NECT1_MOUSE
ID NECT1_MOUSE Reviewed; 515 AA.
AC Q9JKF6; Q6P9M9; Q9ERL5; Q9JI17;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Nectin-1;
DE AltName: Full=Herpes virus entry mediator C;
DE Short=Herpesvirus entry mediator C;
DE Short=HveC;
DE AltName: Full=Nectin cell adhesion molecule 1 {ECO:0000250|UniProtKB:Q15223};
DE AltName: Full=Poliovirus receptor-related protein 1;
DE AltName: CD_antigen=CD111;
DE Flags: Precursor;
GN Name=Nectin1 {ECO:0000250|UniProtKB:Q15223}; Synonyms=Hvec, Prr1, Pvrl1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10781093; DOI=10.1073/pnas.97.9.4867;
RA Menotti L., Lopez M., Avitabile E., Stefan A., Cocchi F., Adelaide J.,
RA Lecocq E., Dubreuil P., Campadelli-Fiume G.;
RT "The murine homolog of human nectin1 delta serves as a species nonspecific
RT mediator for entry of human and animal alpha herpesviruses in a pathway
RT independent of detectable binding to gD.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:4867-4872(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11090177; DOI=10.1128/jvi.74.24.11773-11781.2000;
RA Shukla D., Dal Canto M.C., Rowe C.L., Spear P.G.;
RT "Striking similarity of murine nectin-1alpha to human nectin-1alpha (HveC)
RT in sequence and activity as a glycoprotein D receptor for alphaherpesvirus
RT entry.";
RL J. Virol. 74:11773-11781(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Swiss Webster;
RA Zhan J., Wimmer E.;
RT "Mouse nectin-1 (mPRR1), a herpesvirus receptor, is expressed in the floor
RT plate during embryogenesis, suggesting a role in neural development.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH NECTIN3.
RX PubMed=10744716; DOI=10.1074/jbc.275.14.10291;
RA Satoh-Horikawa K., Nakanishi H., Takahashi K., Miyahara M., Nishimura M.,
RA Tachibana K., Mizoguchi A., Takai Y.;
RT "Nectin-3: a new member of immunoglobulin-like cell adhesion molecules that
RT shows homophilic and heterophilic cell-cell adhesion activities.";
RL J. Biol. Chem. 275:10291-10299(2000).
RN [6]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=11827984; DOI=10.1083/jcb.200103113;
RA Mizoguchi A., Nakanishi H., Kimura K., Matsubara K., Ozaki-Kuroda K.,
RA Katata T., Honda T., Kiyohara Y., Heo K., Higashi M., Tsutsumi T.,
RA Sonoda S., Ide C., Takai Y.;
RT "Nectin: an adhesion molecule involved in formation of synapses.";
RL J. Cell Biol. 156:555-565(2002).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433 AND SER-434, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202 AND ASN-286.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202; ASN-286 AND ASN-332.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421; SER-433; TYR-435 AND
RP SER-509, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP STRUCTURE BY NMR OF 241-334, FUNCTION, SUBUNIT, IG-LIKE DOMAIN, AND
RP DISULFIDE BOND.
RX PubMed=22955284; DOI=10.1074/jbc.m112.345215;
RA Bojesen K.B., Clausen O., Rohde K., Christensen C., Zhang L., Li S.,
RA Kohler L., Nielbo S., Nielsen J., Gjorlund M.D., Poulsen F.M., Bock E.,
RA Berezin V.;
RT "Nectin-1 binds and signals through the fibroblast growth factor
RT receptor.";
RL J. Biol. Chem. 287:37420-37433(2012).
CC -!- FUNCTION: Involved in cell adhesion and synaptogegesis. Has some
CC neurite outgrowth-promoting activity. Receptor for alphaherpesvirus
CC (HSV-1, HSV-2 and pseudorabies virus) entry into cells.
CC {ECO:0000269|PubMed:11827984, ECO:0000269|PubMed:22955284}.
