6533b871fe1ef96bd12d10f8
RESEARCH PRODUCT
The nucleotide and partial amino acid sequences of rat fetuin. Identity with the natural tyrosine kinase inhibitor of the rat insulin receptor.
Hans-ulrich HäringManfred EulitzWerner Müller-esterlOliver PöschkeGünther RauthEdwin FinkStefanie TippmerWilli Jahnen-dechentMartina HaasemannMonika KellererPeter Nawratilsubject
Sequence analysisMolecular Sequence DataBiochemistryTropomyosin receptor kinase CReceptor tyrosine kinaseSubstrate SpecificityComplementary DNASequence Homology Nucleic AcidAnimalsAmino Acid SequencePhosphorylationchemistry.chemical_classificationbiologyBase SequenceDNAProtein-Tyrosine KinasesFetuinMolecular biologyReceptor InsulinAmino acidRatsInsulin receptorBiochemistrychemistryROR1biology.proteinalpha-Fetoproteinsdescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1992-03-01 | European journal of biochemistry |