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Q9NQS3 (PVRL3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Poliovirus receptor-related protein 3
Alternative name(s):
CDw113
Nectin-3
CD_antigen=CD113
Gene names
Name:PVRL3
Synonyms:PRR3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length549 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in cell-cell adhesion through heterophilic trans-interactions with nectin-like proteins or nectins, such as trans-interaction with PVRL2/nectin-2 at Sertoli-spermatid junctions. Trans-interaction with PVR induces activation of CDC42 and RAC small G proteins through common signaling molecules such as SRC and RAP1. Also involved in the formation of cell-cell junctions, including adherens junctions and synapses. Induces endocytosis-mediated down-regulation of PVR from the cell surface, resulting in reduction of cell movement and proliferation. Plays a role in the morphology of the ciliary body. Ref.7

Subunit structure

Cis- and trans-homodimer. Can form trans-heterodimers with PVRL1/nectin-1, PVRL2/nectin-2, PVR, IGSF4B/Necl-1 and with IGSF4. Interacts with MLLT4/afadin. Binds with low affinity to TIGIT. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9

Subcellular location

Cell membrane; Single-pass membrane protein Potential.

Tissue specificity

Predominantly expressed in testis and placenta as well as in many cell lines, including epithelial cell lines. Ref.1

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 AAH17572.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NQS3-1)

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 2 (identifier: Q9NQS3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     357-366: DPPTTTTLQP → AYNSVASLNC
     367-549: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9NQS3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: MARTLRPSPL...PLLLFSRLCG → MAEGWRWCFVRRTPGLLRGPLLPRSFSGNPR
     357-549: DPPTTTTLQP...SVISRREWYV → DVPFKQTSSI...VYIDPREHYV
Note: Ref.2 (BAC11404) sequence differs from that shown at position 268 due to erroneous termination (Translated as Cys).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 5757 Potential
Chain58 – 549492Poliovirus receptor-related protein 3
PRO_0000226372

Regions

Topological domain58 – 404347Extracellular Potential
Transmembrane405 – 42521Helical; Potential
Topological domain426 – 549124Cytoplasmic Potential
Domain59 – 165107Ig-like V-type
Domain170 – 25889Ig-like C2-type 1
Domain269 – 35486Ig-like C2-type 2

Amino acid modifications

Glycosylation731N-linked (GlcNAc...) Ref.9
Glycosylation831N-linked (GlcNAc...) Potential
Glycosylation1251N-linked (GlcNAc...) Ref.9
Glycosylation1861N-linked (GlcNAc...) Ref.9
Glycosylation2221N-linked (GlcNAc...) Ref.9
Glycosylation3311N-linked (GlcNAc...) Ref.9
Disulfide bond78 ↔ 148 By similarity
Disulfide bond193 ↔ 246 By similarity
Disulfide bond291 ↔ 338 By similarity

Natural variations

Alternative sequence1 – 5454MARTL…SRLCG → MAEGWRWCFVRRTPGLLRGP LLPRSFSGNPR in isoform 3.
VSP_046893
Alternative sequence357 – 549193DPPTT…REWYV → DVPFKQTSSIAVAGAVIGAV LALFIIAIFVTVLLTPRKKR PSYLDKVIDLPPTHKPPPLY EERSPPLPQKDLFQPEHLPL QTQFKEREVGNLQHSNGLNS RSFDYEDENPVGEDGIQQMY PLYNQMCYQDRSPGKHHQNN DPKRVYIDPREHYV in isoform 3.
VSP_046894
Alternative sequence357 – 36610DPPTTTTLQP → AYNSVASLNC in isoform 2.
VSP_017435
Alternative sequence367 – 549183Missing in isoform 2.
VSP_017436
Natural variant4321R → L.
Corresponds to variant rs15611 [ dbSNP | Ensembl ].
VAR_049995

Experimental info

Sequence conflict2511P → Q in AAH67808. Ref.4
Sequence conflict2841R → G in BAC11404. Ref.2
Sequence conflict3861K → E in AAH17572. Ref.4
Sequence conflict4651S → P in CAB43256. Ref.5
Sequence conflict5191K → R in CAB43256. Ref.5
Sequence conflict5481Y → C in CAB43256. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 6D1104CCB4A9D731

FASTA54961,002
        10         20         30         40         50         60 
MARTLRPSPL CPGGGKAQLS SASLLGAGLL LQPPTPPPLL LLLFPLLLFS RLCGALAGPI 

        70         80         90        100        110        120 
IVEPHVTAVW GKNVSLKCLI EVNETITQIS WEKIHGKSSQ TVAVHHPQYG FSVQGEYQGR 

       130        140        150        160        170        180 
VLFKNYSLND ATITLHNIGF SDSGKYICKA VTFPLGNAQS STTVTVLVEP TVSLIKGPDS 

       190        200        210        220        230        240 
LIDGGNETVA AICIAATGKP VAHIDWEGDL GEMESTTTSF PNETATIISQ YKLFPTRFAR 

       250        260        270        280        290        300 
GRRITCVVKH PALEKDIRYS FILDIQYAPE VSVTGYDGNW FVGRKGVNLK CNADANPPPF 

