ID D2W5E8_NAEGR Unreviewed; 509 AA.
AC D2W5E8;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC35704.1};
GN ORFNames=NAEGRDRAFT_82354 {ECO:0000313|EMBL:EFC35704.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC35704.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC35704.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; GG739061; EFC35704.1; -; Genomic_DNA.
DR RefSeq; XP_002668448.1; XM_002668402.1.
DR AlphaFoldDB; D2W5E8; -.
DR EnsemblProtists; EFC35704; EFC35704; NAEGRDRAFT_82354.
DR GeneID; 8861830; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_82354; -.
DR eggNOG; KOG0476; Eukaryota.
DR InParanoid; D2W5E8; -.
DR OrthoDB; 1194at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 1.10.3080.10; Clc chloride channel; 2.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; Cl-channel_volt-gated.
DR PANTHER; PTHR45720; CHLORIDE CHANNEL PROTEIN 2; 1.
DR PANTHER; PTHR45720:SF10; CHLORIDE CHANNEL PROTEIN 2; 1.
DR Pfam; PF00654; Voltage_CLC; 2.
DR PRINTS; PR00762; CLCHANNEL.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF81340; Clc chloride channel; 2.
PE 4: Predicted;
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 99..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 509 AA; 56047 MW; C52C92836E661FA0 CRC64;
MITDVVSPTV TIHNNDNNND DTKDDSNKQS TKPNVVSDST ITPNETSKKT GLTASSTVTT
LDDMETKVIL TNLKNASNVN YVETQNWKKG LKGIRRKKYT WTFLTVCGFV GGVIIYTHDL
IVKYMFQGRL TLINAFDSNS YFGLRLVLWI LFNLVFMYVS LMMTIFIAPA SEGSGIPAIK
AILNGTPLED PLSFKTFLVK IITLPAVLGT GMFFGKVIIG AGCGRFFGEI VAIIFPNGFV
AGQPIYAGAY AVVGIVALTA SATHAFSTVF IFLEIVGVAV YLPSLMAALI AVRISRLCTA
NFYDTSIKVK GWPALLESMT DSEDLKVTNI MTSVDKLDIL EENVSMRDLE LLLQKKKLPK
ILPVVSSKDN LVLLGQVHLK SLEFQYNLMK ARLNNSGKEI TQASNFAPIS DEGYGSANDG
NDSSATNMAG YASFELQDRD ETDIIRIEYE TCDITISESQ SAQRAHMLFS QLCLDEAFVV
WKGRLMGQLA RQMLINTVSA RERNQIIVV
//
