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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

LOC396897  -  apomucin

Sus scrofa

 
 
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Disease relevance of LOC396897

 

High impact information on LOC396897

  • Moreover, immunoblots of apomucin prepared in the presence or the absence of protease inhibitors, with antibodies specific for the half-cystine-rich domains or the tandem repeat sequences, show that the half-cystine-rich domain is absent in apomucin unless protease inhibitors are present throughout [2].
  • The molecular weight of undegraded apomucin has not been established exactly, but gel filtration in 6 M guanidine hydrochloride suggests that it is considerably higher than 250,000 [2].
  • The amino acid composition of apomucin isolated in the absence of protease inhibitors was shown earlier (Eckhardt, A. E., Timpte, C. S., Abernethy, J. L., Toumadje, A., Johnson, W. C., Jr., and Hill, R. L. (1987) J. Biol. Chem. 282, 11339-11344) to be devoid of half-cystine [2].
  • The nucleotide sequence of 1510 bases in the 3.7-kilobase cDNA insert of lambda PSM103 has been established, thereby giving a deduced amino acid sequence of 503 residues in apomucin, or about 45% of the molecule [1].
  • Although the sequences around 192 serine and threonine residues have been established in apomucin, a recognition sequence for the N-acetylgalactosaminyltransferase that initiates glycosylation of apomucin is not evident, except that the glycosylated residues occur in turns [1].
 

Biological context of LOC396897

  • Moreover, the peptide was isolated in 760% yield, indicating that the tandem repeat occurs at least eight times in apomucin [1].
  • The presence of such a long repetitive region in the gene for apomucin raises the possibility for considerable polymorphism in the gene and a corresponding size heterogeneity of apomucin [1].
  • We now describe the complete sequence and genomic organization of the apomucin encoded by 43 exons [3].
 

Anatomical context of LOC396897

 

Associations of LOC396897 with chemical compounds

 

Analytical, diagnostic and therapeutic context of LOC396897

References

  1. Porcine submaxillary gland apomucin contains tandemly repeated, identical sequences of 81 residues. Timpte, C.S., Eckhardt, A.E., Abernethy, J.L., Hill, R.L. J. Biol. Chem. (1988) [Pubmed]
  2. Porcine submaxillary mucin contains a cystine-rich, carboxyl-terminal domain in addition to a highly repetitive, glycosylated domain. Eckhardt, A.E., Timpte, C.S., Abernethy, J.L., Zhao, Y., Hill, R.L. J. Biol. Chem. (1991) [Pubmed]
  3. The gene encoding mouse Muc19: cDNA, genomic organization and relationship to Smgc. Culp, D.J., Latchney, L.R., Fallon, M.A., Denny, P.A., Denny, P.C., Couwenhoven, R.I., Chuang, S. Physiol. Genomics (2004) [Pubmed]
  4. The subcellular localization of apomucin and nonreducing terminal N-acetylgalactosamine in porcine submaxillary glands. Deschuyteneer, M., Eckhardt, A.E., Roth, J., Hill, R.L. J. Biol. Chem. (1988) [Pubmed]
  5. Structural properties of porcine submaxillary gland apomucin. Eckhardt, A.E., Timpte, C.S., Abernethy, J.L., Toumadje, A., Johnson, W.C., Hill, R.L. J. Biol. Chem. (1987) [Pubmed]
  6. A novel approach for chemically deglycosylating O-linked glycoproteins. The deglycosylation of submaxillary and respiratory mucins. Gerken, T.A., Gupta, R., Jentoft, N. Biochemistry (1992) [Pubmed]
 
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