Flippase that catalyzes in an ATP-dependent manner the transport of retinal-phosphatidylethanolamine conjugates like the 11-cis and all-trans isomers of N-retinylidene-phosphatidylethanolamine from the lumen to the cytoplasmic leaflet of photoreceptor outer segment disk membranes, where N-cis-retinylidene-phosphatidylethanolamine (N-cis-R-PE) is then isomerized to its all-trans isomer (N-trans-R-PE) and reduced by RDH8 to produce all-trans-retinol (all-trans-rol) and therefore prevents the accumulation of excess of 11-cis-retinal and its schiff-base conjugate and the formation of toxic bisretinoid (PubMed:10852960, PubMed:10412977, PubMed:22735453). Displays both ATPase and GTPase activity that is strongly influenced by the lipid environment and the presence of retinoid compounds (By similarity). Binds the unprotonated form of N-retinylidene-phosphatidylethanolamine with high affinity in the absence of ATP and ATP binding and hydrolysis induce a protein conformational change that causes the dissociation of N-retinylidene-phosphatidylethanolamine (By similarity). ATP + H2O + N-all-trans-retinylidenephosphatidylethanolamine(out) = ADP + H(+) + N-all-trans-retinylidenephosphatidylethanolamine(in) + phosphate ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2. a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) + phosphate ATP + H2O + N-11-cis-retinylidenephosphatidylethanolamine(out) = ADP + H(+) + N-11-cis-retinylidenephosphatidylethanolamine(in) + phosphate ATPase activity is decreased by cholesterol and ceramide. ATPase activity is stimulated by phosphatidylethanolamine. Phospholipids translocase activity is highly reduced by berylium fluoride and aluminum floride. N-ethylmaleimide inhibits phospholipid translocase activity. Localized to the rim and incisures of rod outer segments disks. Retinal-specific (PubMed:9202155). Seems to be exclusively found in the rims of rod photoreceptor cells. The second extracellular domain (ECD2, aa 1395-1680) undergoes conformational change in response to its specific interaction with its substrate all-trans-retinal. Nucleotide binding domain 1 (NBD1, aa 854-1375) binds preferentially and with high affinity with the 11-cis retinal. N-glycosylated. Proteolytic cleavage by trypsin leads to a 120-kDa N-terminal fragment and a 115-kDa C-terminal fragment that are linked through disulfide bonds. Phosphorylation is independent of light exposure and modulates ATPase activity. Delayed dark adaptation but normal final rod threshold. Belongs to the ABC transporter superfamily. ABCA family.