Open AccessThe axonally secreted cell adhesion molecule, axonin‐1
Author(s) -
ZUELLIG Richard A.,
RADER Christoph,
SCHROEDER Annelies,
KALOUSEK Markus B.,
BOHLEN UND HALBACH Friedrich,
OSTERWALDER Thomas,
INAN Canan,
STOECKLI Esther T.,
AFFOLTER H.Urs,
FRITZ Andreas,
HAFEN Ernst,
SONDEREGGER Peter
Publication year - 1992
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1992.tb16655.x
Subject(s) - complementary dna , signal peptide , amino acid , fibronectin , peptide sequence , microbiology and biotechnology , biology , molecular cloning , nucleic acid sequence , biochemistry , chemistry , gene , cell
Axonin‐1 is an axon‐associated cell adhesion molecule (AxCAM) of the chicken, which promotes neurite outgrowth by interaction with the AxCAM L1(G4) of the neuritic membrane. Here we report the cloning and sequence determination of a cDNA encoding axonin‐1. Peptides generated by enzymatic cleavage showed similarity to the AxCAM F11. Degenerated polymerase chain reaction (PCR) primers were designed and an axonin‐1 fragment was amplified from mRNA of embryonic retina. Screening of a cDNA library from embryonic brain resulted in the isolation of a 4.0‐kb cDNA insert with an open reading frame of 3108 nucleotides. The deduced polypeptide of 1036 amino acids includes a putative hydrophobic N‐terminal signal sequence of 23 or 25 amino acids and a C‐terminal hydrophobic sequence of 29 amino acids which is suggestive of sequences serving as signal for the attachment of a glycosyl‐phosphatidylinositol (glycosyl‐PtdIns) anchor. The putative mature form of axonin‐1 comprises six immunoglobulin‐like repeats, followed by four fibronectin‐type III repeats. Axonin‐1 exhibits 75% amino acid identity with the AxCAM TAG‐1 of the rat, suggesting that it is the chicken homologue of TAG‐1. Like TAG‐1, axonin‐1 is glycosyl‐PtdIns‐anchored to the neuronal membrane; in contrast to TAG‐1, it does not exhibit an Arg‐Gly‐Asp sequence.