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http://purl.uniprot.org/citations/12826663http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12826663http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12826663http://www.w3.org/2000/01/rdf-schema#comment"Nectins are Ca2+-independent immunoglobulin-like cell-cell adhesion molecules that play roles in organization of a variety of cell-cell junctions in cooperation with or independently of cadherins. Four nectins have been identified. Five nectin-like molecules, which have domain structures similar to those of nectins, have been identified, and we characterized here nectin-like molecule-2 (Necl-2)/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1. Necl-2 showed Ca2+-independent homophilic cell-cell adhesion activity. It furthermore showed Ca2+-independent heterophilic cell-cell adhesion activity with Necl-1/TSLL1/SynCAM3 and nectin-3. Necl-2 was widely expressed in rat tissues examined. Necl-2 localized at the basolateral plasma membrane in epithelial cells of the mouse gall bladder, but not at specialized cell-cell junctions, such as tight junctions, adherens junctions, and desmosomes. Nectins bind afadin, whereas Necl-2 did not bind afadin but bound Pals2, a membrane-associated guanylate kinase family member known to bind Lin-7, implicated in the proper localization of the Let-23 protein in Caenorhabditis elegans, the homologue of mammalian epidermal growth factor receptor. These results indicate the unique localization of Necl-2 and its possible involvement in localization of a transmembrane protein(s) through Pals2."xsd:string
http://purl.uniprot.org/citations/12826663http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m305387200"xsd:string
http://purl.uniprot.org/citations/12826663http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m305387200"xsd:string
http://purl.uniprot.org/citations/12826663http://purl.uniprot.org/core/author"Imai T."xsd:string
http://purl.uniprot.org/citations/12826663http://purl.uniprot.org/core/author"Imai T."xsd:string
http://purl.uniprot.org/citations/12826663http://purl.uniprot.org/core/author"Satoh K."xsd:string
http://purl.uniprot.org/citations/12826663http://purl.uniprot.org/core/author"Satoh K."xsd:string
http://purl.uniprot.org/citations/12826663http://purl.uniprot.org/core/author"Takai Y."xsd:string
http://purl.uniprot.org/citations/12826663http://purl.uniprot.org/core/author"Takai Y."xsd:string
http://purl.uniprot.org/citations/12826663http://purl.uniprot.org/core/author"Takeuchi M."xsd:string
http://purl.uniprot.org/citations/12826663http://purl.uniprot.org/core/author"Takeuchi M."xsd:string
http://purl.uniprot.org/citations/12826663http://purl.uniprot.org/core/author"Itoh S."xsd:string
http://purl.uniprot.org/citations/12826663http://purl.uniprot.org/core/author"Itoh S."xsd:string
http://purl.uniprot.org/citations/12826663http://purl.uniprot.org/core/author"Morimoto K."xsd:string
http://purl.uniprot.org/citations/12826663http://purl.uniprot.org/core/author"Morimoto K."xsd:string
http://purl.uniprot.org/citations/12826663http://purl.uniprot.org/core/author"Ikeda W."xsd:string
http://purl.uniprot.org/citations/12826663http://purl.uniprot.org/core/author"Ikeda W."xsd:string
http://purl.uniprot.org/citations/12826663http://purl.uniprot.org/core/author"Monden M."xsd:string
http://purl.uniprot.org/citations/12826663http://purl.uniprot.org/core/author"Monden M."xsd:string
http://purl.uniprot.org/citations/12826663http://purl.uniprot.org/core/author"Kakunaga S."xsd:string
http://purl.uniprot.org/citations/12826663http://purl.uniprot.org/core/author"Kakunaga S."xsd:string
http://purl.uniprot.org/citations/12826663http://purl.uniprot.org/core/author"Shingai T."xsd:string
http://purl.uniprot.org/citations/12826663http://purl.uniprot.org/core/author"Shingai T."xsd:string