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Subject | Predicate | Object |
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http://purl.uniprot.org/citations/2324102 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/2324102 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/2324102 | http://www.w3.org/2000/01/rdf-schema#comment | "The structure of human syndecan, an integral membrane proteoglycan, has been determined by cloning its full-length cDNA, which codes for the entire 310-amino acid-long core protein, including the NH2-terminal signal peptide. Similar to mouse syndecan (Saunders, S., Jalkanen, M., O'Farrell, S., and Bernfield, M. (1989) J. Cell Biol. 108, 1547-1556), the core protein of human syndecan can be divided into three domains: a matrix-interacting ectodomain containing putative glycosaminoglycan attachment sites, a 25-residue hydrophobic membrane-spanning domain, and a 34-residue cytoplasmic domain. Several interesting conserved structures were revealed by comparing the human syndecan sequence to the murine one. (i) Although the ectodomains are only 70% identical, all putative glycosaminoglycan attachment sites are identical (two of them belong to the consensus sequence SGXG and three others to (E/D)GSG(E/D), as are also (ii) the single putative N-glycosylation site and (iii) the proteinase-sensitive dibasic RK site adjacent to the extracellular face of the transmembrane domain. Furthermore, (iv) the transmembrane domain is 96% identical, as the only change in human syndecan was an alteration of an alanine residue to glycine; and finally, (v) the cytoplasmic domain is 100% identical, including 3 identically located tyrosine residues. Comparison of transmembrane and cytoplasmic domains to a third cell-surface proteoglycan, 48K5 from human lung fibroblasts (Marynen, P., Zhang, J., Cassiman, J., Vanden Berghe, H., and David, C. (1989) J. Biol. Chem. 264, 7017-7024), indicates that the transmembrane and cytoplasmic domains are similar also in this molecule regardless of the presence of a totally nonhomologous ectodomain. Thus, the transmembrane and cytoplasmic domains are unique for these cell-surface proteoglycans, which we propose to be members of a novel gene family of syndecans."xsd:string |
http://purl.uniprot.org/citations/2324102 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(19)39232-4"xsd:string |
http://purl.uniprot.org/citations/2324102 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(19)39232-4"xsd:string |
http://purl.uniprot.org/citations/2324102 | http://purl.uniprot.org/core/author | "Jaakkola P."xsd:string |
http://purl.uniprot.org/citations/2324102 | http://purl.uniprot.org/core/author | "Jaakkola P."xsd:string |
http://purl.uniprot.org/citations/2324102 | http://purl.uniprot.org/core/author | "Jalkanen M."xsd:string |
http://purl.uniprot.org/citations/2324102 | http://purl.uniprot.org/core/author | "Jalkanen M."xsd:string |
http://purl.uniprot.org/citations/2324102 | http://purl.uniprot.org/core/author | "Arvilommi A.-M."xsd:string |
http://purl.uniprot.org/citations/2324102 | http://purl.uniprot.org/core/author | "Arvilommi A.-M."xsd:string |
http://purl.uniprot.org/citations/2324102 | http://purl.uniprot.org/core/author | "Mali M."xsd:string |
http://purl.uniprot.org/citations/2324102 | http://purl.uniprot.org/core/author | "Mali M."xsd:string |
http://purl.uniprot.org/citations/2324102 | http://purl.uniprot.org/core/date | "1990"xsd:gYear |
http://purl.uniprot.org/citations/2324102 | http://purl.uniprot.org/core/date | "1990"xsd:gYear |
http://purl.uniprot.org/citations/2324102 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/2324102 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/2324102 | http://purl.uniprot.org/core/pages | "6884-6889"xsd:string |
http://purl.uniprot.org/citations/2324102 | http://purl.uniprot.org/core/pages | "6884-6889"xsd:string |
http://purl.uniprot.org/citations/2324102 | http://purl.uniprot.org/core/title | "Sequence of human syndecan indicates a novel gene family of integral membrane proteoglycans."xsd:string |
http://purl.uniprot.org/citations/2324102 | http://purl.uniprot.org/core/title | "Sequence of human syndecan indicates a novel gene family of integral membrane proteoglycans."xsd:string |
http://purl.uniprot.org/citations/2324102 | http://purl.uniprot.org/core/volume | "265"xsd:string |
http://purl.uniprot.org/citations/2324102 | http://purl.uniprot.org/core/volume | "265"xsd:string |
http://purl.uniprot.org/citations/2324102 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/2324102 |
http://purl.uniprot.org/citations/2324102 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/2324102 |