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Publication : Molecular cloning of a member of a new class of low-molecular-weight GTP-binding proteins.

First Author  Morimoto BH Year  1991
Journal  Genes Dev Volume  5
Issue  12B Pages  2386-91
PubMed ID  1752434 Mgi Jnum  J:2330
Mgi Id  MGI:50854 Doi  10.1101/gad.5.12b.2386
Citation  Morimoto BH, et al. (1991) Molecular cloning of a member of a new class of low-molecular-weight GTP-binding proteins. Genes Dev 5(12B):2386-91
abstractText  We report the cloning of a low-molecular-weight GTP-binding protein that appears to be the first member of a new class of G proteins. This G protein was cloned from the HT4 neural cell line and has the closest homology to the rab, sec4, and ypt1 members of the low-molecular-weight (LMW) G-protein family. The amino acid sequence identity is only 30% with these other LMW G proteins, but in the four conserved GTP-binding domains, amino acid identity increases to 50-100%. A unique feature that distinguishes this G protein from other LMW G proteins is its carboxy-terminal amino acid sequence -Cys-Cys-Pro. In keeping with the current nomenclature for other members of the ras superfamily, we will designate this new class as rah (ras-related homolog). On the basis of sequence homology, rah may function in vesicular trafficking and possibly in neurotransmitter secretion.
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