Latrophilin 2 is a protein that in humans is encoded by the ADGRL2gene.[5][6]
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.[6]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^White GR, Varley JM, Heighway J (Apr 2000). "Genomic structure and expression profile of LPHH1, a 7TM gene variably expressed in breast cancer cell lines". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1491 (1–3): 75–92. doi:10.1016/s0167-4781(00)00020-8. PMID10760572.
Südhof TC (2001). "alpha-Latrotoxin and its receptors: neurexins and CIRL/latrophilins". Annual Review of Neuroscience. 24 (1): 933–62. doi:10.1146/annurev.neuro.24.1.933. PMID11520923.
Ushkaryov YA, Volynski KE, Ashton AC (Apr 2004). "The multiple actions of black widow spider toxins and their selective use in neurosecretion studies". Toxicon. 43 (5): 527–42. doi:10.1016/j.toxicon.2004.02.008. PMID15066411.
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.
