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Protein

Nectin-3

Gene

PVRL3

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

Functioni

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.1 Publication

GO - Molecular functioni

  1. cell adhesion molecule binding Source: BHF-UCL
  2. protein homodimerization activity Source: HGNC

GO - Biological processi

  1. adherens junction organization Source: Reactome
  2. cell-cell junction organization Source: Reactome
  3. cell junction assembly Source: Reactome
  4. fertilization Source: Ensembl
  5. homophilic cell adhesion via plasma membrane adhesion molecules Source: HGNC
  6. lens morphogenesis in camera-type eye Source: Ensembl
  7. retina morphogenesis in camera-type eye Source: Ensembl
  8. single organismal cell-cell adhesion Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_19195. Adherens junctions interactions.
REACT_19268. Nectin/Necl trans heterodimerization.

Protein family/group databases

MEROPSiI43.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Nectin-3
Alternative name(s):
CDw113
Poliovirus receptor-related protein 3
CD_antigen: CD113
Gene namesi
Name:PVRL3
Synonyms:PRR3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:17664. PVRL3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini58 – 404347ExtracellularSequence AnalysisAdd
BLAST
Transmembranei405 – 42521HelicalSequence AnalysisAdd
BLAST
Topological domaini426 – 549124CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. apical junction complex Source: Ensembl
  2. cell-cell adherens junction Source: Ensembl
  3. integral component of membrane Source: UniProtKB-KW
  4. plasma membrane Source: HGNC
  5. postsynaptic membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134969621.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5757Sequence AnalysisAdd
BLAST
Chaini58 – 549492Nectin-3PRO_0000226372Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi73 – 731N-linked (GlcNAc...)1 Publication
Disulfide bondi78 ↔ 148PROSITE-ProRule annotation
Glycosylationi83 – 831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi125 – 1251N-linked (GlcNAc...)1 Publication
Glycosylationi186 – 1861N-linked (GlcNAc...)1 Publication
Disulfide bondi193 ↔ 246PROSITE-ProRule annotation
Glycosylationi222 – 2221N-linked (GlcNAc...)1 Publication
Disulfide bondi291 ↔ 338PROSITE-ProRule annotation
Glycosylationi331 – 3311N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9NQS3.
PaxDbiQ9NQS3.
PRIDEiQ9NQS3.

PTM databases

PhosphoSiteiQ9NQS3.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9NQS3.
CleanExiHS_PRR3.
HS_PVRL3.
ExpressionAtlasiQ9NQS3. baseline and differential.
GenevestigatoriQ9NQS3.

Organism-specific databases

HPAiCAB009869.
HPA011038.
HPA052242.

Interactioni

Subunit structurei

Cis- and trans-homodimer. Can form trans-heterodimers with PVRL1/nectin-1, PVRL2/nectin-2, PVR, IGSF4B/Necl-1 and with IGSF4. Interaction between PVRL1 and PVRL3 on the pre- and postsynaptic sites, respectively, initiates the formation of puncta adherentia junctions between axons and dendrites. Interacts (via Cytoplasmic domain) with MLLT4/afadin, providing a connection with the actin cytoskeleton. Binds with low affinity to TIGIT.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PVRL1Q152232EBI-2826725,EBI-1771314
PVRL2Q926923EBI-2826725,EBI-718419
TIGITQ495A12EBI-2826725,EBI-4314807

Protein-protein interaction databases

BioGridi117441. 25 interactions.
DIPiDIP-41491N.
IntActiQ9NQS3. 5 interactions.
MINTiMINT-147327.
STRINGi9606.ENSP00000418070.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FOMX-ray3.93A58-359[»]
ProteinModelPortaliQ9NQS3.
SMRiQ9NQS3. Positions 58-359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini59 – 165107Ig-like V-typeAdd
BLAST
Domaini170 – 25889Ig-like C2-type 1Add
BLAST
Domaini269 – 35486Ig-like C2-type 2Add
BLAST

