Voltage-gated proton channel C

Unless otherwise stated all data on this page refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).

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The voltage-gated proton channel (provisionally denoted Hv1) is a putative 4TM proton-selective channel gated by membrane depolarization and which is sensitive to the transmembrane pH gradient [1-3,12,14]. The structure of Hv1 is homologous to the voltage sensing domain (VSD) of the superfamily of voltage-gated ion channels (i.e. segments S1 to S4) and contains no discernable pore region [12,14]. Proton flux through Hv1 is instead most likely mediated by a water wire completed in a crevice of the protein when the voltage-sensing S4 helix moves in response to a change in transmembrane potential [11,17]. Hv1 expresses largely as a dimer mediated by intracellular C-terminal coiled-coil interactions [7] but individual promoters nonetheless support gated H+ flux via separate conduction pathways [5-6,10,15]. Within dimeric structures, the two protomers do not function independently, but display co-operative interactions during gating resulting in increased voltage sensitivity, but slower activation, of the dimeric, versus monomeric, complexes [4,16] .

Channels and Subunits

Hv1 C Show summary »


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Further reading

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How to cite this family page

Database page citation:

Voltage-gated proton channel. Accessed on 30/05/2017. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=124.

Concise Guide to PHARMACOLOGY citation:

Alexander SPH, Catterall WA, Kelly E, Marrion N, Peters JA, Benson HE, Faccenda E, Pawson AJ, Sharman JL, Southan C, Davies JA and CGTP Collaborators (2015) The Concise Guide to PHARMACOLOGY 2015/16: Voltage-gated ion channels. Br J Pharmacol. 172: 5904-5941.