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http://purl.uniprot.org/citations/3198605http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3198605http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3198605http://www.w3.org/2000/01/rdf-schema#comment"We have isolated and sequenced cDNA clones corresponding to the entire coding sequences of the human lysosomal membrane glycoproteins, lamp-1 and lamp-2 (h-lamp-1 and h-lamp-2). The deduced amino acid sequences indicate that h-lamp-1 and h-lamp-2 consist of 416 and 408 amino acid residues, respectively, and suggest that 27 and 28 NH2-terminal residues are cleavable signal peptides. The major portions of both h-lamp-1 and h-lamp-2 reside on the luminal side of the lysosome and are heavily glycosylated by N-glycans: h-lamp-1 and h-lamp-2 were found to contain 19 and 16 potential N-glycosylation sites, respectively. The findings are consistent with the results obtained by endo-beta-N-acetylglucosaminidase F treatment of h-lamp-1 and h-lamp-2 precursors, described in the preceding paper (Carlsson, S. R., Roth, J., Piller, F., and Fukuda, M. (1988) J. Biol. Chem. 263, 18911-18919). These N-glycosylation sites are clustered into two domains separated by a hinge-like structure enriched with proline and serine in h-lamp-1 or proline and threonine in h-lamp-2. The two domains of h-lamp-1 on each side of the hinge region are homologous to each other, whereas no such homology was detected between the two domains of h-lamp-2. Both proteins have one putative transmembrane domain consisting of 24 hydrophobic amino acids near the COOH terminus, and contain a short cytoplasmic segment composed of 11 amino acid residues at the COOH-terminal end. Comparison of h-lamp-1 and h-lamp-2 sequences reveal strong homology between the two molecules, particularly in the proximity to the COOH-terminal end. It is possible that this portion is important for targeting the molecules to lysosomes. These results also suggest that lamp-1 and lamp-2 are evolutionarily related. Comparison of known lamp-1 sequences among different species, on the other hand, show that human lamp-1 has more similarity to lamp-1 from other species than to human lamp-2. This fact, taken together with the finding that h-lamp-2 lacks repeating domains, suggests that lamp-1 and lamp-2 diverged from a putative ancestor gene in early stages of evolution. These results also suggest that lamp-1 and lamp-2 probably have distinctly separate functions despite the fact that they share many structural features."xsd:string
http://purl.uniprot.org/citations/3198605http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)37370-8"xsd:string
http://purl.uniprot.org/citations/3198605http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)37370-8"xsd:string
http://purl.uniprot.org/citations/3198605http://purl.uniprot.org/core/author"Fukuda M."xsd:string
http://purl.uniprot.org/citations/3198605http://purl.uniprot.org/core/author"Fukuda M."xsd:string
http://purl.uniprot.org/citations/3198605http://purl.uniprot.org/core/author"Carlsson S.R."xsd:string
http://purl.uniprot.org/citations/3198605http://purl.uniprot.org/core/author"Carlsson S.R."xsd:string
http://purl.uniprot.org/citations/3198605http://purl.uniprot.org/core/author"Matteson J."xsd:string
http://purl.uniprot.org/citations/3198605http://purl.uniprot.org/core/author"Matteson J."xsd:string
http://purl.uniprot.org/citations/3198605http://purl.uniprot.org/core/author"Viitala J."xsd:string
http://purl.uniprot.org/citations/3198605http://purl.uniprot.org/core/author"Viitala J."xsd:string
http://purl.uniprot.org/citations/3198605http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/3198605http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/3198605http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/3198605http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/3198605http://purl.uniprot.org/core/pages"18920-18928"xsd:string
http://purl.uniprot.org/citations/3198605http://purl.uniprot.org/core/pages"18920-18928"xsd:string
http://purl.uniprot.org/citations/3198605http://purl.uniprot.org/core/title"Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Comparison of their deduced amino acid sequences."xsd:string
http://purl.uniprot.org/citations/3198605http://purl.uniprot.org/core/title"Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Comparison of their deduced amino acid sequences."xsd:string
http://purl.uniprot.org/citations/3198605http://purl.uniprot.org/core/volume"263"xsd:string
http://purl.uniprot.org/citations/3198605http://purl.uniprot.org/core/volume"263"xsd:string
http://purl.uniprot.org/citations/3198605http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3198605
http://purl.uniprot.org/citations/3198605http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3198605
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