Open AccessThe nucleotide and partial amino acid sequences of rat fetuin
Author(s) -
RAUTH Günther,
PÖSCHKE Oliver,
FINK Edwin,
EULITZ Manfred,
TIPPMER Stefanie,
KELLERER Monika,
HÄRING HansUlrich,
NAWRATIL Peter,
HAASEMANN Martina,
JAHNENDECHENT Willi,
MÜLLERESTERL Werner
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.tb16663.x
Subject(s) - complementary dna , amino acid , fetuin , biology , microbiology and biotechnology , open reading frame , peptide sequence , biochemistry , nucleic acid sequence , tyrosine , gene , glycoprotein
Fetuins are among the major plasma proteins, yet their biological role has remained elusive. Here we report the molecular cloning of rat fetuin and the sequence analysis of a full‐length clone, RF619 of 1456 bp with an open reading frame of 1056 bp encoding 352 amino acid residues. The coding part of RF619 was identical with the cDNA sequence of the natural inhibitor of the insulin receptor tyrosine kinase from rat (pp63) except for four substitutions and a single base insertion causing divergence of the predicted protein sequences. Partial amino acid sequences of rat plasma fetuin were in agreement with the predictions based on the RF619 cDNA. Purified rat fetuin inhibited the insulin receptor tyrosine kinase in vitro . Therefore, we conclude that RF619 and pp63 cDNA encode the same protein, i.e. authentic rat fetuin which is a functional tyrosine kinase inhibitor.