185-11195.2001;
RA Martinez W.M., Spear P.G.;
RT "Structural features of nectin-2 (HveB) required for herpes simplex
RT virus entry.";
RL J. Virol. 75:11185-11195(2001).
RN [9]
RP INTERACTION WITH CD226.
RX PubMed=15607800; DOI=10.1016/j.molimm.2004.07.028;
RA Pende D., Bottino C., Castriconi R., Cantoni C., Marcenaro S.,
RA Rivera P., Spaggiari G.M., Dondero A., Carnemolla B., Reymond N.,
RA Mingari M.C., Lopez M., Moretta L., Moretta A.;
RT "PVR (CD155) and Nectin-2 (CD112) as ligands of the human DNAM-1
RT (CD226) activating receptor: involvement in tumor cell lysis.";
RL Mol. Immunol. 42:463-469(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP INTERACTION WITH TIGIT.
RX PubMed=19011627; DOI=10.1038/ni.1674;
RA Yu X., Harden K., Gonzalez L.C., Francesco M., Chiang E., Irving B.,
RA Tom I., Ivelja S., Refino C.J., Clark H., Eaton D., Grogan J.L.;
RT "The surface protein TIGIT suppresses T cell activation by promoting
RT the generation of mature immunoregulatory dendritic cells.";
RL Nat. Immunol. 10:48-57(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Probable cell adhesion protein.
CC -!- SUBUNIT: Can form trans-heterodimers with PVRL3/nectin-3 (By
CC similarity). Interacts with CD226. Binds with low affinity to
CC TIGIT. Interacts with herpes simplex virus 1 (HHV-1) mutant Rid1,
CC herpes simplex virus 1 (HHV-2) and pseudorabies virus (PRV)
CC envelope glycoprotein D; functions as an entry receptor for these
CC viruses.
CC -!- INTERACTION:
CC Q15762:CD226; NbExp=2; IntAct=EBI-718419, EBI-4314442;
CC P55196:MLLT4; NbExp=2; IntAct=EBI-718419, EBI-365875;
CC Q9NQS3:PVRL3; NbExp=2; IntAct=EBI-718419, EBI-2826725;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Delta;
CC IsoId=Q92692-1; Sequence=Displayed;
CC Name=Alpha;
CC IsoId=Q92692-2; Sequence=VSP_002628, VSP_002629;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the nectin family.
CC -!- SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like)
CC domains.
CC -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC domain.
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DR EMBL; X80038; CAA56342.1; -; mRNA.
DR EMBL; AF058448; AAC23797.1; -; mRNA.
DR EMBL; CR456818; CAG33099.1; -; mRNA.
DR EMBL; CH471126; EAW57298.1; -; Genomic_DNA.
DR EMBL; BC003091; AAH03091.1; -; mRNA.
DR EMBL; AF044968; AAC82348.1; -; Genomic_DNA.
DR EMBL; AF044962; AAC82348.1; JOINED; Genomic_DNA.
DR EMBL; AF044963; AAC82348.1; JOINED; Genomic_DNA.
DR EMBL; AF044964; AAC82348.1; JOINED; Genomic_DNA.
DR EMBL; AF044966; AAC82348.1; JOINED; Genomic_DNA.
DR EMBL; AF044967; AAC82348.1; JOINED; Genomic_DNA.
DR EMBL; AF050154; AAD02503.1; -; Genomic_DNA.
DR PIR; I68093; I68093.
DR RefSeq; NP_001036189.1; NM_001042724.1.
DR RefSeq; NP_002847.1; NM_002856.2.
DR UniGene; Hs.655455; -.
DR PDB; 3R0N; X-ray; 1.30 A; A=32-158.
DR PDB; 4DFH; X-ray; 1.85 A; A/B=32-158.
DR PDB; 4DFI; X-ray; 1.80 A; A=32-158.
DR PDB; 4HZA; X-ray; 1.70 A; A/B=32-158.
DR PDBsum; 3R0N; -.
DR PDBsum; 4DFH; -.
DR PDBsum; 4DFI; -.
