ID   TM175_CHRP1             Reviewed;         192 AA.
AC   A0A086F3E3;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   29-OCT-2014, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Potassium channel HX13_20290 {ECO:0000305};
GN   ORFNames=HX13_20290 {ECO:0000312|EMBL:KFF73457.1};
OS   Chryseobacterium sp. (strain P1-3).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1517683;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1-3 {ECO:0000312|EMBL:KFF73457.1};
RA   Park G.-S., Hong S.-J., Kwak Y., Choi J.-B., Jung B.K., Lee C.H.,
RA   Shin J.-H.;
RT   "Chryseobacterium sp. P1-3 whole genome sequence.";
RL   Submitted (JUL-2014) 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       A0A086F3E3; A0A086F3E3: HX13_20290; NbExp=2; IntAct=EBI-20710502, EBI-20710502;
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-16 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; JPEQ01000015; KFF73457.1; -; Genomic_DNA.
DR   RefSeq; WP_050022392.1; NZ_JPEQ01000015.1.
DR   AlphaFoldDB; A0A086F3E3; -.
DR   SMR; A0A086F3E3; -.
DR   EnsemblBacteria; KFF73457; KFF73457; HX13_20290.
DR   OMA; TGWMGEN; -.
DR   Proteomes; UP000028723; Unassembled WGS sequence.
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   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..192
FT                   /note="Potassium channel HX13_20290"
FT                   /id="PRO_0000434743"
FT   TRANSMEM        1..24
FT                   /note="Helical; Name=TM1"
FT                   /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT   TOPO_DOM        25
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT   TOPO_DOM        26..39
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT   TRANSMEM        40..65
FT                   /note="Helical; Name=TM2"
FT                   /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT   TOPO_DOM        66..71
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT   TRANSMEM        72..93
FT                   /note="Helical; Name=TM3"
FT                   /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT   TOPO_DOM        94..101
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT   TRANSMEM        102..126
FT                   /note="Helical; Name=TM4"
FT                   /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT   TOPO_DOM        127..133
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT   TRANSMEM        134..162
FT                   /note="Helical; Name=TM5"
FT                   /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT   TOPO_DOM        163..164
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT   TRANSMEM        165..180
FT                   /note="Helical; Name=TM6"
FT                   /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT   TOPO_DOM        181..192
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT   REGION          26..29
FT                   /note="Short helix H1"
FT                   /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT   REGION          31..37
FT                   /note="Short helix H2"
FT                   /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT   MOTIF           5..11
FT                   /note="RxxxFSD motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT   SITE            16
FT                   /note="Hydrophobic filter residue 1"
FT                   /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT   SITE            20
FT                   /note="Hydrophobic filter residue 2"
FT                   /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT   SITE            23
FT                   /note="Hydrophobic filter residue 3"
FT                   /evidence="ECO:0000250|UniProtKB:K9UJK2"
SQ   SEQUENCE   192 AA;  21996 MW;  5400703856099E2C CRC64;
     MTKGRLEAFS DGVLAIIITI MVLELKVPEG SSWASLQPIL PRFLAYIFSF IYVGIYWNNH
     HHLFQTVKKV NGSILWANLH LLFWLSLMPI ATEWIGTSHF AQNPVATYGI GLIMSAIAYT
     ILENVIIRCE GENSKLKEAI HSKFKEYISI IFYVLGIATS FFYPYIAIGF YYLVALIWLI
     PDKRIEKSLK EN