Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nectin-1

Gene

NECTIN1

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

Functioni

Promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between NECTIN1 and NECTIN3 and between NECTIN1 and NECTIN4. Has some neurite outgrowth-promoting activity.1 Publication
(Microbial infection) Acts as a receptor for herpes simplex virus 1/HHV-1, herpes simplex virus 2/HHV-2, and pseudorabies virus/PRV.2 Publications

GO - Molecular functioni

  • carbohydrate binding Source: Ensembl
  • cell adhesion molecule binding Source: BHF-UCL
  • coreceptor activity Source: ProtInc
  • identical protein binding Source: IntAct
  • protein heterodimerization activity Source: Ensembl
  • protein homodimerization activity Source: HGNC
  • signaling receptor activity Source: GO_Central
  • virion binding Source: Ensembl
  • virus receptor activity Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Molecular functionHost cell receptor for virus entry, Receptor
Biological processCell adhesion, Host-virus interaction

Enzyme and pathway databases

ReactomeiR-HSA-418990 Adherens junctions interactions
R-HSA-420597 Nectin/Necl trans heterodimerization

Names & Taxonomyi

Protein namesi
Recommended name:
Nectin-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 cell adhesion molecule 1Imported
Poliovirus receptor-related protein 1
CD_antigen: CD111
Gene namesi
Name:NECTIN1Imported
Synonyms:HVEC, PRR1, PVRL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000110400.10
HGNCiHGNC:9706 NECTIN1
MIMi600644 gene
neXtProtiNX_Q15223

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini31 – 355ExtracellularSequence analysisAdd BLAST325
Transmembranei356 – 376HelicalSequence analysisAdd BLAST21
Topological domaini377 – 517CytoplasmicSequence analysisAdd BLAST141

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Secreted, Synapse

Pathology & Biotechi

Involvement in diseasei

Ectodermal dysplasia, Margarita Island type (EDMI)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:225060
Non-syndromic orofacial cleft 7 (OFC7)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:225060

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi82N → Y: Impairs interaction with herpes simplex glycoprotein D. Decreases susceptibility to infection by herpes simplex virus. 1 Publication1
Mutagenesisi84S → Y: Impairs interaction with herpes simplex glycoprotein D. Decreases susceptibility to infection by herpes simplex virus. 1 Publication1
Mutagenesisi129F → A or S: Impairs interaction with herpes simplex glycoprotein D. Decreases susceptibility to infection by herpes simplex virus. 1 Publication1

Keywords - Diseasei

Ectodermal dysplasia

Organism-specific databases

DisGeNETi5818
MalaCardsiNECTIN1
MIMi225060 phenotype
OpenTargetsiENSG00000110400
Orphaneti141291 Cleft lip and alveolus
199306 Cleft lip/palate
199302 Isolated cleft lip
3253 Zlotogora-Ogur syndrome
PharmGKBiPA34051

Polymorphism and mutation databases

BioMutaiPVRL1
DMDMi18202503

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
ChainiPRO_000001513331 – 517Nectin-1Add BLAST487

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi36N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi51 ↔ 1241 Publication2 Publications
Glycosylationi72N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi139N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi172 ↔ 2261 Publication2 Publications
Glycosylationi202N-linked (GlcNAc...) (complex) asparagine4 Publications1
Disulfide bondi269 ↔ 3161 Publication2 Publications
Glycosylationi286N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi297N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi307N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi332N-linked (GlcNAc...) asparagine1 Publication1
Modified residuei422PhosphoserineCombined sources1
Modified residuei434PhosphoserineCombined sources1
Modified residuei435PhosphoserineBy similarity1
Modified residuei436PhosphotyrosineBy similarity1
Modified residuei511PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ15223
MaxQBiQ15223
PaxDbiQ15223
PeptideAtlasiQ15223
PRIDEiQ15223
ProteomicsDBi60490
60491 [Q15223-2]
60492 [Q15223-3]