DR PDBsum; 4HZA; -.
DR ProteinModelPortal; Q92692; -.
DR SMR; Q92692; 32-350.
DR DIP; DIP-41043N; -.
DR IntAct; Q92692; 15.
DR MINT; MINT-90946; -.
DR STRING; 9606.ENSP00000252483; -.
DR PhosphoSite; Q92692; -.
DR DMDM; 12643789; -.
DR PaxDb; Q92692; -.
DR PRIDE; Q92692; -.
DR DNASU; 5819; -.
DR Ensembl; ENST00000252483; ENSP00000252483; ENSG00000130202.
DR Ensembl; ENST00000252485; ENSP00000252485; ENSG00000130202.
DR GeneID; 5819; -.
DR KEGG; hsa:5819; -.
DR UCSC; uc002ozw.1; human.
DR CTD; 5819; -.
DR GeneCards; GC19P045349; -.
DR HGNC; HGNC:9707; PVRL2.
DR HPA; CAB026138; -.
DR HPA; HPA012759; -.
DR MIM; 600798; gene.
DR neXtProt; NX_Q92692; -.
DR PharmGKB; PA34052; -.
DR eggNOG; NOG149530; -.
DR HOGENOM; HOG000237277; -.
DR HOVERGEN; HBG019169; -.
DR InParanoid; Q92692; -.
DR KO; K06531; -.
DR OMA; REVTWLR; -.
DR OrthoDB; EOG7D59N6; -.
DR PhylomeDB; Q92692; -.
DR Reactome; REACT_111155; Cell-Cell communication.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; PVRL2; human.
DR EvolutionaryTrace; Q92692; -.
DR GeneWiki; PVRL2; -.
DR GenomeRNAi; 5819; -.
DR NextBio; 22666; -.
DR PRO; PR:Q92692; -.
DR ArrayExpress; Q92692; -.
DR Bgee; Q92692; -.
DR CleanEx; HS_PVRL2; -.
DR Genevestigator; Q92692; -.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0016021; C:integral to membrane; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005915; C:zonula adherens; ISS:BHF-UCL.
DR GO; GO:0015026; F:coreceptor activity; TAS:ProtInc.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0001675; P:acrosome assembly; IEA:Ensembl.
DR GO; GO:0034332; P:adherens junction organization; TAS:Reactome.
DR GO; GO:0051856; P:adhesion to symbiont; IDA:BHF-UCL.
DR GO; GO:0034329; P:cell junction assembly; TAS:Reactome.
DR GO; GO:0032990; P:cell part morphogenesis; IEA:Ensembl.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0051654; P:establishment of mitochondrion localization; IEA:Ensembl.
DR GO; GO:0009566; P:fertilization; IEA:Ensembl.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IDA:BHF-UCL.
DR GO; GO:0007156; P:homophilic cell adhesion; IDA:BHF-UCL.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0002891; P:positive regulation of immunoglobulin mediated immune response; IMP:BHF-UCL.
DR GO; GO:0033005; P:positive regulation of mast cell activation; IMP:BHF-UCL.
DR GO; GO:0002860; P:positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; IMP:BHF-UCL.
DR GO; GO:0009615; P:response to virus; IEA:GOC.
DR GO; GO:0030382; P:sperm mitochondrion organization; IEA:Ensembl.
DR GO; GO:0007286; P:spermatid development; ISS:BHF-UCL.
DR GO; GO:0007289; P:spermatid nucleus differentiation; IEA:Ensembl.
DR GO; GO:0042271; P:susceptibility to natural killer cell mediated cytotoxicity; IMP:BHF-UCL.
DR GO; GO:0060370; P:susceptibility to T cell mediated cytotoxicity; IDA:BHF-UCL.
DR GO; GO:0046814; P:virion attachment, binding of host cell surface coreceptor; IDA:BHF-UCL.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Complete proteome; Disulfide bond; Glycoprotein;
KW Host cell receptor for virus entry; Host-virus interaction;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 31 Potential.
FT CHAIN 32 538 Poliovirus receptor-related protein 2.
FT /FTId=PRO_0000015136.