CC -!- SUBUNIT: Cis- and trans-homodimer. Can form trans-heterodimers with
CC NECTIN3. Interaction between NECTIN1 and NECTIN3 on the pre- and
CC postsynaptic sites, respectively, initiates the formation of puncta
CC adherentia junctions between axons and dendrites. Interacts (via Ig-
CC like C2-type domain 2) with FGFR1, FGFR2 and FGFR3. Interacts (via
CC Cytoplasmic domain) with AFDN, providing a connection with the actin
CC cytoskeleton. Interacts with HSV glycoprotein D (gD).
CC {ECO:0000269|PubMed:10744716, ECO:0000269|PubMed:11827984,
CC ECO:0000269|PubMed:22955284}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11827984};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:11827984}.
CC Presynaptic cell membrane {ECO:0000269|PubMed:11827984}.
CC -!- DOMAIN: Ig-like C2-type 2 mediates neurite outgrowth through binding,
CC induction of phosphorylation, and activation of FGFR.
CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
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DR EMBL; AF239762; AAF60333.1; -; mRNA.
DR EMBL; AF270977; AAF76195.1; -; mRNA.
DR EMBL; AF297665; AAG22808.1; -; mRNA.
DR EMBL; BC060694; AAH60694.1; -; mRNA.
DR CCDS; CCDS23092.1; -.
DR RefSeq; NP_067399.2; NM_021424.2.
DR PDB; 2L7J; NMR; -; A=241-334.
DR PDB; 5B21; X-ray; 2.24 A; A/B=31-144.
DR PDBsum; 2L7J; -.
DR PDBsum; 5B21; -.
DR AlphaFoldDB; Q9JKF6; -.
DR BMRB; Q9JKF6; -.
DR SMR; Q9JKF6; -.
DR BioGRID; 208408; 1.
DR DIP; DIP-41728N; -.
DR MINT; Q9JKF6; -.
DR STRING; 10090.ENSMUSP00000034510; -.
DR GlyConnect; 2528; 15 N-Linked glycans (1 site).
DR GlyGen; Q9JKF6; 7 sites, 15 N-linked glycans (1 site).
DR iPTMnet; Q9JKF6; -.
DR PhosphoSitePlus; Q9JKF6; -.
DR CPTAC; non-CPTAC-3660; -.
DR jPOST; Q9JKF6; -.
DR MaxQB; Q9JKF6; -.
DR PaxDb; Q9JKF6; -.
DR PeptideAtlas; Q9JKF6; -.
DR PRIDE; Q9JKF6; -.
DR ProteomicsDB; 252802; -.
DR Antibodypedia; 4247; 439 antibodies from 38 providers.
DR DNASU; 58235; -.
DR Ensembl; ENSMUST00000034510; ENSMUSP00000034510; ENSMUSG00000032012.
DR GeneID; 58235; -.
DR KEGG; mmu:58235; -.
DR UCSC; uc009pbj.1; mouse.
DR CTD; 5818; -.
DR MGI; MGI:1926483; Nectin1.
DR VEuPathDB; HostDB:ENSMUSG00000032012; -.
DR eggNOG; ENOG502QVRJ; Eukaryota.
DR GeneTree; ENSGT00940000156933; -.
DR HOGENOM; CLU_029618_3_1_1; -.
DR InParanoid; Q9JKF6; -.
DR OrthoDB; 509401at2759; -.
DR PhylomeDB; Q9JKF6; -.
DR TreeFam; TF331051; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR Reactome; R-MMU-420597; Nectin/Necl trans heterodimerization.
DR BioGRID-ORCS; 58235; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Nectin1; mouse.
DR PRO; PR:Q9JKF6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9JKF6; protein.
DR Bgee; ENSMUSG00000032012; Expressed in lip and 140 other tissues.
DR ExpressionAtlas; Q9JKF6; baseline and differential.
DR Genevisible; Q9JKF6; MM.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
DR GO; GO:0043296; C:apical junction complex; IDA:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0044291; C:cell-cell contact zone; IDA:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0032584; C:growth cone membrane; ISO:MGI.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IDA:MGI.
