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DESCRIBE <http://purl.uniprot.org/SHA-384/52DDBEC5801594E9788DCC7F8025F71A65155E9C0654E170ECF99DD8589FD254EAD3C04B1B60BD15CDEEEC72C3872577>
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http://purl.uniprot.org/SHA-384/52DDBEC5801594E9788DCC7F8025F71A65155E9C0654E170ECF99DD8589FD254EAD3C04B1B60BD15CDEEEC72C3872577
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/52DDBEC5801594E9788DCC7F8025F71A65155E9C0654E170ECF99DD8589FD254EAD3C04B1B60BD15CDEEEC72C3872577
http://www.w3.org/2000/01/rdf-schema#comment
"Mechanism of PMCA4 that creates lipid asymmetry is well understood in terms of ATP hydrolysis; molecular models exist for trajectory taken by phospholipid substrates through the enzyme. [review-like article]"
xsd:string
http://purl.uniprot.org/uniprot/#_006D072EF55D512B54DFCD8021FB804C5ACA2A86040E76AECDCD5272C7792400B2D1C9F31D5A1B76E60FDA27C1B48C71
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/52DDBEC5801594E9788DCC7F8025F71A65155E9C0654E170ECF99DD8589FD254EAD3C04B1B60BD15CDEEEC72C3872577
http://purl.uniprot.org/uniprot/P23634
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/52DDBEC5801594E9788DCC7F8025F71A65155E9C0654E170ECF99DD8589FD254EAD3C04B1B60BD15CDEEEC72C3872577
http://purl.uniprot.org/uniprot/#_P23634-mappedCitation-25233416
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/52DDBEC5801594E9788DCC7F8025F71A65155E9C0654E170ECF99DD8589FD254EAD3C04B1B60BD15CDEEEC72C3872577