Members of this family are integral membrane proteins. This family includes a protein with hemolytic activity from Bacillus cereus [1]. It has been proposed that YOL002c encodes a Saccharomyces cerevisiae protein that plays a key role in metabolic pathways that regulate lipid and phosphate metabolism [2]. In eukaryotes, members are seven-transmembrane pass molecules found to encode functional receptors with a broad range of apparent ligand specificities, including progestin and adipoQ receptors, and hence have been named PAQR proteins [3]. The mammalian members include progesterone binding proteins [4]. Unlike the case with GPCR receptor proteins, the evolutionary ancestry of the members of this family can be traced back to the Archaea. This family belongs to the CREST superfamily [5], which are distantly related to GPCRs. [1]. 7495855. Cloning and primary structure of a new hemolysin gene from Bacillus cereus. Baida GE, Kuzmin NP;. Biochim Biophys Acta 1995;1264:151-154. [2]. 11916977. Multiple regulatory roles of a novel Saccharomyces cerevisiae protein, encoded by YOL002c, in lipid and phosphate metabolism. Karpichev IV, Cornivelli L, Small GM;. J Biol Chem 2002;0:0-1. [3]. 16044242. PAQR proteins: a novel membrane receptor family defined by an ancient 7-transmembrane pass motif. Tang YT, Hu T, Arterburn M, Boyle B, Bright JM, Emtage PC, Funk WD;. J Mol Evol. 2005;61:372-380. [4]. 17082257. Steroid and G protein binding characteristics of the seatrout and human progestin membrane receptor alpha subtypes and their evolutionary origins. Thomas P, Pang Y, Dong J, Groenen P, Kelder J, de Vlieg J, Zhu Y, Tubbs C;. Endocrino. TRUNCATED at 1650 bytes (from Pfam)
GO Terms:- Date:
- 2024-10-16