FT TOPO_DOM 32 360 Extracellular (Potential).
FT TRANSMEM 361 381 Helical; (Potential).
FT TOPO_DOM 382 538 Cytoplasmic (Potential).
FT DOMAIN 32 156 Ig-like V-type.
FT DOMAIN 162 256 Ig-like C2-type 1.
FT DOMAIN 261 345 Ig-like C2-type 2.
FT MOD_RES 433 433 Phosphoserine.
FT CARBOHYD 137 137 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 324 324 N-linked (GlcNAc...) (Potential).
FT DISULFID 54 140 By similarity.
FT DISULFID 183 238 By similarity.
FT DISULFID 283 329 By similarity.
FT VAR_SEQ 351 479 NTAGAGATGGIIGGIIAAIIATAVAATGILICRQQRKEQTL
FT QGAEEDEDLEGPPSYKPPTPKAKLEAQEMPSQLFTLGASEH
FT SPLKTPYFDAGASCTEQEMPRYHELPTLEERSGPLHPGATS
FT LGSPIP -> RASPRDVGPLVWGAVGGTLLVLLLLAGGSLA
FT FILLRVRRRRKSPGGAGGGASGDGGFYDPKAQVLGNGDPVF
FT WTPVVPGPMEPDGKDEEEEEEEEKAEKGLMLPPPPALEDDM
FT ESQLDGSLISRRAVYV (in isoform Alpha).
FT /FTId=VSP_002628.
FT VAR_SEQ 480 538 Missing (in isoform Alpha).
FT /FTId=VSP_002629.
FT MUTAGEN 89 89 M->F: Loss of entry of HHV-1/Rid1 and
FT HSV-2. No effect on PRV entry.
FT MUTAGEN 89 89 M->I: Increased entry of HHV-1/Rid1 and
FT HSV-2.
FT STRAND 35 37
FT STRAND 40 43
FT STRAND 50 52
FT STRAND 55 58
FT STRAND 64 71
FT HELIX 77 79
FT STRAND 81 86
FT TURN 87 89
FT STRAND 90 92
FT STRAND 95 98
FT HELIX 100 102
FT STRAND 103 107
FT TURN 113 115
FT STRAND 125 127
FT HELIX 132 134
FT STRAND 136 145
FT STRAND 148 157
SQ SEQUENCE 538 AA; 57742 MW; 3AE4F83E92F6F624 CRC64;
MARAAALLPS RSPPTPLLWP LLLLLLLETG AQDVRVQVLP EVRGQLGGTV ELPCHLLPPV
PGLYISLVTW QRPDAPANHQ NVAAFHPKMG PSFPSPKPGS ERLSFVSAKQ STGQDTEAEL
QDATLALHGL TVEDEGNYTC EFATFPKGSV RGMTWLRVIA KPKNQAEAQK VTFSQDPTTV
ALCISKEGRP PARISWLSSL DWEAKETQVS GTLAGTVTVT SRFTLVPSGR ADGVTVTCKV
EHESFEEPAL IPVTLSVRYP PEVSISGYDD NWYLGRTDAT LSCDVRSNPE PTGYDWSTTS
GTFPTSAVAQ GSQLVIHAVD SLFNTTFVCT VTNAVGMGRA EQVIFVRETP NTAGAGATGG
IIGGIIAAII ATAVAATGIL ICRQQRKEQT LQGAEEDEDL EGPPSYKPPT PKAKLEAQEM
PSQLFTLGAS EHSPLKTPYF DAGASCTEQE MPRYHELPTL EERSGPLHPG ATSLGSPIPV
PPGPPAVEDV SLDLEDEEGE EEEEYLDKIN PIYDALSYSS PSDSYQGKGF VMSRAMYV
//
MIM
600798
*RECORD*
*FIELD* NO
600798
*FIELD* TI
*600798 POLIOVIRUS RECEPTOR-LIKE 2; PVRL2
;;HERPESVIRUS ENTRY MEDIATOR B; HVEB;;
POLIOVIRUS RECEPTOR-RELATED 2; PVRR2; PRR2;;
read moreCD112 ANTIGEN; CD112;;
NECTIN 2
*FIELD* TX
CLONING
Entry of the poliovirus into permissive cells is dependent on the
expression of a specific receptor, the poliovirus receptor (PVR;
173850), which is an integral membrane glycoprotein. Its extracellular
region exhibits 3 immunoglobulin-like domains. Two integral forms,
PVR-alpha and PVR-delta, and 2 soluble forms, PVR-beta and PVR-gamma,
are lacking a transmembrane region generated by alternative splicing of
mRNA. The normal cellular function of PVR is unknown. The identification
of human PVR prompted study of its counterpart in other species. In the
monkey, 2 genes located at 2 separate genetic loci, AGM1 and AGM2, have
been cloned. AGM1 encodes 2 membrane-bound splice variant forms
homologous to PVR-alpha and PVR-delta. AGM2 encodes a membrane-bound
form, PVR-alpha-2. Morrison and Racaniello (1992) described a murine
gene, Mph, as a structural homolog of human PVR. Two Mph molecules,
Mph-alpha and Mph-beta, are thought to be generated by alternative
splicing from a primary transcript.