DR GO; GO:0046790; F:virion binding; ISO:MGI.
DR GO; GO:0007411; P:axon guidance; ISO:MGI.
DR GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
DR GO; GO:0002934; P:desmosome organization; IMP:MGI.
DR GO; GO:0070166; P:enamel mineralization; IMP:MGI.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:HGNC-UCL.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:HGNC-UCL.
DR GO; GO:0006826; P:iron ion transport; IMP:MGI.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
DR GO; GO:1902414; P:protein localization to cell junction; IDA:MGI.
DR GO; GO:0051963; P:regulation of synapse assembly; ISO:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0046718; P:viral entry into host cell; ISO:MGI.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:InterPro.
DR CDD; cd05886; Ig1_Nectin-1_like; 1.
DR CDD; cd05890; Ig2_Nectin-1_like; 1.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR041849; Nectin-1_Ig1.
DR InterPro; IPR041850; Nectin-1_Ig2.
DR InterPro; IPR033314; Nectin1.
DR PANTHER; PTHR23277:SF69; PTHR23277:SF69; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell membrane; Cell projection;
KW Disulfide bond; Glycoprotein; Host-virus interaction;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..515
FT /note="Nectin-1"
FT /id="PRO_0000015134"
FT TOPO_DOM 31..354
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..141
FT /note="Ig-like V-type"
FT DOMAIN 145..243
FT /note="Ig-like C2-type 1"
FT DOMAIN 247..334
FT /note="Ig-like C2-type 2"
FT REGION 282..299
FT /note="Interaction with FGFR"
FT REGION 399..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 435
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 51..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 172..226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 269..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:22955284"
FT CONFLICT 138
FT /note="L -> P (in Ref. 1; AAF60333)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="D -> N (in Ref. 2; AAF76195 and 3; AAG22808)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="P -> PP (in Ref. 2; AAF76195)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="G -> S (in Ref. 1; AAF60333 and 2; AAF76195)"
FT /evidence="ECO:0000305"
FT STRAND 33..42
FT /evidence="ECO:0007829|PDB:5B21"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:5B21"
FT STRAND 61..70
FT /evidence="ECO:0007829|PDB:5B21"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:5B21"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:5B21"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:5B21"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:5B21"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:5B21"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:5B21"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:5B21"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:5B21"
FT STRAND 132..143
FT /evidence="ECO:0007829|PDB:5B21"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:2L7J"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:2L7J"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:2L7J"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:2L7J"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:2L7J"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:2L7J"
FT STRAND 312..320
FT /evidence="ECO:0007829|PDB:2L7J"
FT STRAND 323..331
FT /evidence="ECO:0007829|PDB:2L7J"
SQ SEQUENCE 515 AA; 57035 MW; A56FA2C7F8B25AFB CRC64;
MARMGLAGAA GRWWGLALGL TAFFLPGTHT QVVQVNDSMY GFIGTDVVLH CSFANPLPSV
KITQVTWQKA SNGSKQNMAI YNPTMGVSVL PPYEKRVEFL RPSFIDGTIR LSGLELEDEG
MYICEFATFP TGNRESQLNL TVMAKPTNWI EGTRAVLRAR KGQDDKVLVA TCTSANGKPP
SAVSWETRLK GEAEYQEIRN PNGTVTVISR YRLVPSREAH RQSLACIVNY HLDRFRESLT
LNVQYEPEVT IEGFDGNWYL QRTDVKLTCK ADANPPATEY HWTTLNGSLP KGVEAQNRTL
FFRGPITYSL AGTYICEATN PIGTRSGQVE VNITEFPYTP TPEHGRRAGQ MPTAIIGGVA
GSVLLVLIVV GGIIVALRRR RHTFKGDYST KKHVYGNGYS KAGIPQHHPP MAQNLQYPDD
SDDEKKAGPL GGSSYEEEEE EEGGGGGERK VGGPHPKYDE DAKRPYFTVD EAEARQDGYG
DRTLGYQYDP EQLDLAENMV SQNDGSFISK KEWYV
