ID A2C604_PROM3 Unreviewed; 135 AA. AC A2C604; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 29-MAY-2024, entry version 79. DE RecName: Full=Fluoride-specific ion channel FluC {ECO:0000256|HAMAP-Rule:MF_00454}; GN Name=fluC {ECO:0000256|HAMAP-Rule:MF_00454}; GN Synonyms=crcB {ECO:0000256|HAMAP-Rule:MF_00454}; GN OrderedLocusNames=P9303_01591 {ECO:0000313|EMBL:ABM76914.1}; OS Prochlorococcus marinus (strain MIT 9303). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Prochlorococcaceae; Prochlorococcus. OX NCBI_TaxID=59922 {ECO:0000313|EMBL:ABM76914.1, ECO:0000313|Proteomes:UP000002274}; RN [1] {ECO:0000313|EMBL:ABM76914.1, ECO:0000313|Proteomes:UP000002274} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9303 {ECO:0000313|EMBL:ABM76914.1, RC ECO:0000313|Proteomes:UP000002274}; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., RA Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(2007). CC -!- FUNCTION: Fluoride-specific ion channel. Important for reducing CC fluoride concentration in the cell, thus reducing its toxicity. CC {ECO:0000256|HAMAP-Rule:MF_00454}. CC -!- CATALYTIC ACTIVITY: CC Reaction=fluoride(in) = fluoride(out); Xref=Rhea:RHEA:76159, CC ChEBI:CHEBI:17051; Evidence={ECO:0000256|ARBA:ARBA00035585}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76160; CC Evidence={ECO:0000256|ARBA:ARBA00035585}; CC -!- ACTIVITY REGULATION: Na(+) is not transported, but it plays an CC essential structural role and its presence is essential for fluoride CC channel function. {ECO:0000256|HAMAP-Rule:MF_00454}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00454}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00454}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass CC membrane protein {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the fluoride channel Fluc/FEX (TC 1.A.43) CC family. {ECO:0000256|ARBA:ARBA00035120, ECO:0000256|HAMAP- CC Rule:MF_00454}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000554; ABM76914.1; -; Genomic_DNA. DR AlphaFoldDB; A2C604; -. DR STRING; 59922.P9303_01591; -. DR KEGG; pmf:P9303_01591; -. DR HOGENOM; CLU_114342_2_3_3; -. DR Proteomes; UP000002274; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0062054; F:fluoride channel activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0140114; P:cellular detoxification of fluoride; IEA:UniProtKB-UniRule. DR HAMAP; MF_00454; FluC; 1. DR InterPro; IPR003691; FluC. DR PANTHER; PTHR28259; FLUORIDE EXPORT PROTEIN 1-RELATED; 1. DR PANTHER; PTHR28259:SF1; FLUORIDE EXPORT PROTEIN 1-RELATED; 1. DR Pfam; PF02537; CRCB; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00454}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_00454}; KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|HAMAP- KW Rule:MF_00454}; Ion transport {ECO:0000256|HAMAP-Rule:MF_00454}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00454}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00454}; KW Sodium {ECO:0000256|HAMAP-Rule:MF_00454}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_00454}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_00454}; Transport {ECO:0000256|HAMAP-Rule:MF_00454}. FT TRANSMEM 12..33 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT TRANSMEM 45..65 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT TRANSMEM 77..100 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT TRANSMEM 112..133 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT BINDING 87 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_note="structural" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT BINDING 90 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_note="structural" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" SQ SEQUENCE 135 AA; 13803 MW; 3E9CE0E61D1D9A5C CRC64; MAGSMSDLAL PAWQASLVAI GAVPGAWLRL RVVNHLEPMV PRKHWGTFAV NMVAAFALGL VLALQAKCAP ASGASPLILL IGVGFFGSLS TFSTFAGEVL NTLREHRWSE ALVLAVGSIL GGLLAVAAGV GLADG //