1.A.114.1.1 Plasma membrane proton-activated chloride channel, PACC1, or acid-sensitive outwardly-rectifying anion channel PAORAC/ASOR or TMEM206, of 350 aas and 2 TMSs. Ion permeation-changing mutations along the length of TMS2 and at the end
of TMS1 suggest that these segments line the pore. TMEM206 probably has orthologs in all
vertebrates (Ullrich et al. 2019). Knockout of mouse Pac abolished I Cl,H in neurons and attenuated brain damage after ischemic stroke (Yang et al. 2019). The cryoEM structure (3.1 Å resolution) in active and desensitized states has been determined (Wang et al. 2022). The acid-sensitive site critical for chloral hydrate activation of the proton-activated chloride channel has been identified (Xu et al. 2022). The molecular mechanism underlying desensitization of the proton-activated chloride channel, PAC, has been examined (Osei-Owusu et al. 2022).
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Accession Number: | Q9H813 |
Protein Name: | Proton-activated chloride channel |
Length: | 350 |
Molecular Weight: | 40043.00 |
Species: | Homo sapiens (Human) [9606] |
Number of TMSs: | 2 |
Location1 / Topology2 / Orientation3: |
Cell membrane1 / Multi-pass membrane protein2 |
Substrate |
anion, chloride |
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1: MIRQERSTSY QELSEELVQV VENSELADEQ DKETVRVQGP GILPGLDSES ASSSIRFSKA
61: CLKNVFSVLL IFIYLLLMAV AVFLVYRTIT DFREKLKHPV MSVSYKEVDR YDAPGIALYP
121: GQAQLLSCKH HYEVIPPLTS PGQPGDMNCT TQRINYTDPF SNQTVKSALI VQGPREVKKR
181: ELVFLQFRLN KSSEDFSAID YLLFSSFQEF LQSPNRVGFM QACESAYSSW KFSGGFRTWV
241: KMSLVKTKEE DGREAVEFRQ ETSVVNYIDQ RPAAKKSAQL FFVVFEWKDP FIQKVQDIVT
301: ANPWNTIALL CGAFLALFKA AEFAKLSIKW MIKIRKRYLK RRGQATSHIS