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Literature summary for 7.6.2.1 extracted from

  • Baldridge, R.D.; Graham, T.R.
    Identification of residues defining phospholipid flippase substrate specificity of type IV P-type ATPases (2012), Proc. Natl. Acad. Sci. USA, 109, E290-E298.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.6.2.1

Protein Variants

Protein Variants Comment Organism
F511L the mutant has a specific activity that is 35% that of wild type Drs2 Saccharomyces cerevisiae
F511Y the mutant retains wild type activity, the substitution in Drs2 specifically abrogates phosphatidylserine recognition by this flippase causing phosphatidylserine exposure on the outer leaflet of the plasma membrane without disrupting phospatidylethanolamine asymmetry Saccharomyces cerevisiae
Y618F acquisition of the phosphatidylserine substrate maps to a Tyr618Phe substitution in transmembrane segment 4 of Dnf1. The rate of 7-nitrobenz-2–oxa-1,3-diazol-4-yl phospholipid uptake by Dnf1 Y618F is comparable to wild type Dnf1 Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P32660
-
-
Saccharomyces cerevisiae P39524
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + phosphatidylcholine/in
-
 Saccharomyces cerevisiae ADP + phosphate + phosphatidylcholine/out
-
 ?
ATP + H2O + phosphatidylcholine/in preferred substrate of Dnf1 Saccharomyces cerevisiae ADP + phosphate + phosphatidylcholine/out
-
 ?
ATP + H2O + phosphatidylserine/in
-
 Saccharomyces cerevisiae ADP + phosphate + phosphatidylserine/out
-
 ?
ATP + H2O + phosphatidylserine/in preferred substrate of Drs2 Saccharomyces cerevisiae ADP + phosphate + phosphatidylserine/out
-
 ?
additional information wild type Dnf1 cannot translocate NBD-SM or NBD-PA Saccharomyces cerevisiae ?
-
 ?

Synonyms

Synonyms Comment Organism
Dnf1
-
 Saccharomyces cerevisiae
Drs2
-
 Saccharomyces cerevisiae
P4-ATPase
-
 Saccharomyces cerevisiae
phospholipid flippase
-
 Saccharomyces cerevisiae
type IV P-type ATPase
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function type IV P-type ATPases catalyzes translocation of phospholipid across a membrane to establish an asymmetric bilayer structure with phosphatidylserine and phosphatidylethanolamine restricted to the cytosolic leaflet Saccharomyces cerevisiae