A new repetitive protein from Xenopus laevis skin highly homologous to pancreatic spasmolytic polypeptide.
A cDNA sequence has been used to derive the precursor structure of a highly repetitive protein in Xenopus laevis skin. From the sequence of a whole family of secretory proteins can be predicted containing a classical hydrophobic signal sequence at the NH2-terminal end of the precursor. The proteins contain four domains with high homology to porcine pancreatic spasmolytic polypeptide. These four cysteine-rich, presumably physiologically active domains are separated in the molecule by a repetitive element, locating two such domains to the NH2 terminus of the precursor protein and the remaining two to the COOH-terminal end. The separating spacer consists of very unusual, precise, threonine and proline-rich repeats containing 9 residues which could be targets for extensive O-glycosylation. Additionally, processing at two pairs of basic residues is suggested to liberate two polypeptides ("spasmolysins") and "spasmolysin-glycoprotein."
Hoffmann
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Max-Planck-Institut für Psychiatrie, Abteilung Neurochemie, Martinsried Federal Republic of Germany.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004247:DNA / Q000032:analysis; D036341:Intercellular Signaling Peptides and Proteins; D008969:Molecular Sequence Data; D009077:Mucins; D009124:Muscle Proteins; D009479:Neuropeptides; D010276:Parasympatholytics / Q000032:analysis*; D010455:Peptides / Q000032:analysis*; D012091:Repetitive Sequences, Nucleic Acid; D012867:Skin / Q000032:analysis*; D000071164:Trefoil Factor-2; D000071165:Trefoil Factor-3; D014982:Xenopus laevis
D036341:Intercellular Signaling Peptides and Proteins; D009077:Mucins; D009124:Muscle Proteins; D009479:Neuropeptides; D010276:Parasympatholytics; D010455:Peptides; C099037:TFF3 protein, rat; C000604008:Tff2 protein, rat; D000071164:Trefoil Factor-2; D000071165:Trefoil Factor-3; C034407:pancreatic spasmolytic polypeptide; D004247:DNA