PTM databases

GlyConnecti1536
iPTMnetiQ15223
PhosphoSitePlusiQ15223

Miscellaneous databases

PMAP-CutDBiQ15223

Expressioni

Gene expression databases

BgeeiENSG00000110400 Expressed in 205 organ(s), highest expression level in esophagus mucosa
CleanExiHS_PVRL1
GenevisibleiQ15223 HS

Organism-specific databases

HPAiCAB016135
HPA026846

Interactioni

Subunit structurei

Interacts (via Ig-like C2-type domain 2) with FGFR1, FGFR2 and FGFR3 (By similarity). Cis- and trans-homodimer. Can form trans-heterodimers with NECTIN3 and with NECTIN4. Interaction between NECTIN1 and NECTIN3 on the pre- and postsynaptic sites, respectively, initiates the formation of puncta adherentia junctions between axons and dendrites. Interacts (via cytoplasmic domain) with AFDN (via PDZ domain); this interaction recruits NECTIN1 to cadherin-based adherens junctions and provides a connection with the actin cytoskeleton. Interacts with integrin alphaV/beta3.By similarity4 Publications
(Microbial infection) Interacts with herpes simplex virus 1/HHV-1, herpes simplex virus 2/HHV-2, and pseudorabies virus/PRV envelope glycoprotein D (PubMed:21980294, PubMed:22146396, PubMed:9696799, PubMed:9657005).4 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi111776, 10 interactors
CORUMiQ15223
DIPiDIP-40302N
IntActiQ15223, 11 interactors
MINTiQ15223
STRINGi9606.ENSP00000264025

Structurei

Secondary structure

1517
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ15223
SMRiQ15223
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15223

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 141Ig-like V-typeAdd BLAST111
Domaini149 – 238Ig-like C2-type 1Add BLAST90
Domaini247 – 334Ig-like C2-type 2Add BLAST88

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni282 – 299Interaction with FGFRBy similarityAdd BLAST18

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi437 – 444Poly-Glu8
Compositional biasi445 – 449Poly-Gly5

Domaini

Ig-like C2-type 2 mediates neurite outgrowth through binding, induction of phosphorylation, and activation of FGFR.By similarity

Sequence similaritiesi

Belongs to the nectin family.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IF17 Eukaryota
ENOG410YK75 LUCA
GeneTreeiENSGT00900000140811
HOGENOMiHOG000115804
HOVERGENiHBG100542
InParanoidiQ15223
KOiK06081
OMAiTCVTTYN
OrthoDBiEOG091G0BLQ
PhylomeDBiQ15223
TreeFamiTF331051

Family and domain databases

Gene3Di2.60.40.10, 3 hits
InterProiView protein in InterPro
IPR013162 CD80_C2-set
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR013106 Ig_V-set
IPR033314 Nectin1
PANTHERiPTHR23277:SF69 PTHR23277:SF69, 1 hit
PfamiView protein in Pfam
PF08205 C2-set_2, 1 hit
PF07686 V-set, 1 hit
SMARTiView protein in SMART
SM00409 IG, 3 hits
SM00408 IGc2, 2 hits
SM00406 IGv, 1 hit
SUPFAMiSSF48726 SSF48726, 3 hits
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 2 hits

