rdf:type |
|
lifeskim:mentions |
umls-concept:C0006556,
umls-concept:C0009015,
umls-concept:C0017363,
umls-concept:C0017968,
umls-concept:C0034693,
umls-concept:C0034721,
umls-concept:C0205314,
umls-concept:C0442040,
umls-concept:C0679622,
umls-concept:C0680022,
umls-concept:C1880022
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pubmed:issue |
2
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pubmed:dateCreated |
1995-5-9
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/J05490,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/J05491,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/K02247,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/K03202,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/K03203,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/K03204,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/K03205,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/K03206,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/K03207,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L08134,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M11897,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M11898,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M11899,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M11900,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M11902,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M12099,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M13057,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M13058,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M23236,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M31032,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M58653,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M58654,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M64792,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M76536,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M81321,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M81322,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X07881,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X07882,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X58438,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X61126
|
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.
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pubmed:grant |
|
pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Mar
|
pubmed:issn |
0014-2956
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
1
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pubmed:volume |
228
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
343-50
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:7705348-Amino Acid Sequence,
pubmed-meshheading:7705348-Animals,
pubmed-meshheading:7705348-Base Sequence,
pubmed-meshheading:7705348-Cloning, Molecular,
pubmed-meshheading:7705348-DNA, Complementary,
pubmed-meshheading:7705348-Exons,
pubmed-meshheading:7705348-Glycosylation,
pubmed-meshheading:7705348-Male,
pubmed-meshheading:7705348-Molecular Sequence Data,
pubmed-meshheading:7705348-Multigene Family,
pubmed-meshheading:7705348-Peptides,
pubmed-meshheading:7705348-Proline-Rich Protein Domains,
pubmed-meshheading:7705348-Rats,
pubmed-meshheading:7705348-Rats, Sprague-Dawley,
pubmed-meshheading:7705348-Salivary Proline-Rich Proteins,
pubmed-meshheading:7705348-Salivary Proteins and Peptides
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pubmed:year |
1995
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pubmed:articleTitle |
cDNA cloning and characterization of rat salivary glycoproteins. Novel members of the proline-rich-protein multigene families.
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pubmed:affiliation |
Section of Molecular and Cellular Biology, University of California, Davis 95616, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|