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1.A.46.2.8
Functionally characterized bestrophin homologue, KpBEST, YneE or RFP-TM of 305 aas and 3 or 4 TMSs per subunit.  KpBest is a pentamer that forms a five-helix transmembrane pore, closed by three rings of conserved hydrophobic residues, and has a cytoplasmic cavern with a restricted exit (Yang et al. 2014). From electrophysiological analysis of structure-inspired mutations in KpBest and hBest1, a sensitive control of ion selectivity was observed in the bestrophins, including reversal of anion/cation selectivity, and dramatic activation by mutations at the cytoplasmic exit.  The wild type protein seems to be a cation (Na+) channel but the I66F mutation changed it into an anion (Cl-) channel (Yang et al. 2014).  There are two  constrictions in the channel, one provides the ion selectivity and the other serves as the gate.

Accession Number:W9BH30
Protein Name:Bestrophin, RFP-TM, chloride channel family protein
Length:305
Molecular Weight:34903.00
Species:Klebsiella pneumoniae [573]
Number of TMSs:3
Substrate Na+

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FASTA formatted sequence
1:	MIIRPEQHWF LRLFDWHGSV LSKIIFRLLL NVLMSIIAII SYQWYEQLGI HLTVAPFSLL 
61:	GIAIAIFLGF RNSASYSRFV EARNLWGTVL IAERTLVRQL RNILPAEHDA HRRIVSYLVA 
121:	FSWSLKHQLR KTDPTADLRR LLPEERVTEI LASSMPTNRI LLLAGNEIGQ LREAGKLSDI 
181:	TYGLMDNKLD ELAHVLGGCE RLATTPVPFA YTLILQRTVY LFCTLLPFAL VGDLHYMTPF 
241:	VSVFISYTFL SWDSLAEELE DPFGTAANDL PLNAMCNTIE RNLLDMTGQH PLPETLRPDR 
301:	YFNLT