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In molecular biology, copines is a name for the group of human proteins that includes members such as CPNE1, CPNE4, CPNE6, and CPNE8.[1] These are highly conserved, calcium-dependent membrane proteins found in a variety of eukaryotes.[2] The domain structure of these 55 kDa [3] proteins suggests that they may have a role in membrane trafficking in some prokaryotes as well as eukaryotes.[4] Copines contains two C2 domains which play a role in signal transduction by binding to calcium, phospholipids, or polyphosphates. The core domain located at the C-terminus part of the copine is found to have a unique and conserved primary sequence. The function of the core domain is still uncertain, however, researchers believe it has a similar function to the "A domain" in integrins.[3]


  1. ^ "copine family". UniProtKB. Retrieved 28 March 2013.
  2. ^ Damer, Cynthia K; Marina Bayeva; Emily S Hahn; Javier Rivera; Catherine I Socec (2005). "Copine A, a calcium-dependent membrane-binding protein, transiently localizes to the plasma membrane and intracellular vacuoles in Dictyostelium". BMC Cell Biology. 6: 46. doi:10.1186/1471-2121-6-46. PMC 1327671. PMID 16343335.
  3. ^ a b Tomsig, Jose Luis; Creutz, Carl E. (2000-12-01). "Biochemical Characterization of Copine: A Ubiquitous Ca2+-Dependent, Phospholipid-Binding Protein". Biochemistry. 39 (51): 16163–16175. doi:10.1021/bi0019949. ISSN 0006-2960.
  4. ^ Creutz CE, Tomsig JL, Snyder SL, Gautier MC, Skouri F, Beisson J, Cohen J (Feb 1998). "The copines, a novel class of C2 domain-containing, calcium-dependent, phospholipid-binding proteins conserved from Paramecium to humans". J Biol Chem. 273 (3): 1393–402. doi:10.1074/jbc.273.3.1393. PMID 9430674.