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Q15223 (PVRL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Poliovirus receptor-related protein 1
Alternative name(s):
Herpes virus entry mediator C
Short name=Herpesvirus entry mediator C
Short name=HveC
Herpesvirus Ig-like receptor
Short name=HIgR
Nectin-1
CD_antigen=CD111
Gene names
Name:PVRL1
Synonyms:HVEC, PRR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between PVRL1/nectin-1 and PVRL3/nectin-3 and between PVRL1/nectin-1 and PVRL4/nectin-4. Ref.1

Subunit structure

Can form trans-heterodimers with PVRL3/nectin-3 and with PVRL4/nectin-4. Interacts (via C-terminus) with afadin (via PDZ domain); this interaction recruits PVRL1 to cadherin-based adherens junctions. Interacts with integrin alphaV/beta3. Interacts with herpes simplex virus 1 (HHV-1), herpes simplex virus 2 (HHV-2), and pseudorabies virus (PRV) envelope glycoprotein D; functions as an entry receptor for these viruses. Ref.6 Ref.7 Ref.8 Ref.10

Subcellular location

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

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

Isoform Gamma: Secreted.

Involvement in disease

Ectodermal dysplasia, Margarita Island type (EDMI) [MIM:225060]: An autosomal recessive form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. It is a syndrome characterized by the association of cleft lip/palate, ectodermal dysplasia (sparse short and dry scalp hair, sparse eyebrows and eyelashes), and partial syndactyly of the fingers and/or toes. Two thirds of the patients do not manifest oral cleft but present with abnormal teeth and nails.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5

Non-syndromic orofacial cleft 7 (OFC7) [MIM:225060]: A birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5

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.

Sequence caution

The sequence CAA53980.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

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

Traceable author statement. Source: Reactome

cell junction assembly

Traceable author statement. Source: Reactome

desmosome organization

Inferred from electronic annotation. Source: Compara

enamel mineralization

Inferred from electronic annotation. Source: Compara

heterophilic cell-cell adhesion

Inferred from sequence or structural similarity. Source: HGNC

homophilic cell adhesion

Inferred from sequence or structural similarity. Source: HGNC

immune response

Non-traceable author statement Ref.5. Source: UniProtKB

iron ion transport

Inferred from electronic annotation. Source: Compara

lens morphogenesis in camera-type eye

Inferred from electronic annotation. Source: Compara

retina development in camera-type eye

Inferred from electronic annotation. Source: Compara

viral entry into host cell

Non-traceable author statement PubMed 12885915. Source: UniProtKB

   Cellular_componentcell-cell adherens junction

Inferred from direct assay Ref.7. Source: BHF-UCL

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Non-traceable author statement Ref.5. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functioncoreceptor activity

Traceable author statement Ref.2. Source: ProtInc

protein homodimerization activity

Inferred from sequence or structural similarity. Source: HGNC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PVRL3Q9NQS32EBI-1771314,EBI-2826725
PVRL4Q96NY82EBI-1771314,EBI-4314784

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Delta (identifier: Q15223-1)

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 Alpha (identifier: Q15223-2)

The sequence of this isoform differs from the canonical sequence as follows:
     336-458: FPYTPSPPEH...GERKVGGPHP → KPRPQRGLGS...RTTEPRGECP
     459-517: Missing.
Isoform Gamma (identifier: Q15223-3)

The sequence of this isoform differs from the canonical sequence as follows:
     335-352: EFPYTPSPPEHGRRAGPV → AFCQLIYPGKGRTRARMF
     353-517: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 517487Poliovirus receptor-related protein 1
PRO_0000015133

Regions

Topological domain31 – 355325Extracellular Potential
Transmembrane356 – 37621Helical; Potential
Topological domain377 – 517141Cytoplasmic Potential
Domain31 – 141111Ig-like V-type
Domain149 – 23890Ig-like C2-type 1
Domain247 – 33488Ig-like C2-type 2
Compositional bias437 – 4448Poly-Glu
Compositional bias445 – 4495Poly-Gly

Amino acid modifications

Modified residue4221Phosphoserine Ref.13
Modified residue4341Phosphoserine Ref.13
Modified residue4351Phosphoserine By similarity
Glycosylation361N-linked (GlcNAc...) Potential
Glycosylation721N-linked (GlcNAc...) Potential
Glycosylation1391N-linked (GlcNAc...) Potential
Glycosylation2021N-linked (GlcNAc...) Ref.9
Glycosylation2861N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Glycosylation3071N-linked (GlcNAc...) Potential
Glycosylation3321N-linked (GlcNAc...) Ref.11
Disulfide bond51 ↔ 124 By similarity
Disulfide bond172 ↔ 226 By similarity
Disulfide bond269 ↔ 316 By similarity

