InterPro : IPR004014

Name  Cation-transporting P-type ATPase, N-terminal Short Name  ATPase_P-typ_cation-transptr_N
Type  Domain Description  Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. There are several different types of transmembrane ATPases, which can differ in function (ATP hydrolysis and/or synthesis), structure (e.g., F-, V- and A-ATPases, which contain rotary motors) and in the type of ions they transport [, ]. The different types include:F-ATPases (F1F0-ATPases), which are found in mitochondria, chloroplasts and bacterial plasma membranes where they are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).V-ATPases (V1V0-ATPases), which are primarily found in eukaryotic and they function as proton pumps that acidify intracellular compartments and, in some cases, transport protons across the plasma membrane []. They are also found in bacteria [].A-ATPases (A1A0-ATPases), which are found in Archaea and function like F-ATPases, though with respect to their structure and some inhibitor responses, A-ATPases are more closely related to the V-ATPases [, ].P-ATPases (E1E2-ATPases), which are found in bacteria and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes.E-ATPases, which are cell-surface enzymes that hydrolyse a range of NTPs, including extracellular ATP.P-ATPases (also knownas E1-E2 ATPases) () are found in bacteria and in a number of eukaryotic plasma membranes and organelles []. P-ATPases function to transport a variety of different compounds, including ions and phospholipids, across a membrane using ATP hydrolysis for energy. There are many different classes of P-ATPases, which transport specific types of ion: H+, Na+, K+, Mg2+, Ca2+, Ag+and Ag2+, Zn2+, Co2+, Pb2+, Ni2+, Cd2+, Cu+and Cu2+. P-ATPases can be composed of one or two polypeptides, and can usually assume two main conformations called E1 and E2.This entry represents the conserved N-terminal region found in several classes of cation-transporting P-type ATPases, including those that transport H+(), Na+(), Ca2+(), Na+/K+(), and H+/K+(). In the H+/K+- and Na+/K+-exchange P-ATPases, this domain is found in the catalytic alpha chain. In gastric H+/K+-ATPases, this domain undergoes reversible sequential phosphorylation inducing conformational changes that may be important for regulating the function of these ATPases [, ].
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

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0 Child Features

0 Contains

7 Found In

Id Name Short Name Type
IPR006413 P-type ATPase, subfamily IIA, PMR1-type P-type_ATPase_IIA_PMR1 Family
IPR005782 P-type ATPase, subfamily IIA, SERCA-type P-type_ATPase_IIA Family
IPR005775 P-type ATPase, subfamily IIC P-type_ATPase_IIC Family
IPR006408 P-type ATPase, subfamily IIB P-type_ATPase_IIB Family
IPR006415 P-type ATPase, subfamily IIIB P-type_ATPase_IIIB Family
IPR006534 P-type ATPase, subfamily IIIA P-type_ATPase_IIIA Family
IPR006414 P-type ATPase, subfamily IID P-type_ATPase_IID Family

0 Parent Features

9 Publications

First Author Title Year Journal Volume Pages
Cross RL The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio. 2004 FEBS Lett 576 1-4
Rappas M Mechanisms of ATPases--a multi-disciplinary approach. 2004 Curr Protein Pept Sci 5 89-105
Toei M Regulation and isoform function of the V-ATPases. 2010 Biochemistry 49 4715-23
Grüber G New insights into structure-function relationships between archeal ATP synthase (A1A0) and vacuolar type ATPase (V1V0). 2008 Bioessays 30 1096-109
Schäfer G F-type or V-type? The chimeric nature of the archaebacterial ATP synthase. 1992 Biochim Biophys Acta 1101 232-5
Radax C F-and V-ATPases in the genus Thermus and related species. 1998 Syst Appl Microbiol 21 12-22
Axelsen KB Evolution of substrate specificities in the P-type ATPase superfamily. 1998 J Mol Evol 46 84-101
Fujitani N Structure determination and conformational change induced by tyrosine phosphorylation of the N-terminal domain of the alpha-chain of pig gastric H+/K+-ATPase. 2003 Biochem Biophys Res Commun 300 223-9
Segall L Structural basis for alpha1 versus alpha2 isoform-distinct behavior of the Na,K-ATPase. 2003 J Biol Chem 278 9027-34



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)