Sequence similaritiesi

Belongs to the nectin family.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG47602.
GeneTreeiENSGT00770000120512.
HOGENOMiHOG000115805.
HOVERGENiHBG082234.
InParanoidiQ9NQS3.
KOiK06592.
OMAiSAGNDER.
OrthoDBiEOG73RBB5.
PhylomeDBiQ9NQS3.
TreeFamiTF331051.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF08205. C2-set_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NQS3-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MARTLRPSPL CPGGGKAQLS SASLLGAGLL LQPPTPPPLL LLLFPLLLFS
60 70 80 90 100
RLCGALAGPI IVEPHVTAVW GKNVSLKCLI EVNETITQIS WEKIHGKSSQ
110 120 130 140 150
TVAVHHPQYG FSVQGEYQGR VLFKNYSLND ATITLHNIGF SDSGKYICKA
160 170 180 190 200
VTFPLGNAQS STTVTVLVEP TVSLIKGPDS LIDGGNETVA AICIAATGKP
210 220 230 240 250
VAHIDWEGDL GEMESTTTSF PNETATIISQ YKLFPTRFAR GRRITCVVKH
260 270 280 290 300
PALEKDIRYS FILDIQYAPE VSVTGYDGNW FVGRKGVNLK CNADANPPPF
310 320 330 340 350
KSVWSRLDGQ WPDGLLASDN TLHFVHPLTF NYSGVYICKV TNSLGQRSDQ
360 370 380 390 400
KVIYISDPPT TTTLQPTIQW HPSTADIEDL ATEPKKLPFP LSTLATIKDD
410 420 430 440 450
TIATIIASVV GGALFIVLVS VLAGIFCYRR RRTFRGDYFA KNYIPPSDMQ
460 470 480 490 500
KESQIDVLQQ DELDSYPDSV KKENKNPVNN LIRKDYLEEP EKTQWNNVEN
510 520 530 540
LNRFERPMDY YEDLKMGMKF VSDEHYDENE DDLVSHVDGS VISRREWYV
Length:549
Mass (Da):61,002
Last modified:October 1, 2000 - v1
Checksum:i6D1104CCB4A9D731
GO
Isoform 2 (identifier: Q9NQS3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     357-366: DPPTTTTLQP → AYNSVASLNC
     367-549: Missing.

Note: No experimental confirmation available.

Show »
Length:366
Mass (Da):39,692
Checksum:i091C0A4640DB8661
GO
Isoform 3 (identifier: Q9NQS3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: MARTLRPSPL...PLLLFSRLCG → MAEGWRWCFVRRTPGLLRGPLLPRSFSGNPR
     357-549: DPPTTTTLQP...SVISRREWYV → DVPFKQTSSI...VYIDPREHYV

Show »
Length:487
Mass (Da):54,375
Checksum:iA59BE81140C93511
GO

Sequence cautioni

The sequence AAH17572.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
Isoform 3 : The sequence BAC11404.1 differs from that shown. Reason: Erroneous termination at position 268. Translated as Cys.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511P → Q in AAH67808. (PubMed:15489334)Curated
Sequence conflicti284 – 2841R → G in BAC11404. (PubMed:14702039)Curated
Sequence conflicti386 – 3861K → E in AAH17572. (PubMed:15489334)Curated
Sequence conflicti465 – 4651S → P in CAB43256. (PubMed:17974005)Curated
Sequence conflicti519 – 5191K → R in CAB43256. (PubMed:17974005)Curated
Sequence conflicti548 – 5481Y → C in CAB43256. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti432 – 4321R → L.
Corresponds to variant rs15611 [ dbSNP | Ensembl ].
VAR_049995

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5454MARTL…SRLCG → MAEGWRWCFVRRTPGLLRGP LLPRSFSGNPR in isoform 3. 1 PublicationVSP_046893Add
BLAST
Alternative sequencei357 – 549193DPPTT…REWYV → DVPFKQTSSIAVAGAVIGAV LALFIIAIFVTVLLTPRKKR PSYLDKVIDLPPTHKPPPLY EERSPPLPQKDLFQPEHLPL QTQFKEREVGNLQHSNGLNS RSFDYEDENPVGEDGIQQMY PLYNQMCYQDRSPGKHHQNN DPKRVYIDPREHYV in isoform 3. 1 PublicationVSP_046894Add
BLAST
Alternative sequencei357 – 36610DPPTTTTLQP → AYNSVASLNC in isoform 2. 1 PublicationVSP_017435
Alternative sequencei367 – 549183Missing in isoform 2. 1 PublicationVSP_017436Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2957.1. [Q9NQS3-1]
CCDS58842.1. [Q9NQS3-2]
CCDS58843.1. [Q9NQS3-3]
PIRiT08732.
RefSeqiNP_001230215.1. NM_001243286.1. [Q9NQS3-2]
NP_001230217.1. NM_001243288.1. [Q9NQS3-3]
NP_056295.1. NM_015480.2. [Q9NQS3-1]
UniGeneiHs.293917.

