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Protein

Nectin-1

Gene

Nectin1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in cell adhesion and synaptogegesis. Has some neurite outgrowth-promoting activity. Receptor for alphaherpesvirus (HSV-1, HSV-2 and pseudorabies virus) entry into cells.2 Publications

GO - Molecular functioni

  • carbohydrate binding Source: Ensembl
  • cell adhesion molecule binding Source: MGI
  • protein homodimerization activity Source: HGNC
  • receptor activity Source: MGI
  • virion binding Source: Ensembl

GO - Biological processi

  • axon guidance Source: Ensembl
  • camera-type eye morphogenesis Source: MGI
  • desmosome organization Source: MGI
  • enamel mineralization Source: MGI
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: HGNC
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: HGNC
  • iron ion transport Source: MGI
  • lens morphogenesis in camera-type eye Source: MGI
  • regulation of synapse assembly Source: Ensembl
  • retina development in camera-type eye Source: MGI
  • single organismal cell-cell adhesion Source: MGI
  • viral entry into host cell Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Cell adhesion, Host-virus interaction

Enzyme and pathway databases

ReactomeiR-MMU-418990. Adherens junctions interactions.
R-MMU-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
Nectin cell adhesion molecule 1By similarity
Poliovirus receptor-related protein 1
CD_antigen: CD111
Gene namesi
Name:Nectin1By similarity
Synonyms:Hvec, Prr1, Pvrl1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1926483. Pvrl1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 354324ExtracellularSequence analysisAdd
BLAST
Transmembranei355 – 37521HelicalSequence analysisAdd
BLAST
Topological domaini376 – 515140CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence analysisAdd
BLAST
Chaini31 – 515485Nectin-1PRO_0000015134Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi36 – 361N-linked (GlcNAc...)Sequence analysis
Disulfide bondi51 ↔ 124PROSITE-ProRule annotation
Glycosylationi72 – 721N-linked (GlcNAc...)Sequence analysis
Glycosylationi139 – 1391N-linked (GlcNAc...)Sequence analysis
Disulfide bondi172 ↔ 226PROSITE-ProRule annotation
Glycosylationi200 – 2001N-linked (GlcNAc...); atypical1 Publication
Glycosylationi202 – 2021N-linked (GlcNAc...)2 Publications
Disulfide bondi269 ↔ 316PROSITE-ProRule annotation1 Publication
Glycosylationi274 – 2741N-linked (GlcNAc...); atypical1 Publication
Glycosylationi286 – 2861N-linked (GlcNAc...)2 Publications
Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence analysis
Glycosylationi332 – 3321N-linked (GlcNAc...)1 Publication
Modified residuei421 – 4211PhosphoserineCombined sources
Modified residuei433 – 4331PhosphoserineCombined sources
Modified residuei434 – 4341PhosphoserineCombined sources
Modified residuei435 – 4351PhosphotyrosineCombined sources
Modified residuei509 – 5091PhosphoserineCombined sources

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9JKF6.
PaxDbiQ9JKF6.
PRIDEiQ9JKF6.

PTM databases

iPTMnetiQ9JKF6.
PhosphoSiteiQ9JKF6.

Expressioni

Gene expression databases

BgeeiQ9JKF6.
CleanExiMM_PVRL1.
GenevisibleiQ9JKF6. MM.

