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- W2392742449 abstract "In order to reveal the construction features of goat IGFBP-5 and provide a basis for further study on its expression and physical function in goat growth and development,IGFBP-5 CDS was cloned from liver of newborn Nanjiang Mongolian Grazelle,and analyzed using biology softwares,for instance:ExPasy,NetPhos,NetOGlyc,and SignalP.The whole length of IGFBP-5 CDS was 819bp(GC 64.96%) and encoded 272 amino acid residues.The theory values of IGFBP-5 pI and molecular weight were 8.56 and 30.392kD,respectively.Residues 1 to 19 at N-terminal formed signal peptide,and there were two hydrophilic regions and five hydrophobic regions in primary sequence of goat IGFBP-5,while the grand average of hydroppathicity(GRAVY) was-0.619,and sub-cellular localization was extracellular for mature peptide.Followed by alpha helix(13.6%) and extended strand(2.6%),random coil(83.8%) was most common.Insulin-like growth factor-binding protein(IGFBP) N-terminal domain signature and thyroglobulin type-1 repeat signature in C-terminal region were found.There were 3 O-glycosylation sites and 22 phosphorylation sites,and the main modification included CKⅡ,PKA,PKC,and MAPK.The homology of nucleotide and amino acid sequence of goat IGFBP-5 gene with others was above 89% and 94%,respectively,in addition,the N-terminal sequences were same among species.There was one particular amino acid insertion in primary IGFBP-5 of human(Leu3) and goat(Ala102).The results indicated that IGFBP-5 of goat was a weakly hydrophilic secretory protein with signal peptide,and phosphorylation was the main factor to regulate its function." @default.
- W2392742449 created "2016-06-24" @default.
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- W2392742449 date "2011-01-01" @default.
- W2392742449 modified "2023-09-23" @default.
- W2392742449 title "Molecular Cloning and Characterization of Goat IGFBP-5 Gene" @default.
- W2392742449 hasPublicationYear "2011" @default.
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