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Phospholipid translocation also seems to be implicated in vesicle formation and in uptake of lipid signaling molecules. The beta subunit may assist in binding of the phospholipid substrate. Required for the proper folding, assembly and ER to Golgi exit of the ATP8A2:CDC50A flippase complex. ATP8A2:CDC50A may be involved in regulation of neurite outgrowth, and, reconstituted to liposomes, predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). The ATP8A1:CDC50A flippase complex seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane. Required for the formation of the ATP8A2, ATP8B1 and ATP8B2 P-type ATPAse intermediate phosphoenzymes. Involved in uptake of platelet-activating factor (PAF). Can also mediate the export of alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B and ATP11C from the ER to other membrane localizations"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9NV96"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23269685"}],"value":"Component of various P4-ATPase flippase complexes which consists of a catalytic alpha subunit and an accessory beta subunit. Interacts with ATP8A1 to form a flippase complex; this complex forms an intermediate phosphoenzyme. The ATP8A2:CDC50A flippase complex has been purified, and ATP8B1:CDC50A and ATP8B2:CDC50A flippase complexes have been shown to form intermediate phosphoenzymes in vitro (By similarity). Interacts with alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B and ATP11C (PubMed:23269685, PubMed:29799007, PubMed:30018401)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q8VEK0","intActId":"EBI-8381028"},"interactantTwo":{"uniProtKBAccession":"P70704","geneName":"Atp8a1","intActId":"EBI-20828407"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q8VEK0","intActId":"EBI-8381028"},"interactantTwo":{"uniProtKBAccession":"P05067-4","geneName":"APP","intActId":"EBI-302641"},"numberOfExperiments":6,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"Q8VEK0","intActId":"EBI-8381028"},"interactantTwo":{"uniProtKBAccession":"P05067","geneName":"APP","chainId":"PRO_0000000091","intActId":"EBI-3894543"},"numberOfExperiments":3,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22253360"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22253360"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Cell membrane","id":"SL-0039"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22253360"}],"value":"Golgi apparatus","id":"SL-0132"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22253360"}],"value":"Cytoplasmic vesicle, secretory vesicle membrane","id":"SL-0245"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22253360"}],"value":"Apical cell membrane","id":"SL-0015"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22253360"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22307598"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24413176"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30018401"}],"value":"Expressed in photoreceptor cells; detected in retina outer segment (at protein level). 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