Description

IPR006544 is a P-type ATPase, subfamily V.

<p>This entry includes P-type ATPases from eukaryotes that form a different clade, designated subfamily V (P5-ATPases) [[cite:PUB00009616]]. P-type ATPases use ATP for intracellular cation homeostasis and are required for proper lysosomal and mitochondria maintenance [[cite:PUB00096637], [cite:PUB00101911]], also playing a role in the maintenance of neuronal integrity [[cite:PUB00094241]]. P5-type ATPases can be subdivided in two subtypes based on the conservation of residues in the transmembrane domain, the P5A-type, which localize to the ER membrane (ATP13A1 from human and SPF1 from yeast), and P5B-type ATPases which are vacuolar or lysosomal membrane-associated proteins. Humans express four isoforms, ATP13A2 to ATP13A5 [[cite:PUB00151055], [cite:PUB00151056]].</p> <p>SPF1 from yeast and ATP13A1 are ER translocases required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum [[cite:PUB00096637], [cite:PUB00151058]]. They were initially thought to mediate ion transport such as calcium or manganese but then it was reported that they specifically binds moderately hydrophobic transmembrane with short hydrophilic lumenal domains that misinsert into the endoplasmic reticulum [[cite:PUB00096637], [cite:PUB00151061], [cite:PUB00151059]].</p> <p>Human ATP13A2 (also known as PARK9), the most studied member of the P5B-type, is a neuroprotective ATPase enriched in the brain that selectively imports spermine ions from lysosomes into the cytosol [[cite:PUB00094240], [cite:PUB00101910], [cite:PUB00151060]]. Mutations ATP13A2 cause a rare monogenic form of juvenile-onset Parkinson's disease named Kufor-Rakeb syndrome and other neurodegenerative diseases [[cite:PUB00151057]].</p> <p>This entry includes also other isoforms such as ATP13A3, ATP13A4, ATP13A5.</p> <p>P-ATPases (also known as E1-E2 ATPases) ([ec:3.6.3.-]) are found in bacteria and in a number of eukaryotic plasma membranes and organelles [[cite:PUB00009616]]. 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.</p> <p>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.</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 2

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: