Structure and chromosomal localization of the mammalian agrin gene.
Agrin, a component of the synaptic basal lamina, has been shown to induce clustering of ACh receptors on the surface of muscle fibers. Analysis of cDNAs isolated from a rat embryonic spinal cord library demonstrated that agrin contains domains similar to regions of protease inhibitors, laminin and epidermal growth factor. The domain structure of agrin is further revealed here in an analysis of the agrin gene. Two additional internal repeated sequences are defined: one rich in cysteine residues with no homology to other proteins, and another similar to the laminin G domain, which is involved in heparin binding. Alternative RNA splicing at two positions in the gene predicts up to eight possible forms of the agrin protein. The gene (symbol AGRN/Agrn) has been assigned to chromosome 1 region pter-p32 in human and to mouse chromosome 4.
Rupp
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F
Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University School of Medicine, California 94305.
Ozçelik
T
T
Linial
M
M
Peterson
K
K
Francke
U
U
Scheller
R
R
D018171:Agrin; D000818:Animals; D001483:Base Sequence; D002874:Chromosome Mapping; D004247:DNA / Q000302:isolation & purification; D004622:Embryo, Mammalian / Q000378:metabolism; D005796:Genes; D006801:Humans; D007536:Isomerism; D051379:Mice / Q000235:genetics; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000235:genetics*; D012326:RNA Splicing; D013116:Spinal Cord
D018171:Agrin; D009419:Nerve Tissue Proteins; D004247:DNA