InterPro : IPR006413

Name  P-type ATPase, subfamily IIA, PMR1-type Short Name  P-type_ATPase_IIA_PMR1
Type  Family 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 known as 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 family represents the P-type ATPase responsible for translocating calcium ions across the golgi membrane of fungi and animals [, ]and is of particular importance in the sarcoplasmic reticulum of skeletal and cardiac muscle in vertebrates []. The calcium P-type ATPases have been characterised as Type IIA based on a phylogenetic analysis which distinguishes this group from the Type IIB PMCA calcium pump []described in . A separate analysis divides Type IIA into sub-types, SERCA and PMR1 []the former of which is described in .

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



2 Child Features

Id Name Short Name Type
IPR030336 Calcium-transporting ATPase type 2C member 1 ATP2C1 Family
IPR030334 Calcium-transporting ATPase type 2C member 2 ATP2C2 Family

4 Contains

Id Name Short Name Type
IPR008250 P-type ATPase, A domain ATPase_P-typ_transduc_dom_A Domain
IPR004014 Cation-transporting P-type ATPase, N-terminal ATPase_P-typ_cation-transptr_N Domain
IPR006068 Cation-transporting P-type ATPase, C-terminal ATPase_P-typ_cation-transptr_C Domain
IPR018303 P-type ATPase, phosphorylation site ATPase_P-typ_P_site PTM

0 Found In

1 Parent Features

Id Name Short Name Type
IPR001757 P-type ATPase P_typ_ATPase Family

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
Pittman JK Two additional type IIA Ca(2+)-ATPases are expressed in Arabidopsis thaliana: evidence that type IIA sub-groups exist. 1999 Gene 236 137-47
Rudolph HK The yeast secretory pathway is perturbed by mutations in PMR1, a member of a Ca2+ ATPase family. 1989 Cell 58 133-45

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)