Genome annotation databases

EnsembliENST00000319792; ENSP00000321514; ENSG00000177707. [Q9NQS3-2]
ENST00000485303; ENSP00000418070; ENSG00000177707. [Q9NQS3-1]
ENST00000493615; ENSP00000420579; ENSG00000177707. [Q9NQS3-3]
GeneIDi25945.
KEGGihsa:25945.
UCSCiuc003dxt.2. human. [Q9NQS3-1]
uc021xch.1. human. [Q9NQS3-2]

Polymorphism databases

DMDMi74762752.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2957.1. [Q9NQS3-1]
CCDS58842.1. [Q9NQS3-2]
CCDS58843.1. [Q9NQS3-3]
PIRiT08732.
RefSeqiNP_001230215.1. NM_001243286.1. [Q9NQS3-2]
NP_001230217.1. NM_001243288.1. [Q9NQS3-3]
NP_056295.1. NM_015480.2. [Q9NQS3-1]
UniGeneiHs.293917.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FOMX-ray3.93A58-359[»]
ProteinModelPortaliQ9NQS3.
SMRiQ9NQS3. Positions 58-359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117441. 25 interactions.
DIPiDIP-41491N.
IntActiQ9NQS3. 5 interactions.
MINTiMINT-147327.
STRINGi9606.ENSP00000418070.

Protein family/group databases

MEROPSiI43.001.

PTM databases

PhosphoSiteiQ9NQS3.

Polymorphism databases

DMDMi74762752.

Proteomic databases

MaxQBiQ9NQS3.
PaxDbiQ9NQS3.
PRIDEiQ9NQS3.

Protocols and materials databases

DNASUi25945.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000319792; ENSP00000321514; ENSG00000177707. [Q9NQS3-2]
ENST00000485303; ENSP00000418070; ENSG00000177707. [Q9NQS3-1]
ENST00000493615; ENSP00000420579; ENSG00000177707. [Q9NQS3-3]
GeneIDi25945.
KEGGihsa:25945.
UCSCiuc003dxt.2. human. [Q9NQS3-1]
uc021xch.1. human. [Q9NQS3-2]

Organism-specific databases

CTDi25945.
GeneCardsiGC03P110788.
HGNCiHGNC:17664. PVRL3.
HPAiCAB009869.
HPA011038.
HPA052242.
MIMi607147. gene.
neXtProtiNX_Q9NQS3.
PharmGKBiPA134969621.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG47602.
GeneTreeiENSGT00770000120512.
HOGENOMiHOG000115805.
HOVERGENiHBG082234.
InParanoidiQ9NQS3.
KOiK06592.
OMAiSAGNDER.
OrthoDBiEOG73RBB5.
PhylomeDBiQ9NQS3.
TreeFamiTF331051.

Enzyme and pathway databases

ReactomeiREACT_19195. Adherens junctions interactions.
REACT_19268. Nectin/Necl trans heterodimerization.

Miscellaneous databases

ChiTaRSiPVRL3. human.
GeneWikiiPVRL3.
GenomeRNAii25945.
NextBioi47534.
PROiQ9NQS3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NQS3.
CleanExiHS_PRR3.
HS_PVRL3.
ExpressionAtlasiQ9NQS3. baseline and differential.
GenevestigatoriQ9NQS3.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF08205. C2-set_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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.

Entry informationi

Entry nameiPVRL3_HUMAN
AccessioniPrimary (citable) accession number: Q9NQS3
Secondary accession number(s): E9PFR0
, Q6NVZ3, Q8NC05, Q8WVU4, Q9BVA9, Q9Y412
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: October 1, 2000
Last modified: February 4, 2015
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.