Following the discovery of the human PVR-related gene (PVRR1; 600644),
other PVR-related molecules were sought. Using degenerate
oligonucleotides in a PCR-based methodology, Eberle et al. (1995)
identified a second PVR-related cDNA, which they called PRR2.
Furthermore, they presented evidence that PRR2, and not PVR, is the
homolog of Mph, and questioned the existence of a true murine homolog of
PVR. The PRR2 gene encodes 2 glycoproteins, PRR2-alpha (short form) and
PRR2-delta (long form), which have 69% and 73% identity within Mph-alpha
and Mph-beta, respectively. In contrast, the human PVR protein exhibits
only 51% identity which is, moreover, restricted to the 3 immunoglobulin
domains of the murine protein. Northern blot analysis showed that 2 mRNA
isoforms of 3.0 kb (PRR2-alpha) and 4.4 kb (PRR2-delta) are ubiquitously
found in various normal human tissues.
GENE FUNCTION
Bottino et al. (2003) immunized mice with natural killer
(NK)-susceptible human target cells and obtained antibodies to PVR and
PVRL2. Binding analysis and flow cytometry demonstrated that both
molecules bound strongly with DNAM1 (CD226; 605397), but not with other
activating NK receptors, including NKp46 (NCR1; 604530) and NKp30 (NCR3;
611550). Expression of PVR or PVRL2 rendered cells susceptible to
enhanced lysis in a DNAM1-dependent manner that was nearly abrogated in
the presence of antibody to PVR, PVRL2, or DNAM1.
BIOCHEMICAL FEATURES
Liu et al. (2012) generated the crystal structure of the nectin-2
Ig-like V-set domain at 1.85-angstrom resolution. The structure bound to
both the soluble ectodomain of DNAM1 and cell surface-expressed
full-length DNAM1. Mutational analysis revealed that disruption of the
homodimeric interface of nectin-2 led to failure of homodimer formation
and loss of binding to DNAM1.
MAPPING
By isotopic hybridization, Eberle et al. (1995) mapped the PRR2 gene to
19q13.2-q13.4 in the same chromosomal region as PVR. By genomic sequence
analysis, Freitas et al. (1998) mapped the PRR2 gene to chromosome
19q13.2, where it lies centromeric to the TOMM40 gene (608061) and the
APOE (107741)-APOC2 (608083) gene cluster.
*FIELD* RF
1. Bottino, C.; Castriconi, R.; Pende, D.; Rivera, P.; Nanni, M.;
Carnemolla, B.; Cantoni, C.; Grassi, J.; Marcenaro, S.; Reymond, N.;
Vitale, M.; Moretta, L.; Lopez, M.; Moretta, A.: Identification of
PVR (CD155) and nectin-2 (CD112) as cell surface ligands for the human
DNAM-1 (CD226) activating molecule. J. Exp. Med. 198: 557-567, 2003.
