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3.E.1.6.7
Na+ or H+ pumping bacteriorhodopsin, NaR, Kr2 or KR2.  It uses light to pump protons or sodium ions from the cell depending on the ionic composition of the medium. In cells suspended in a KCl solution, NaR functions as a light-driven proton pump, whereas in a NaCl solution, it exhibits light-driven sodium ion pumping, a novel activity within the rhodopsin family (da Silva et al. 2015).  A cation switch controls its conformations, and specific interactions of Na+ with the half-channels open an appropriate path for ion translocation (da Silva et al. 2015). Several high resolution x-ray structures have been solved (4XTO, Kato et al. 2015). Putative Na+ binding sites have been identified, and it was shown how protonation and conformational changes gate the ion through these sites toward the extracellular side (Suomivuori et al. 2017). Evidence for homology of this and other microbial rhodopsin with GPCR receptors including mamalian rhodopsins has been presented (Yee et al. 2013; Shalaeva et al. 2015).

Accession Number:N0DKS8
Protein Name:Sodium pumping rhodopsin
Length:280
Molecular Weight:31524.00
Species:Dokdonia eikasta [308116]
Number of TMSs:7
Substrate H+, Na+

Cross database links:

Structure:
3X3B   3X3C   4XTL   4XTN   4XTO     

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  • 2° Structure (Network Protein Sequence Analysis)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MTQELGNANF ENFIGATEGF SEIAYQFTSH ILTLGYAVML AGLLYFILTI KNVDKKFQMS 
61:	NILSAVVMVS AFLLLYAQAQ NWTSSFTFNE EVGRYFLDPS GDLFNNGYRY LNWLIDVPML 
121:	LFQILFVVSL TTSKFSSVRN QFWFSGAMMI ITGYIGQFYE VSNLTAFLVW GAISSAFFFH 
181:	ILWVMKKVIN EGKEGISPAG QKILSNIWIL FLISWTLYPG AYLMPYLTGV DGFLYSEDGV 
241:	MARQLVYTIA DVSSKVIYGV LLGNLAITLS KNKELVEANS