TM175_STRC3
ID TM175_STRC3 Reviewed; 206 AA.
AC S5VBU1;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Potassium channel B446_29190 {ECO:0000305};
GN ORFNames=B446_29190 {ECO:0000312|EMBL:AGS72644.1};
OS Streptomyces collinus (strain DSM 40733 / Tue 365).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1214242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40733 / Tue 365 {ECO:0000312|EMBL:AGS72644.1};
RA Ruckert C., Szczepanowski R., Goesmann A., Pross E.K., Musiol E.M.,
RA Blin K., Wohlleben W., Puhler A., Weber T., Kalinowski J.;
RT "The complete genome sequence of Streptomyces collinus Tu 365.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=26317472; DOI=10.1016/j.cell.2015.08.002;
RA Cang C., Aranda K., Seo Y.J., Gasnier B., Ren D.;
RT "TMEM175 is an organelle K(+) channel regulating lysosomal function.";
RL Cell 162:1101-1112(2015).
RN [3]
RP SUBUNIT.
RX PubMed=28723891; DOI=10.1038/nature23269;
RA Lee C., Guo J., Zeng W., Kim S., She J., Cang C., Ren D., Jiang Y.;
RT "The lysosomal potassium channel TMEM175 adopts a novel tetrameric
RT architecture.";
RL Nature 547:472-475(2017).
CC -!- FUNCTION: Potassium channel. {ECO:0000305|PubMed:26317472}.
CC -!- SUBUNIT: Homotetramer (PubMed:28723891). {ECO:0000269|PubMed:28723891}.
CC -!- INTERACTION:
CC S5VBU1; S5VBU1: B446_29190; NbExp=2; IntAct=EBI-20710485, EBI-20710485;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DOMAIN: The six transmembrane regions are tightly packed within each
CC subunit without undergoing domain swapping. Transmembranes TM1-TM3 are
CC positioned on the inner circle of the channel tetramer and participate
CC in inter-subunit interactions that are central to the assembly of the
CC ion conduction pore. The RxxxFSD motif within transmembrane TM1
CC coordinates a network of specific inter- and intra-subunit interactions
CC with other conserved residues on TM2 and TM3 and plays a key role in
CC the tetrameric assembly of the channel. Transmembrane TM4-TM6 are
CC positioned on the periphery of the channel and do not contribute to
CC contacts with neighboring subunits. Transmembranes TM1 and TM2 are
CC linked by an extended strand-like tail and two short helices (H1 and
CC H2) which protrude outwards from the main body of the transmembrane
CC domain and enclose the external open entrance of the ion conduction
CC pore in the channel tetramer. Transmembrane TM1 forms the pore-lining
CC inner helix at the center of the channel, creating an hourglass-shaped
CC ion permeation pathway in the channel tetramer. Three hydrophobic
CC residues on the C-terminal half of the TM1 helix form a bottleneck
CC along the ion conduction pathway and serve as the selectivity filter of
CC the channel. Ile-17 is probably responsible for channel selectivity.
CC {ECO:0000250|UniProtKB:K9UJK2}.
CC -!- SIMILARITY: Belongs to the TMEM175 family. {ECO:0000305}.
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DR EMBL; CP006259; AGS72644.1; -; Genomic_DNA.
DR RefSeq; WP_020943054.1; NC_021985.1.
DR AlphaFoldDB; S5VBU1; -.
DR SMR; S5VBU1; -.
DR TCDB; 1.A.78.2.3; the k+-selective channel in endosomes and lysosomes (kel) family.
DR KEGG; sci:B446_29190; -.
DR PATRIC; fig|1214242.5.peg.5979; -.
DR eggNOG; COG3548; Bacteria.
DR HOGENOM; CLU_090238_0_0_11; -.
DR OMA; PWGWAVM; -.
DR OrthoDB; 1399320at2; -.
DR Proteomes; UP000015423; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0022841; F:potassium ion leak channel activity; TAS:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; TAS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR InterPro; IPR010617; TMEM175.
DR Pfam; PF06736; TMEM175; 1.
PE 1: Evidence at protein level;
KW Ion channel; Ion transport; Membrane; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..206
FT /note="Potassium channel B446_29190"
FT /id="PRO_0000434744"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT TRANSMEM 2..25
FT /note="Helical; Name=TM1"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT TOPO_DOM 26..44
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT TRANSMEM 45..70
FT /note="Helical; Name=TM2"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT TOPO_DOM 71..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT TRANSMEM 77..102
FT /note="Helical; Name=TM3"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT TOPO_DOM 103..110
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT TRANSMEM 111..135
FT /note="Helical; Name=TM4"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT TOPO_DOM 136..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT TRANSMEM 148..174
FT /note="Helical; Name=TM5"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT TOPO_DOM 175..176
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT TRANSMEM 177..192
FT /note="Helical; Name=TM6"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT TOPO_DOM 193..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT REGION 31..34
FT /note="Short helix H1"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT REGION 36..42
FT /note="Short helix H2"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT MOTIF 6..12
FT /note="RxxxFSD motif"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT SITE 17
FT /note="Hydrophobic filter residue 1"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT SITE 21
FT /note="Hydrophobic filter residue 2"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT SITE 24
FT /note="Hydrophobic filter residue 3"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
SQ SEQUENCE 206 AA; 22387 MW; C43BD455A7A082F4 CRC64;
MNESGRVEAF SDGVFAIAIT LLILDIKVPK ADGPGGLWHA LGAQWPSYAA YVVSFLVIGI
MWVNHHQVFS YVARVDRALM FLNLLVLMVV AAVPWPTAML AEYLREDRAS HVAAAVYSLV
MVAMALAFQA LWWHLTRTGH LFDPRVDAPA ARATRIRFAL GSLGYPLTVG LAFVSAPLTL
AAHGLLALYY GFNQVPVPTR EAAAPS
