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| pubmed-article:7705348 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:7705348 | pubmed:dateCreated | 1995-5-9 | lld:pubmed |
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| pubmed-article:7705348 | pubmed:abstractText | The cDNAs for two glycoproteins, the 158-kDa submandibular glycoprotein (SGP158) and the 200-kDa parotid glycoprotein (PGP200), have been cloned from rat submandibular and parotid glands, respectively. Both cDNAs encode for identical proteins with repeating peptides -Asp-Gln-Gly-(Asn)-Gln-Thr-Gln-Pro-Arg-Pro-Pro-His-Pro-. A full-length cDNA encoding SGP158 was obtained using the strategy of anchor-PCR, and a full-length cDNA of PGP200 was prepared using RNA-PCR. Sequence analysis of the cDNAs revealed that SGP158 and PGP200 are identical proteins with 23 repeating peptides. Twenty-one peptides contain potential N-glycosylation sites and these two glycoproteins differ only in their glycosylation patterns. Southern-blot analysis showed that a single-copy gene encodes both mRNAs. PGP200 is constitutively expressed, but the synthesis of SGP158 is totally dependent upon treatment of animals with the beta-agonist isoproterenol. The first 106-nucleotide sequence of cDNAs for PGP200 and SGP158, which corresponds to the 5'-untranslated region and sequence encoding the signal peptide, is highly conserved when compared with proline-rich protein and glutamine-rich protein gene sequences. Based on the nucleotide sequences of exon I, a phylogenetic tree was constructed for 35 members of these multigene families. The tree fits with the generally recognized phylogeny of mammalian orders. We propose that exon I sequences of the proline-rich protein and glutamine-rich protein multigene families are relatively new and are possibly generated through exon shuffling during evolution. | lld:pubmed |
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| pubmed-article:7705348 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7705348 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7705348 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7705348 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7705348 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:7705348 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:7705348 | pubmed:author | pubmed-author:CarlsonD MDM | lld:pubmed |
| pubmed-article:7705348 | pubmed:author | pubmed-author:SubramaniamNN | lld:pubmed |
| pubmed-article:7705348 | pubmed:author | pubmed-author:MiaoY JYJ | lld:pubmed |
| pubmed-article:7705348 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7705348 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:7705348 | pubmed:volume | 228 | lld:pubmed |
| pubmed-article:7705348 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7705348 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7705348 | pubmed:pagination | 343-50 | lld:pubmed |
| pubmed-article:7705348 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:7705348 | pubmed:meshHeading | pubmed-meshheading:7705348-... | lld:pubmed |
| pubmed-article:7705348 | pubmed:meshHeading | pubmed-meshheading:7705348-... | lld:pubmed |
| pubmed-article:7705348 | pubmed:meshHeading | pubmed-meshheading:7705348-... | lld:pubmed |
| pubmed-article:7705348 | pubmed:meshHeading | pubmed-meshheading:7705348-... | lld:pubmed |
| pubmed-article:7705348 | pubmed:meshHeading | pubmed-meshheading:7705348-... | lld:pubmed |
| pubmed-article:7705348 | pubmed:meshHeading | pubmed-meshheading:7705348-... | lld:pubmed |
| pubmed-article:7705348 | pubmed:meshHeading | pubmed-meshheading:7705348-... | lld:pubmed |
| pubmed-article:7705348 | pubmed:meshHeading | pubmed-meshheading:7705348-... | lld:pubmed |
| pubmed-article:7705348 | pubmed:meshHeading | pubmed-meshheading:7705348-... | lld:pubmed |
| pubmed-article:7705348 | pubmed:meshHeading | pubmed-meshheading:7705348-... | lld:pubmed |
| pubmed-article:7705348 | pubmed:meshHeading | pubmed-meshheading:7705348-... | lld:pubmed |
| pubmed-article:7705348 | pubmed:meshHeading | pubmed-meshheading:7705348-... | lld:pubmed |
| pubmed-article:7705348 | pubmed:meshHeading | pubmed-meshheading:7705348-... | lld:pubmed |
| pubmed-article:7705348 | pubmed:meshHeading | pubmed-meshheading:7705348-... | lld:pubmed |
| pubmed-article:7705348 | pubmed:meshHeading | pubmed-meshheading:7705348-... | lld:pubmed |
| pubmed-article:7705348 | pubmed:meshHeading | pubmed-meshheading:7705348-... | lld:pubmed |
| pubmed-article:7705348 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7705348 | pubmed:articleTitle | cDNA cloning and characterization of rat salivary glycoproteins. Novel members of the proline-rich-protein multigene families. | lld:pubmed |
| pubmed-article:7705348 | pubmed:affiliation | Section of Molecular and Cellular Biology, University of California, Davis 95616, USA. | lld:pubmed |
| pubmed-article:7705348 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7705348 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| entrez-gene:245985 | entrezgene:pubmed | pubmed-article:7705348 | lld:entrezgene |
