Molecular cloning and characterization of an isoprenylated 67 kDa protein.
The cDNA coding for a 67 kDa protein (p67) was isolated from a rat Schwann cell library. A recombinant form of p67 expressed in bacteria was used to produce polyclonal anti-p67 antibodies. By immunoblot analysis p67 was found to be expressed in most tissues and cell lines examined. Inspection of the deduced amino acid sequence revealed a COOH-terminal consensus sequence for isoprenylation. Consistent with this finding, p67 was a substrate for isoprenylation in vitro by geranylgeranylpyrophosphate. p67 was associated predominantly with the particulate fraction of rat smooth muscle cells. The rat p67 sequence was highly homologous to a family of recently described human and mouse gamma-interferon inducible, guanine nucleotide binding proteins.
Asundi
V K
VK
Sigfried and Janet Weis Center for Research, Geisinger Clinic, Danville, PA 17822-2613.
Stahl
R C
RC
Showalter
L
L
Conner
K J
KJ
Carey
D J
DJ
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics*; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000302:isolation & purification*; D019204:GTP-Binding Proteins / Q000235:genetics*; D008969:Molecular Sequence Data; D017368:Protein Prenylation; D051381:Rats; D017207:Rats, Sprague-Dawley; D012583:Schwann Cells / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
D002352:Carrier Proteins; D018076:DNA, Complementary; C086640:Gbp2 protein, rat; D019204:GTP-Binding Proteins