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. AlignAdd to basket
Isoform Delta (identifier: Q15223-1) [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
MARMGLAGAA GRWWGLALGL TAFFLPGVHS QVVQVNDSMY GFIGTDVVLH
60 70 80 90 100
CSFANPLPSV KITQVTWQKS TNGSKQNVAI YNPSMGVSVL APYRERVEFL
110 120 130 140 150
RPSFTDGTIR LSRLELEDEG VYICEFATFP TGNRESQLNL TVMAKPTNWI
160 170 180 190 200
EGTQAVLRAK KGQDDKVLVA TCTSANGKPP SVVSWETRLK GEAEYQEIRN
210 220 230 240 250
PNGTVTVISR YRLVPSREAH QQSLACIVNY HMDRFKESLT LNVQYEPEVT
260 270 280 290 300
IEGFDGNWYL QRMDVKLTCK ADANPPATEY HWTTLNGSLP KGVEAQNRTL
310 320 330 340 350
FFKGPINYSL AGTYICEATN PIGTRSGQVE VNITEFPYTP SPPEHGRRAG
360 370 380 390 400
PVPTAIIGGV AGSILLVLIV VGGIVVALRR RRHTFKGDYS TKKHVYGNGY
410 420 430 440 450
SKAGIPQHHP PMAQNLQYPD DSDDEKKAGP LGGSSYEEEE EEEEGGGGGE
460 470 480 490 500
RKVGGPHPKY DEDAKRPYFT VDEAEARQDG YGDRTLGYQY DPEQLDLAEN
510
MVSQNDGSFI SKKEWYV
Length:517
Mass (Da):57,158
Last modified:September 26, 2001 - v3
Checksum:iDF34C8AEC893EE6D
GO
Isoform Alpha (identifier: Q15223-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     336-458: FPYTPSPPEH...GERKVGGPHP → KPRPQRGLGS...RTTEPRGECP
     459-517: Missing.

Show »
Length:458
Mass (Da):50,721
Checksum:iAB507515F86D7B45
GO
Isoform Gamma (identifier: Q15223-3) [UniParc]FASTAAdd to basket

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

Show »
Length:352
Mass (Da):39,150
Checksum:i2FB60588FA752D99
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_002624335 – 352EFPYT…RAGPV → AFCQLIYPGKGRTRARMF in isoform Gamma. 1 PublicationAdd BLAST18
Alternative sequenceiVSP_002626336 – 458FPYTP…GGPHP → KPRPQRGLGSAARLLAGTVA VFLILVAVLTVFFLYNRQQK SPPETDGAGTDQPLSQKPEP SPSRQSSLVPEDIQVVHLDP GRQQQQEEEDLQKLSLQPPY YDLGVSPSYHPSVRTTEPRG ECP in isoform Alpha. CuratedAdd BLAST123
Alternative sequenceiVSP_002625353 – 517Missing in isoform Gamma. 1 PublicationAdd BLAST165
Alternative sequenceiVSP_002627459 – 517Missing in isoform Alpha. CuratedAdd BLAST59

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
, AF196768, AF196769, AF196770, AF196771 Genomic DNA Translation: AAG16648.1
AF196774
, AF196768, AF196769, AF196770, AF196771, AF196772, AF196773 Genomic DNA Translation: AAG16649.1
CCDSiCCDS8425.1 [Q15223-2]
CCDS8426.1 [Q15223-1]
CCDS8427.1 [Q15223-3]
PIRiJC4024
RefSeqiNP_002846.3, NM_002855.4 [Q15223-1]
NP_976030.1, NM_203285.1 [Q15223-2]
NP_976031.1, NM_203286.1 [Q15223-3]
UniGeneiHs.334846

Genome annotation databases

EnsembliENST00000264025; ENSP00000264025; ENSG00000110400 [Q15223-1]
ENST00000340882; ENSP00000345289; ENSG00000110400 [Q15223-3]
ENST00000341398; ENSP00000344974; ENSG00000110400 [Q15223-2]
GeneIDi5818
KEGGihsa:5818
UCSCiuc001pwu.2 human [Q15223-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
, AF196768, AF196769, AF196770, AF196771 Genomic DNA Translation: AAG16648.1
AF196774
, AF196768, AF196769, AF196770, AF196771, AF196772, AF196773 Genomic DNA Translation: AAG16649.1
CCDSiCCDS8425.1 [Q15223-2]
CCDS8426.1 [Q15223-1]
CCDS8427.1 [Q15223-3]
PIRiJC4024
RefSeqiNP_002846.3, NM_002855.4 [Q15223-1]
NP_976030.1, NM_203285.1 [Q15223-2]
NP_976031.1, NM_203286.1 [Q15223-3]
UniGeneiHs.334846

