Latrophilin 2 is a protein that in humans is encoded by the ADGRL2gene.[1][2]
This gene encodes a member of the latrophilin subfamily of G-protein coupled receptors (GPCR). Latrophilins may function in both cell adhesion and signal transduction. In experiments with non-human species, endogenous proteolytic cleavage within a cysteine-rich GPS (G-protein-coupled-receptor proteolysis site) domain resulted in two subunits (a large extracellular N-terminal cell adhesion subunit and a subunit with substantial similarity to the secretin/calcitonin family of GPCRs) being non-covalently bound at the cell membrane. While several transcript variants have been described, the biological validity of only one has been determined.[2]
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Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Oct 1998). "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 5 (5): 277–86. doi:10.1093/dnares/5.5.277. PMID9872452.
White GR, Varley JM, Heighway J (Dec 1998). "Isolation and characterization of a human homologue of the latrophilin gene from a region of 1p31.1 implicated in breast cancer". Oncogene. 17 (26): 3513–9. doi:10.1038/sj.onc.1202487. PMID10030676.
Kreienkamp HJ, Zitzer H, Gundelfinger ED, Richter D, Bockers TM (Oct 2000). "The calcium-independent receptor for alpha-latrotoxin from human and rodent brains interacts with members of the ProSAP/SSTRIP/Shank family of multidomain proteins". The Journal of Biological Chemistry. 275 (42): 32387–90. doi:10.1074/jbc.C000490200. PMID10964907.
Bjarnadóttir TK, Fredriksson R, Höglund PJ, Gloriam DE, Lagerström MC, Schiöth HB (Jul 2004). "The human and mouse repertoire of the adhesion family of G-protein-coupled receptors". Genomics. 84 (1): 23–33. doi:10.1016/j.ygeno.2003.12.004. PMID15203201.
