Fig. 2
From: Identification of a Novel V1-type AVP Receptor Based on the Molecular Recognition Theory
Sequences and structural features of the V6 cDNA encoded AVP V1-type receptor. (A) The nucleotide sequence of the 1.7-Kb V6 cDNA is presented with the deduced amino acid sequence (in single letter amino acid code). The ORF contains the initiating methionine that is identified by 9/13 identity with the Kozak consensus sequence (21). A single putative transmembrane domain (H-1) is predicted based on the Kyte-Doolittle scale with a window of 17 amino acids (22,23). The single region of highest identity with the AVP cRNA-based oligonucleotide probe is marked [ ], showing 86% identity over a stretch of 22 nucleotides; identical nucleotides are dotted. The serine residue within the consensus sequence for a potential PKC phosphorylation site is highlighted. (B) Proposed structure of the V6 cDNA encoded AVP V1-type receptor. Based on the localization of a single 17 amino acid-long hydrophobic region (H-1) as putative transmembrane domain and the putative AVP binding domain (AVP) proximal to H-1, the putative structure is oriented with the N-terminus extracellularly and the C-terminus intracellularly. Black circles highlight the putative AVP binding domain and the potential PKC-phosphorylation site. (C) Comparison of the AVP cRNA sequence with the nucleotide and amino acid sequence of the V6 encoded AVP receptor identifies aa22–29 as potential AVP binding domain. The stippled areas indicate regions of homology. Nucleotides encompassing the AVP binding domain that are present in identical codon position within the AVP antisense peptide frame 2 are indicated by asterisks.