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ATPase

The plasma membrane H(+) ATPase of plants and fungi generates a proton gradient that drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses. Forms a functional cation-translocating unit with CNGC17 that is activated by PSKR1/BAK1 and possibly other BAK1/RLK complexes .

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ATPase 1, plasma membrane-type

Also known as ATPase 1, plasma membrane-type (Proton pump 1).
Encodes a plasma membrane proton ATPase. Mutants have a reduced ability to close their stomata in response to drought and are affected in stomatal but not seed responsiveness to ABA.

ATPase 11, plasma membrane-type

Also known as ATPase 11, plasma membrane-type (Proton pump 11).
The plasma membrane H+ ATPase of plants and fungi generates a proton gradient that drives the active transport of nutrients by H+-symport. The resulting external acidification and/or internal alkinization may mediate growth responses ().

ATPase 2, plasma membrane-type

Also known as ATPase 2, plasma membrane-type (Proton pump 2).
belongs to the P-type ATPase superfamily of cation-transporting ATPases, pumps protons out of the cell, generating a proton gradient that drives the active transport of nutrients by proton symport. has two autoinhibitory regions within the C-terminal dom

ATPase 5, plasma membrane-type

Also known as ATPase 5, plasma membrane-type (Proton pump 5).
The plasma membrane H+ ATPase of plants and fungi generates a proton gradient that drives the active transport of nutrients by H+-symport. The resulting external acidification and/or internal alkinization may mediate growth responses ().

ATPase 6, plasma membrane-type

Also known as ATPase 6, plasma membrane-type (Proton pump 6).
The plasma membrane H+ ATPase of plants and fungi generates a proton gradient that drives the active transport of nutrients by H+-symport. The resulting external acidification and/or internal alkinization may mediate growth responses ().

ATPase 7, plasma membrane-type

Also known as ATPase 7, plasma membrane-type (Proton pump 7).
The plasma membrane H+ ATPase of plants and fungi generates a proton gradient that drives the active transport of nutrients by H+-symport. The resulting external acidification and/or internal alkinization may mediate growth responses ().

ATPase 8, plasma membrane-type

Also known as ATPase 8, plasma membrane-type (Proton pump 8).
The plasma membrane H+ ATPase of plants and fungi generates a proton gradient that drives the active transport of nutrients by H+-symport. The resulting external acidification and/or internal alkinization may mediate growth responses ().

ATPase 9, plasma membrane-type

Also known as ATPase 9, plasma membrane-type (Proton pump 9).
The plasma membrane H+ ATPase of plants and fungi generates a proton gradient that drives the active transport of nutrients by H+-symport. The resulting external acidification and/or internal alkinization may mediate growth responses.

ATPase asna1

Also known as ATPase asna1 (Arsenical pump-driving ATPase) (Arsenite-stimulated ATPase).
ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting.

ATPase asna-1

Also known as ATPase asna-1 (Arsenical pump-driving ATPase) (Arsenite-stimulated ATPase).
ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting (). May be involved in insulin signaling.

ATPase ASNA1 homolog

Also known as ATPase ASNA1 homolog (Arsenical pump-driving ATPase homolog) (Arsenite-stimulated ATPase).
ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting.

ATPase ASNA1 homolog 1

Also known as ATPase ASNA1 homolog 1 (Arsenical pump-driving ATPase homolog 1) (Arsenite-stimulated ATPase 1).
ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting.

ATPase ASNA1 homolog 2

Also known as ATPase ASNA1 homolog 2 (Arsenical pump-driving ATPase homolog 2) (Arsenite-stimulated ATPase 2).
ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting.

ATPase GET3

Also known as ATPase GET3 (Arsenical pump-driving ATPase) (Arsenite-stimulated ATPase) (Golgi to ER traffic protein 3) (Guided entry of tail-anchored proteins 3).
ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting.

ATPase SWSAP1

SWSAP1: ATPase which is preferentially stimulated by single- stranded DNA and is involved in homologous recombination repair (HRR). Has a DNA-binding activity which is independent of its ATPase activity.

Molecular Function: ATPase activity; single-stranded DNA binding

Biological Process: double-strand break repair via homologous recombination; protein stabilization

ATPase WRNIP1

Also known as ATPase WRNIP1 (Werner helicase-interacting protein 1 homolog).
Functions as a modulator for initiation or reinitiation events during DNA polymerase delta-mediated DNA synthesis. Has an intrinsic ATPase activity that functions as a sensor of DNA damage or of arrested replication forks and regulates the extent of DNA synthesis ().

ATPase WRNIP1 homolog C26H5.02c

Functions as a modulator for initiation or reinitiation events during DNA polymerase delta-mediated DNA synthesis. Has an intrinsic ATPase activity that functions as a sensor of DNA damage or of arrested replication forks and regulates the extent of DNA synthesis ().
Proteins Root Name Listing
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