Natural variations

Alternative sequence335 – 35218EFPYT…RAGPV → AFCQLIYPGKGRTRARMF in isoform Gamma.
VSP_002624
Alternative sequence336 – 458123FPYTP…GGPHP → KPRPQRGLGSAARLLAGTVA VFLILVAVLTVFFLYNRQQK SPPETDGAGTDQPLSQKPEP SPSRQSSLVPEDIQVVHLDP GRQQQQEEEDLQKLSLQPPY YDLGVSPSYHPSVRTTEPRG ECP in isoform Alpha.
VSP_002626
Alternative sequence353 – 517165Missing in isoform Gamma.
VSP_002625
Alternative sequence459 – 51759Missing in isoform Alpha.
VSP_002627

Secondary structure

1 .......................................................... 517
Helix Strand Turn

Details...

Sequences

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

Last modified September 26, 2001. Version 3.
Checksum: DF34C8AEC893EE6D

FASTA51757,158
        10         20         30         40         50         60 
MARMGLAGAA GRWWGLALGL TAFFLPGVHS QVVQVNDSMY GFIGTDVVLH CSFANPLPSV 

        70         80         90        100        110        120 
KITQVTWQKS TNGSKQNVAI YNPSMGVSVL APYRERVEFL RPSFTDGTIR LSRLELEDEG 

       130        140        150        160        170        180 
VYICEFATFP TGNRESQLNL TVMAKPTNWI EGTQAVLRAK KGQDDKVLVA TCTSANGKPP 

       190        200        210        220        230        240 
SVVSWETRLK GEAEYQEIRN PNGTVTVISR YRLVPSREAH QQSLACIVNY HMDRFKESLT 

       250        260        270        280        290        300 
LNVQYEPEVT IEGFDGNWYL QRMDVKLTCK ADANPPATEY HWTTLNGSLP KGVEAQNRTL 

       310        320        330        340        350        360 
FFKGPINYSL AGTYICEATN PIGTRSGQVE VNITEFPYTP SPPEHGRRAG PVPTAIIGGV 

       370        380        390        400        410        420 
AGSILLVLIV VGGIVVALRR RRHTFKGDYS TKKHVYGNGY SKAGIPQHHP PMAQNLQYPD 

       430        440        450        460        470        480 
DSDDEKKAGP LGGSSYEEEE EEEEGGGGGE RKVGGPHPKY DEDAKRPYFT VDEAEARQDG 

       490        500        510 
YGDRTLGYQY DPEQLDLAEN MVSQNDGSFI SKKEWYV

« Hide

Isoform Alpha [UniParc].

Checksum: AB507515F86D7B45
Show »

FASTA45850,721
Isoform Gamma [UniParc].

Checksum: 2FB60588FA752D99
Show »

FASTA35239,150

References

« Hide 'large scale' references
[1]"cDNA characterization and chromosomal localization of a gene related to the poliovirus receptor gene."
Lopez M., Eberle F., Mattei M.-G., Gabert J., Bardin F., Maroc C., Dubreuil P.
Gene 155:261-265(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA), FUNCTION AS A RECEPTOR FOR HHV-1; HHV-2 AND PRV.
[2]"Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor."
Geraghty R.J., Krummenacher C., Cohen G.H., Eisenberg R.J., Spear P.G.
Science 280:1618-1620(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA).
[3]"Novel, soluble isoform of the herpes simplex virus (HSV) receptor nectin1 (or prr1-HIgR-Hvec) modulates positively and negatively susceptibility to hsv infection."
Lopez M., Cocchi F., Avitabile E., Leclerc A., Adelaide J., Campadelli-Fjume G., Dubreuil P.
J. Virol. 75:5684-5691(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA).
[4]"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 DELTA).
Tissue: Brain.
[5]"Mutations of PVRL1, encoding a cell-cell adhesion molecule/herpesvirus receptor, in cleft lip/palate-ectodermal dysplasia."
Suzuki K., Hu D., Bustos T., Zlotogora J., Richieri-Costa A., Helms J.A., Spritz R.A.
Nat. Genet. 25:427-430(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-517 (ISOFORMS ALPHA AND DELTA), DISEASE.
[6]"Herpes simplex virus glycoprotein D can bind to poliovirus receptor-related protein 1 or herpesvirus entry mediator, two structurally unrelated mediators of virus entry."
Krummenacher C., Nicola A.V., Whitbeck J.C., Lou H., Hou W., Lambris J.D., Geraghty R.J., Spear P.G., Cohen G.H., Eisenberg R.J.
J. Virol. 72:7064-7074(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HHV-1 AND HHV-2 GLYCOPROTEIN D.
[7]"Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein."
Takahashi K., Nakanishi H., Miyahara M., Mandai K., Satoh K., Satoh A., Nishioka H., Aoki J., Nomoto A., Mizoguchi A., Takai Y.
J. Cell Biol. 145:539-549(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AFADIN.
[8]"Nectin4/PRR4, a new afadin-associated member of the nectin family that trans-interacts with nectin1/PRR1 through V domain interaction."
Reymond N., Fabre S., Lecocq E., Adelaide J., Dubreuil P., Lopez M.
J. Biol. Chem. 276:43205-43215(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PVRL3 AND PVRL4.
[9]"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-202, MASS SPECTROMETRY.
Tissue: Plasma.
[10]"Interaction of integrin alpha(v)beta3 with nectin. Implication in cross-talk between cell-matrix and cell-cell junctions."
Sakamoto Y., Ogita H., Hirota T., Kawakatsu T., Fukuyama T., Yasumi M., Kanzaki N., Ozaki M., Takai Y.
J. Biol. Chem. 281:19631-19644(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INTEGRIN ITGAV/ITGB3.
[11]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-332, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422 AND SER-434, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X76400 mRNA. Translation: CAA53980.2. Different initiation.
AF060231 mRNA. Translation: AAC23798.1.
AY029539 mRNA. Translation: AAK33124.1.
BC104948 mRNA. Translation: AAI04949.1.
BC113471 mRNA. Translation: AAI13472.1.
AF252867 expand/collapse EMBL AC list , AF196768, AF196769, AF196770, AF196771 Genomic DNA. Translation: AAG16648.1.
AF196774 expand/collapse EMBL AC list , AF196768, AF196769, AF196770, AF196771, AF196772, AF196773 Genomic DNA. Translation: AAG16649.1.
IPIIPI00003648.
IPI00218887.
IPI00218888.
PIRJC4024.
RefSeqNP_002846.3. NM_002855.4.
NP_976030.1. NM_203285.1.
NP_976031.1. NM_203286.1.
UniGeneHs.334846.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ALPX-ray2.80A/B30-335[»]
3SKUX-ray4.00D/E/F31-345[»]
3U82X-ray3.16B30-335[»]
3U83X-ray2.50A30-335[»]
4FMFX-ray3.20A/B/C/D31-337[»]
ProteinModelPortalQ15223.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-40302N.
IntActQ15223. 2 interactions.
MINTMINT-90873.
STRING9606.ENSP00000264025.

Protein family/group databases

MEROPSI43.001.

PTM databases

PhosphoSiteQ15223.

Polymorphism databases

DMDM18202503.

Proteomic databases

PaxDbQ15223.
PeptideAtlasQ15223.
PRIDEQ15223.

Protocols and materials databases

DNASU5818.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264025; ENSP00000264025; ENSG00000110400.
ENST00000340882; ENSP00000345289; ENSG00000110400.
ENST00000341398; ENSP00000344974; ENSG00000110400.
GeneID5818.
KEGGhsa:5818.
UCSCuc001pwu.1. human.
uc001pwv.3. human.
uc001pww.3. human.

Organism-specific databases

CTD5818.
GeneCardsGC11M119542.
HGNCHGNC:9706. PVRL1.
HPACAB016135.
HPA026846.
MIM225060. phenotype.
600644. gene.
neXtProtNX_Q15223.
Orphanet1991. Cleft lip with or without cleft palate.
3253. Zlotogora-Ogur syndrome.
PharmGKBPA34051.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG147558.
HOGENOMHOG000115804.
HOVERGENHBG100542.
InParanoidQ15223.
KOK06081.
OMASPYKERV.
PhylomeDBQ15223.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpressQ15223.
BgeeQ15223.
CleanExHS_PVRL1.
GenevestigatorQ15223.
GermOnlineENSG00000110400. Homo sapiens.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR003596. Ig_V-set_subgr.
[Graphical view]
PfamPF08205. C2-set_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPVRL1. human.
EvolutionaryTraceQ15223.
GenomeRNAi5818.
NextBio22658.
PMAP-CutDBQ15223.
SOURCESearch...

Entry information

Entry namePVRL1_HUMAN
AccessionPrimary (citable) accession number: Q15223
Secondary accession number(s): O75465 expand/collapse secondary AC list , Q2M3D3, Q9HBE6, Q9HBW2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: May 1, 2013
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents