Cloning and sequence analysis of human pituitary cDNA encoding the novel polypeptide 7B2

FEBS Lett. 1988 Jul 4;234(1):160-4. doi: 10.1016/0014-5793(88)81324-3.


Application of a differential hybridization technique led to the isolation of a human pituitary cDNA clone encoding the complete structure of the polypeptide 7B2. This protein of unknown function, which is sorted to secretory granules, appears to be present selectively in neurons and endocrine cells. The polypeptide chain of human 7B2, preceded by a cleaved signal peptide, comprises 185 amino acids (a calculated Mr of 20,793). Interesting features of the highly-conserved 7B2 structure include (i) a serine phosphorylation consensus sequence, (ii) the occurrence of three pairs of dibasic amino acids representing potential proteolytic cleavage sites and, in particular, (iii) the presence of three regions homologous to GTP-binding domains giving 7B2 structural characteristics of a GTP-binding protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Biological Evolution
  • Cloning, Molecular*
  • DNA / genetics*
  • DNA / isolation & purification
  • DNA, Recombinant
  • GTP-Binding Proteins / genetics
  • Humans
  • Molecular Sequence Data
  • Nerve Tissue Proteins*
  • Neuroendocrine Secretory Protein 7B2
  • Nucleic Acid Hybridization
  • Pituitary Gland / analysis*
  • Pituitary Hormones / genetics*
  • Protein Processing, Post-Translational
  • Protein Sorting Signals
  • RNA, Messenger / genetics
  • Sequence Homology, Nucleic Acid
  • Xenopus laevis


  • DNA, Recombinant
  • Nerve Tissue Proteins
  • Neuroendocrine Secretory Protein 7B2
  • Pituitary Hormones
  • Protein Sorting Signals
  • RNA, Messenger
  • SCG5 protein, human
  • DNA
  • GTP-Binding Proteins

Associated data

  • GENBANK/Y00757