Interactioni

Subunit structurei

Cis- and trans-homodimer. Can form trans-heterodimers with NECTIN3. 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 Ig-like C2-type domain 2) with FGFR1, FGFR2 and FGFR3. Interacts (via Cytoplasmic domain) with MLLT4/afadin, providing a connection with the actin cytoskeleton. Interacts with HSV glycoprotein D (gD).3 Publications

GO - Molecular functioni

  • cell adhesion molecule binding Source: MGI
  • protein homodimerization activity Source: HGNC

Protein-protein interaction databases

DIPiDIP-41728N.
MINTiMINT-254710.
STRINGi10090.ENSMUSP00000034510.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L7JNMR-A241-334[»]
ProteinModelPortaliQ9JKF6.
SMRiQ9JKF6. Positions 33-335.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 141111Ig-like V-typeAdd
BLAST
Domaini145 – 24399Ig-like C2-type 1Add
BLAST
Domaini247 – 33488Ig-like C2-type 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni282 – 29918Interaction with FGFRAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi436 – 4427Poly-Glu
Compositional biasi443 – 4475Poly-Gly

Domaini

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

Sequence similaritiesi

Belongs to the nectin family.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IF17. Eukaryota.
ENOG410YK75. LUCA.
GeneTreeiENSGT00770000120512.
HOGENOMiHOG000115804.
HOVERGENiHBG100542.
InParanoidiQ9JKF6.
KOiK06081.
OMAiHVFGNGY.
OrthoDBiEOG73RBB5.
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.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR033314. Nectin1.
[Graphical view]
PANTHERiPTHR23277:SF69. PTHR23277:SF69. 1 hit.
PfamiPF08205. C2-set_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 2 hits.
SM00408. IGc2. 2 hits.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9JKF6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARMGLAGAA GRWWGLALGL TAFFLPGTHT QVVQVNDSMY GFIGTDVVLH
60 70 80 90 100
CSFANPLPSV KITQVTWQKA SNGSKQNMAI YNPTMGVSVL PPYEKRVEFL
110 120 130 140 150
RPSFIDGTIR LSGLELEDEG MYICEFATFP TGNRESQLNL TVMAKPTNWI
160 170 180 190 200
EGTRAVLRAR KGQDDKVLVA TCTSANGKPP SAVSWETRLK GEAEYQEIRN
210 220 230 240 250
PNGTVTVISR YRLVPSREAH RQSLACIVNY HLDRFRESLT LNVQYEPEVT
260 270 280 290 300
IEGFDGNWYL QRTDVKLTCK ADANPPATEY HWTTLNGSLP KGVEAQNRTL
310 320 330 340 350
FFRGPITYSL AGTYICEATN PIGTRSGQVE VNITEFPYTP TPEHGRRAGQ
360 370 380 390 400
MPTAIIGGVA GSVLLVLIVV GGIIVALRRR RHTFKGDYST KKHVYGNGYS
410 420 430 440 450
KAGIPQHHPP MAQNLQYPDD SDDEKKAGPL GGSSYEEEEE EEGGGGGERK
460 470 480 490 500
VGGPHPKYDE DAKRPYFTVD EAEARQDGYG DRTLGYQYDP EQLDLAENMV
510
SQNDGSFISK KEWYV
Length:515
Mass (Da):57,035
Last modified:July 27, 2011 - v3
Checksum:iA56FA2C7F8B25AFB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381L → P in AAF60333 (PubMed:10781093).Curated
Sequence conflicti165 – 1651D → N in AAF76195 (PubMed:11090177).Curated
Sequence conflicti165 – 1651D → N in AAG22808 (Ref. 3) Curated
Sequence conflicti342 – 3421P → PP in AAF76195 (PubMed:11090177).Curated
Sequence conflicti428 – 4281G → S in AAF60333 (PubMed:10781093).Curated
Sequence conflicti428 – 4281G → S in AAF76195 (PubMed:11090177).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF239762 mRNA. Translation: AAF60333.1.
AF270977 mRNA. Translation: AAF76195.1.
AF297665 mRNA. Translation: AAG22808.1.
BC060694 mRNA. Translation: AAH60694.1.
CCDSiCCDS23092.1.
RefSeqiNP_067399.2. NM_021424.2.
UniGeneiMm.335096.

