P-domains as shuffled cysteine-rich modules in integumentary mucin C.1 (FIM-C.1) from Xenopus laevis. Polydispersity and genetic polymorphism.
A new frog integumentary mucin (FIM-C.1) has been discovered by molecular cloning. This mucin contains at least six typical P-domains as cysteine-rich modules. Shuffled P-domains have previously been detected in FIM-A.1, and they also form the basis of various P-domain peptides, which presumably have growth-modulating activities. Furthermore, FIM-C.1 contains at least three threonine-rich clusters, which consist of semi-repetitive cassettes. Various polydisperse transcripts have been characterized. They originate from two genes only and differ by deletions/insertions that are congruent with the semi-repetitive cassettes. Thus, polydispersities are probably generated by alternative splicing. Southern analysis revealed genetic polymorphism between different individuals. Furthermore, a specific antiserum was generated against a synthetic peptide deduced from the COOH-terminal end of FIM-C.1 and used for Western analysis.
Hauser
F
F
Max-Planck-Institut für Psychiatrie, Abteilung Neurochemie, Martinsried, Federal Republic of Germany.
Hoffmann
W
W
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D003062:Codon / Q000235:genetics; D003545:Cysteine; D008969:Molecular Sequence Data; D009077:Mucins / Q000235:genetics* / Q000302:isolation & purification; D009838:Oligodeoxyribonucleotides; D016133:Polymerase Chain Reaction; D011110:Polymorphism, Genetic; D015183:Restriction Mapping; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid; D013698:Templates, Genetic; D029867:Xenopus Proteins; D014982:Xenopus laevis
D003062:Codon; C078406:FIM-C.1 protein, Xenopus; D009077:Mucins; D009838:Oligodeoxyribonucleotides; D029867:Xenopus Proteins; D003545:Cysteine