       310        320        330        340        350        360 
KSVWSRLDGQ WPDGLLASDN TLHFVHPLTF NYSGVYICKV TNSLGQRSDQ KVIYISDPPT 

       370        380        390        400        410        420 
TTTLQPTIQW HPSTADIEDL ATEPKKLPFP LSTLATIKDD TIATIIASVV GGALFIVLVS 

       430        440        450        460        470        480 
VLAGIFCYRR RRTFRGDYFA KNYIPPSDMQ KESQIDVLQQ DELDSYPDSV KKENKNPVNN 

       490        500        510        520        530        540 
LIRKDYLEEP EKTQWNNVEN LNRFERPMDY YEDLKMGMKF VSDEHYDENE DDLVSHVDGS 


VISRREWYV 

« Hide

Isoform 2 [UniParc].

Checksum: 091C0A4640DB8661
Show »

FASTA36639,692
Isoform 3 [UniParc].

Checksum: A59BE81140C93511
Show »

FASTA48754,375

References

« Hide 'large scale' references
[1]"Human nectin3/PRR3: a novel member of the PVR/PRR/nectin family that interacts with afadin."
Reymond N., Borg J.-P., Lecocq E., Adelaide J., Campadelli-Fiume G., Dubreuil P., Lopez M.
Gene 255:347-355(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH MLLT4.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Placenta.
[3]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 246-549 (ISOFORM 1).
Tissue: Brain, Cervix and Kidney.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 143-549 (ISOFORM 1).
Tissue: Fetal kidney.
[6]"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 PVR.
[7]"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: FUNCTION, INTERACTION WITH PVR.
[8]"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.
[9]"Nectin ectodomain structures reveal a canonical adhesive interface."
Harrison O.J., Vendome J., Brasch J., Jin X., Hong S., Katsamba P.S., Ahlsen G., Troyanovsky R.B., Troyanovsky S.M., Honig B., Shapiro L.
Nat. Struct. Mol. Biol. 19:906-915(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.93 ANGSTROMS) OF 58-359, SUBUNIT, GLYCOSYLATION AT ASN-73; ASN-125; ASN-186; ASN-222 AND ASN-331, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF282874 mRNA. Translation: AAF97597.1.
AK075105 mRNA. Translation: BAC11404.1. Different termination.
AC133436 Genomic DNA. No translation available.
AC133477 Genomic DNA. No translation available.
AC137833 Genomic DNA. No translation available.
BC001336 mRNA. Translation: AAH01336.1.
BC017572 mRNA. Translation: AAH17572.1. Different initiation.
BC067808 mRNA. Translation: AAH67808.1.
AL050071 mRNA. Translation: CAB43256.1.
PIRT08732.
RefSeqNP_001230215.1. NM_001243286.1.
NP_001230217.1. NM_001243288.1.
NP_056295.1. NM_015480.2.
UniGeneHs.293917.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4FOMX-ray3.93A58-359[»]
ProteinModelPortalQ9NQS3.
SMRQ9NQS3. Positions 58-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117441. 9 interactions.
DIPDIP-41491N.
IntActQ9NQS3. 5 interactions.
MINTMINT-147327.
STRING9606.ENSP00000418070.

Protein family/group databases

MEROPSI43.001.

PTM databases

PhosphoSiteQ9NQS3.

Polymorphism databases

DMDM74762752.

Proteomic databases

PaxDbQ9NQS3.
PRIDEQ9NQS3.

Protocols and materials databases

DNASU25945.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319792; ENSP00000321514; ENSG00000177707. [Q9NQS3-2]
ENST00000485303; ENSP00000418070; ENSG00000177707. [Q9NQS3-1]
ENST00000493615; ENSP00000420579; ENSG00000177707. [Q9NQS3-3]
GeneID25945.
KEGGhsa:25945.
UCSCuc003dxt.2. human. [Q9NQS3-1]
uc021xch.1. human. [Q9NQS3-2]

Organism-specific databases

CTD25945.
GeneCardsGC03P110788.
HGNCHGNC:17664. PVRL3.
HPACAB009869.
HPA011038.
HPA052242.
MIM607147. gene.
neXtProtNX_Q9NQS3.
PharmGKBPA134969621.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47602.
HOGENOMHOG000115805.
HOVERGENHBG082234.
InParanoidQ9NQS3.
KOK06592.
OMADVPFKQT.
OrthoDBEOG73RBB5.
PhylomeDBQ9NQS3.
TreeFamTF331051.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpressQ9NQS3.
BgeeQ9NQS3.
CleanExHS_PRR3.
HS_PVRL3.
GenevestigatorQ9NQS3.

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.
[Graphical view]
PfamPF08205. C2-set_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPVRL3. human.
GeneWikiPVRL3.
GenomeRNAi25945.
NextBio47534.
PROQ9NQS3.
SOURCESearch...

Entry information

Entry namePVRL3_HUMAN
AccessionPrimary (citable) accession number: Q9NQS3
Secondary accession number(s): E9PFR0 expand/collapse secondary AC list , Q6NVZ3, Q8NC05, Q8WVU4, Q9BVA9, Q9Y412
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Human cell differentiation molecules

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