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4MYWX-ray3.19B/D30-335[»]
ProteinModelPortaliQ15223
SMRiQ15223
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111776, 10 interactors
CORUMiQ15223
DIPiDIP-40302N
IntActiQ15223, 11 interactors
MINTiQ15223
STRINGi9606.ENSP00000264025

PTM databases

GlyConnecti1536
iPTMnetiQ15223
PhosphoSitePlusiQ15223

Polymorphism and mutation databases

BioMutaiPVRL1
DMDMi18202503

Proteomic databases

EPDiQ15223
MaxQBiQ15223
PaxDbiQ15223
PeptideAtlasiQ15223
PRIDEiQ15223
ProteomicsDBi60490
60491 [Q15223-2]
60492 [Q15223-3]

Protocols and materials databases

DNASUi5818
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264025; ENSP00000264025; ENSG00000110400 [Q15223-1]
ENST00000340882; ENSP00000345289; ENSG00000110400 [Q15223-3]
ENST00000341398; ENSP00000344974; ENSG00000110400 [Q15223-2]
GeneIDi5818
KEGGihsa:5818
UCSCiuc001pwu.2 human [Q15223-1]

Organism-specific databases

CTDi5818
DisGeNETi5818
EuPathDBiHostDB:ENSG00000110400.10
GeneCardsiNECTIN1
HGNCiHGNC:9706 NECTIN1
HPAiCAB016135
HPA026846
MalaCardsiNECTIN1
MIMi225060 phenotype
600644 gene
neXtProtiNX_Q15223
OpenTargetsiENSG00000110400
Orphaneti141291 Cleft lip and alveolus
199306 Cleft lip/palate
199302 Isolated cleft lip
3253 Zlotogora-Ogur syndrome
PharmGKBiPA34051
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IF17 Eukaryota
ENOG410YK75 LUCA
GeneTreeiENSGT00900000140811
HOGENOMiHOG000115804
HOVERGENiHBG100542
InParanoidiQ15223
KOiK06081
OMAiTCVTTYN
OrthoDBiEOG091G0BLQ
PhylomeDBiQ15223
TreeFamiTF331051

Enzyme and pathway databases

ReactomeiR-HSA-418990 Adherens junctions interactions
R-HSA-420597 Nectin/Necl trans heterodimerization

Miscellaneous databases

ChiTaRSiNECTIN1 human
EvolutionaryTraceiQ15223
GeneWikiiPVRL1
GenomeRNAii5818
PMAP-CutDBiQ15223
PROiPR:Q15223
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000110400 Expressed in 205 organ(s), highest expression level in esophagus mucosa
CleanExiHS_PVRL1
GenevisibleiQ15223 HS

Family and domain databases

Gene3Di2.60.40.10, 3 hits
InterProiView protein in InterPro
IPR013162 CD80_C2-set
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR013106 Ig_V-set
IPR033314 Nectin1
PANTHERiPTHR23277:SF69 PTHR23277:SF69, 1 hit
PfamiView protein in Pfam
PF08205 C2-set_2, 1 hit
PF07686 V-set, 1 hit
SMARTiView protein in SMART
SM00409 IG, 3 hits
SM00408 IGc2, 2 hits
SM00406 IGv, 1 hit
SUPFAMiSSF48726 SSF48726, 3 hits
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 2 hits
ProtoNetiSearch...

Entry informationi

Entry nameiNECT1_HUMAN
AccessioniPrimary (citable) accession number: Q15223
Secondary accession number(s): O75465
, Q2M3D3, Q9HBE6, Q9HBW2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: November 7, 2018
This is version 181 of the entry and version 3 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  5. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again