Preferred Label : P-type ATPases;
MeSH definition : A highly conserved family of ATPases that facilitate the transport of lipids and cations
across the plasma membrane. Structurally, they are elongated ALPHA-HELICES constituting
five functionally distinct domains: three cytoplasmic domains A, N, and P which contain
the catalytic sites, and two transmembrane domains. The N domain phosphorylates the
P-domain at an invariant ASPARTATE residue, which, in turn, is dephosphorylated by
the A domain. The phosphorylation and dephosphorylation cycles drive conformational
changes in the protein between two states (E1 and E2), which allow the substrate to
access the other side of the membrane.;
MeSH synonym : ATPases, P-type; P type ATPases; Phosphorylation-type ATPases; ATPases, Phosphorylation-type; Phosphorylation type ATPases; P-type Adenosine Triphosphatases; Adenosine Triphosphatases, P-type; P type Adenosine Triphosphatases; Triphosphatases, P-type Adenosine; Phosphorylation-type Adenosine Triphosphatases; Adenosine Triphosphatases, Phosphorylation-type; Phosphorylation type Adenosine Triphosphatases; Triphosphatases, Phosphorylation-type Adenosine; E1-E2 ATPases; ATPases, E1-E2; E1 E2 ATPases; P-type Adenosine Triphosphatase; Adenosine Triphosphatase, P-type; P type Adenosine Triphosphatase; Triphosphatase, P-type Adenosine; P-type ATPase; ATPase, P-type; P type ATPase; Atpase, P Type; Type Atpase, P; E1-E2 ATPase; ATPase, E1-E2; E1 E2 ATPase;
Registry Number MeSH : EC 3.6.3.-;
Origin ID : D000073779;
UMLS CUI : C4505118;
Allowable qualifiers
- Automatic exact mappings (from CISMeF team)
- Record concept(s)
- Related MeSH Supplementary Concept(s)
- Semantic type(s)
A highly conserved family of ATPases that facilitate the transport of lipids and cations
across the plasma membrane. Structurally, they are elongated ALPHA-HELICES constituting
five functionally distinct domains: three cytoplasmic domains A, N, and P which contain
the catalytic sites, and two transmembrane domains. The N domain phosphorylates the
P-domain at an invariant ASPARTATE residue, which, in turn, is dephosphorylated by
the A domain. The phosphorylation and dephosphorylation cycles drive conformational
changes in the protein between two states (E1 and E2), which allow the substrate to
access the other side of the membrane.