Genome annotation databases

EnsembliENSMUST00000034510; ENSMUSP00000034510; ENSMUSG00000032012.
GeneIDi58235.
KEGGimmu:58235.
UCSCiuc009pbj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF239762 mRNA. Translation: AAF60333.1.
AF270977 mRNA. Translation: AAF76195.1.
AF297665 mRNA. Translation: AAG22808.1.
BC060694 mRNA. Translation: AAH60694.1.
CCDSiCCDS23092.1.
RefSeqiNP_067399.2. NM_021424.2.
UniGeneiMm.335096.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L7JNMR-A241-334[»]
ProteinModelPortaliQ9JKF6.
SMRiQ9JKF6. Positions 33-335.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-41728N.
MINTiMINT-254710.
STRINGi10090.ENSMUSP00000034510.

PTM databases

iPTMnetiQ9JKF6.
PhosphoSiteiQ9JKF6.

Proteomic databases

MaxQBiQ9JKF6.
PaxDbiQ9JKF6.
PRIDEiQ9JKF6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034510; ENSMUSP00000034510; ENSMUSG00000032012.
GeneIDi58235.
KEGGimmu:58235.
UCSCiuc009pbj.1. mouse.

Organism-specific databases

CTDi58235.
MGIiMGI:1926483. Pvrl1.

Phylogenomic databases

eggNOGiENOG410IF17. Eukaryota.
ENOG410YK75. LUCA.
GeneTreeiENSGT00770000120512.
HOGENOMiHOG000115804.
HOVERGENiHBG100542.
InParanoidiQ9JKF6.
KOiK06081.
OMAiHVFGNGY.
OrthoDBiEOG73RBB5.
TreeFamiTF331051.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiPvrl1. mouse.
NextBioi314269.
PROiQ9JKF6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JKF6.
CleanExiMM_PVRL1.
GenevisibleiQ9JKF6. MM.

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.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR033314. Nectin1.
[Graphical view]
PANTHERiPTHR23277:SF69. PTHR23277:SF69. 1 hit.
PfamiPF08205. C2-set_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 2 hits.
SM00408. IGc2. 2 hits.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The murine homolog of human nectin1 delta serves as a species nonspecific mediator for entry of human and animal alpha herpesviruses in a pathway independent of detectable binding to gD."
    Menotti L., Lopez M., Avitabile E., Stefan A., Cocchi F., Adelaide J., Lecocq E., Dubreuil P., Campadelli-Fiume G.
    Proc. Natl. Acad. Sci. U.S.A. 97:4867-4872(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Striking similarity of murine nectin-1alpha to human nectin-1alpha (HveC) in sequence and activity as a glycoprotein D receptor for alphaherpesvirus entry."
    Shukla D., Dal Canto M.C., Rowe C.L., Spear P.G.
    J. Virol. 74:11773-11781(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Mouse nectin-1 (mPRR1), a herpesvirus receptor, is expressed in the floor plate during embryogenesis, suggesting a role in neural development."
    Zhan J., Wimmer E.
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Swiss Webster.
  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].
    Strain: C57BL/6J.
    Tissue: Brain.
  5. "Nectin-3: a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activities."
    Satoh-Horikawa K., Nakanishi H., Takahashi K., Miyahara M., Nishimura M., Tachibana K., Mizoguchi A., Takai Y.
    J. Biol. Chem. 275:10291-10299(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NECTIN3.
  6. Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433 AND SER-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
    Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
    Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-200; ASN-202; ASN-274 AND ASN-286.
    Tissue: Myoblast.
  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-202; ASN-286 AND ASN-332.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421; SER-433; TYR-435 AND SER-509, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney and Lung.
  13. Cited for: STRUCTURE BY NMR OF 241-334, FUNCTION, SUBUNIT, IG-LIKE DOMAIN, DISULFIDE BOND.

Entry informationi

Entry nameiNECT1_MOUSE
AccessioniPrimary (citable) accession number: Q9JKF6
Secondary accession number(s): Q6P9M9, Q9ERL5, Q9JI17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.