2. Eberle, F.; Dubreuil, P.; Mattei, M.-G.; Devilard, E.; Lopez, M.
: The human PRR2 gene, related to the human poliovirus receptor gene
(PVR), is the true homolog of the murine Mph gene. Gene 159: 267-272,
1995.
3. Freitas, E. M.; Zhang, W. J.; Lalonde, J.-P.; Tay, G. K.; Gaudieri,
S.; Ashworth, L. K.; van Bockxmeer, F. M.; Dawkins, R. L.: Sequencing
of 42kb of the APO E-C2 gene cluster reveals a new gene: PEREC1. DNA
Seq. 9: 89-101, 1998.
4. Liu, J.; Qian, X.; Chen, Z.; Xu, X.; Gao, F.; Zhang, S.; Zhang,
R.; Qi, J.; Gao, G. F.; Yan, J.: Crystal structure of cell adhesion
molecule nectin-2/CD112 and its binding to immune receptor DNAM-1/CD226. J
Immun. 188: 5511-5520, 2012.
5. Morrison, M. E.; Racaniello, V. R.: Molecular cloning and expression
of a murine homolog of the human poliovirus receptor gene. J. Virol. 66:
2807-2813, 1992.
*FIELD* CN
Paul J. Converse - updated: 05/03/2013
Paul J. Converse - updated: 11/14/2005
Patricia A. Hartz - updated: 8/27/2003
*FIELD* CD
Victor A. McKusick: 9/27/1995
*FIELD* ED
mgross: 05/03/2013
carol: 4/6/2011
mgross: 10/24/2007
mgross: 4/5/2006
terry: 4/3/2006
mgross: 11/14/2005
terry: 11/14/2005
wwang: 9/28/2005
ckniffin: 9/24/2003
mgross: 8/27/2003
carol: 11/10/1999
carol: 8/12/1998
alopez: 6/8/1998
mark: 9/27/1995
*RECORD*
*FIELD* NO
600798
*FIELD* TI
*600798 POLIOVIRUS RECEPTOR-LIKE 2; PVRL2
;;HERPESVIRUS ENTRY MEDIATOR B; HVEB;;
POLIOVIRUS RECEPTOR-RELATED 2; PVRR2; PRR2;;
read moreCD112 ANTIGEN; CD112;;
NECTIN 2
*FIELD* TX
CLONING
Entry of the poliovirus into permissive cells is dependent on the
expression of a specific receptor, the poliovirus receptor (PVR;
173850), which is an integral membrane glycoprotein. Its extracellular
region exhibits 3 immunoglobulin-like domains. Two integral forms,
PVR-alpha and PVR-delta, and 2 soluble forms, PVR-beta and PVR-gamma,
are lacking a transmembrane region generated by alternative splicing of
mRNA. The normal cellular function of PVR is unknown. The identification
of human PVR prompted study of its counterpart in other species. In the
monkey, 2 genes located at 2 separate genetic loci, AGM1 and AGM2, have
been cloned. AGM1 encodes 2 membrane-bound splice variant forms
homologous to PVR-alpha and PVR-delta. AGM2 encodes a membrane-bound
form, PVR-alpha-2. Morrison and Racaniello (1992) described a murine
gene, Mph, as a structural homolog of human PVR. Two Mph molecules,
Mph-alpha and Mph-beta, are thought to be generated by alternative
splicing from a primary transcript.
Following the discovery of the human PVR-related gene (PVRR1; 600644),
other PVR-related molecules were sought. Using degenerate
oligonucleotides in a PCR-based methodology, Eberle et al. (1995)
identified a second PVR-related cDNA, which they called PRR2.
Furthermore, they presented evidence that PRR2, and not PVR, is the
homolog of Mph, and questioned the existence of a true murine homolog of
PVR. The PRR2 gene encodes 2 glycoproteins, PRR2-alpha (short form) and
PRR2-delta (long form), which have 69% and 73% identity within Mph-alpha
and Mph-beta, respectively. In contrast, the human PVR protein exhibits
only 51% identity which is, moreover, restricted to the 3 immunoglobulin
domains of the murine protein. Northern blot analysis showed that 2 mRNA
isoforms of 3.0 kb (PRR2-alpha) and 4.4 kb (PRR2-delta) are ubiquitously
found in various normal human tissues.
