The primary sequence of the PFK-1 inactivating zinc-binding protein as deduced from cDNA sequencing. Identity of the zinc-binding protein with rat parathymosin.
We have recently described the sequence of the Zn2+-binding domain (43 amino acid residues) of a newly detected Zn2+-binding protein which reversibly inactivates phosphofructokinase-1 in a Zn2+-dependent manner [(1986) J. Biol. Chem. 269, 5895-5900; (1988) Eur. J. Biochem. 177, 561-568]. Here, we describe the primary sequence of this protein based on a full-length cDNA. A sequence comparison reveals the identity of the Zn2+-binding protein with a protein called parathymosin-alpha.
Trompeter
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HI
Abteilung Klinische Biochemie, Universität Göttingen, FRG.
Brand
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Söling
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D036341:Intercellular Signaling Peptides and Proteins; D008667:Metalloproteins / Q000235:genetics*; D008969:Molecular Sequence Data; D015345:Oligonucleotide Probes; D011506:Proteins / Q000235:genetics*; D012333:RNA, Messenger / Q000235:genetics; D051381:Rats; D013947:Thymosin / Q000031:analogs & derivatives* / Q000235:genetics; D015032:Zinc / Q000502:physiology
D036341:Intercellular Signaling Peptides and Proteins; D008667:Metalloproteins; D015345:Oligonucleotide Probes; D011506:Proteins; C048633:Ptms protein, rat; D012333:RNA, Messenger; D013947:Thymosin; D004247:DNA; C044498:parathymosin alpha; D015032:Zinc