GENE FUNCTION
Bottino et al. (2003) immunized mice with natural killer
(NK)-susceptible human target cells and obtained antibodies to PVR and
PVRL2. Binding analysis and flow cytometry demonstrated that both
molecules bound strongly with DNAM1 (CD226; 605397), but not with other
activating NK receptors, including NKp46 (NCR1; 604530) and NKp30 (NCR3;
611550). Expression of PVR or PVRL2 rendered cells susceptible to
enhanced lysis in a DNAM1-dependent manner that was nearly abrogated in
the presence of antibody to PVR, PVRL2, or DNAM1.
BIOCHEMICAL FEATURES
Liu et al. (2012) generated the crystal structure of the nectin-2
Ig-like V-set domain at 1.85-angstrom resolution. The structure bound to
both the soluble ectodomain of DNAM1 and cell surface-expressed
full-length DNAM1. Mutational analysis revealed that disruption of the
homodimeric interface of nectin-2 led to failure of homodimer formation
and loss of binding to DNAM1.
MAPPING
By isotopic hybridization, Eberle et al. (1995) mapped the PRR2 gene to
19q13.2-q13.4 in the same chromosomal region as PVR. By genomic sequence
analysis, Freitas et al. (1998) mapped the PRR2 gene to chromosome
19q13.2, where it lies centromeric to the TOMM40 gene (608061) and the
APOE (107741)-APOC2 (608083) gene cluster.
*FIELD* RF
1. Bottino, C.; Castriconi, R.; Pende, D.; Rivera, P.; Nanni, M.;
Carnemolla, B.; Cantoni, C.; Grassi, J.; Marcenaro, S.; Reymond, N.;
Vitale, M.; Moretta, L.; Lopez, M.; Moretta, A.: Identification of
PVR (CD155) and nectin-2 (CD112) as cell surface ligands for the human
DNAM-1 (CD226) activating molecule. J. Exp. Med. 198: 557-567, 2003.
2. Eberle, F.; Dubreuil, P.; Mattei, M.-G.; Devilard, E.; Lopez, M.
: The human PRR2 gene, related to the human poliovirus receptor gene
(PVR), is the true homolog of the murine Mph gene. Gene 159: 267-272,
1995.
3. Freitas, E. M.; Zhang, W. J.; Lalonde, J.-P.; Tay, G. K.; Gaudieri,
S.; Ashworth, L. K.; van Bockxmeer, F. M.; Dawkins, R. L.: Sequencing
of 42kb of the APO E-C2 gene cluster reveals a new gene: PEREC1. DNA
Seq. 9: 89-101, 1998.
4. Liu, J.; Qian, X.; Chen, Z.; Xu, X.; Gao, F.; Zhang, S.; Zhang,
R.; Qi, J.; Gao, G. F.; Yan, J.: Crystal structure of cell adhesion
molecule nectin-2/CD112 and its binding to immune receptor DNAM-1/CD226. J
Immun. 188: 5511-5520, 2012.
5. Morrison, M. E.; Racaniello, V. R.: Molecular cloning and expression
of a murine homolog of the human poliovirus receptor gene. J. Virol. 66:
2807-2813, 1992.
*FIELD* CN
Paul J. Converse - updated: 05/03/2013
Paul J. Converse - updated: 11/14/2005
Patricia A. Hartz - updated: 8/27/2003
*FIELD* CD
Victor A. McKusick: 9/27/1995
*FIELD* ED
mgross: 05/03/2013
carol: 4/6/2011
mgross: 10/24/2007
mgross: 4/5/2006
terry: 4/3/2006
mgross: 11/14/2005
terry: 11/14/2005
wwang: 9/28/2005
ckniffin: 9/24/2003
mgross: 8/27/2003
carol: 11/10/1999
carol: 8/12/1998
alopez: 6/8/1998
mark: 9/27/1995