TM175_DANRE
ID TM175_DANRE Reviewed; 520 AA.
AC A5PN43;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Endosomal/lysosomal potassium channel TMEM175 {ECO:0000305};
DE AltName: Full=Transmembrane protein 175 {ECO:0000250|UniProtKB:Q9BSA9};
GN Name=tmem175 {ECO:0000250|UniProtKB:Q9BSA9};
GN ORFNames=si:ch211-168m18.2 {ECO:0000303|PubMed:23594743};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Organelle-specific potassium channel specifically responsible
CC for potassium conductance in endosomes and lysosomes. Forms a
CC potassium-permeable leak-like channel. {ECO:0000250|UniProtKB:Q9BSA9}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9BSA9}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q9BSA9};
CC Multi-pass membrane protein {ECO:0000255}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q9BSA9}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: Composed of two modules of six transmembranes, forming a
CC homodimer with a tetrameric architecture. The six transmembrane regions
CC of each module are tightly packed within each subunit without
CC undergoing domain swapping. Forms a central ion-conduction pore lined
CC by the side chains of the pore-lining helices. Conserved isoleucine
CC residues (Ile-62 in the first module and Ile-288 in the second module)
CC in the center of the pore serve as the gate in the closed conformation.
CC In the widened channel in the open conformation, the same residues
CC establish a constriction essential for potassium selectivity.
CC {ECO:0000250|UniProtKB:Q9BSA9}.
CC -!- SIMILARITY: Belongs to the TMEM175 family. {ECO:0000305}.
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DR EMBL; BX927346; CAN87989.1; -; Genomic_DNA.
DR RefSeq; NP_001093545.1; NM_001100075.1.
DR AlphaFoldDB; A5PN43; -.
DR SMR; A5PN43; -.
DR STRING; 7955.ENSDARP00000102863; -.
DR PaxDb; A5PN43; -.
DR Ensembl; ENSDART00000112728; ENSDARP00000102863; ENSDARG00000076376.
DR GeneID; 100002086; -.
DR KEGG; dre:100002086; -.
DR CTD; 84286; -.
DR ZFIN; ZDB-GENE-070705-79; tmem175.
DR eggNOG; ENOG502QR5C; Eukaryota.
DR GeneTree; ENSGT00390000015667; -.
DR HOGENOM; CLU_052593_0_0_1; -.
DR InParanoid; A5PN43; -.
DR OMA; FFFPVSY; -.
DR OrthoDB; 894975at2759; -.
DR PhylomeDB; A5PN43; -.
DR TreeFam; TF328838; -.
DR PRO; PR:A5PN43; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000076376; Expressed in brain and 20 other tissues.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0031303; C:integral component of endosome membrane; ISS:UniProtKB.
DR GO; GO:1905103; C:integral component of lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005267; F:potassium channel activity; ISS:UniProtKB.
DR GO; GO:0022841; F:potassium ion leak channel activity; ISS:UniProtKB.
DR GO; GO:0070050; P:neuron cellular homeostasis; ISS:UniProtKB.
DR GO; GO:0090385; P:phagosome-lysosome fusion; ISS:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0035751; P:regulation of lysosomal lumen pH; ISS:UniProtKB.
DR InterPro; IPR010617; TMEM175.
DR Pfam; PF06736; TMEM175; 2.
PE 3: Inferred from homology;
KW Endosome; Ion channel; Ion transport; Lysosome; Membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..520
FT /note="Endosomal/lysosomal potassium channel TMEM175"
FT /id="PRO_0000360412"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 50..72
FT /note="Helical; Name=TM1-1"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TOPO_DOM 73..93
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 94..116
FT /note="Helical; Name=TM2-1"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TOPO_DOM 117..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 123..144
FT /note="Helical; Name=TM3-1"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TOPO_DOM 145..154
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 155..176
FT /note="Helical; Name=TM4-1"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TOPO_DOM 177..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 201..221
FT /note="Helical; Name=TM5-1"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical; Name=TM6-1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 275..299
FT /note="Helical; Name=TM1-2"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TOPO_DOM 300..326
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 327..349
FT /note="Helical; Name=TM2-2"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TOPO_DOM 350..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 356..377
FT /note="Helical; Name=TM3-2"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TOPO_DOM 378..392
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 393..413
FT /note="Helical; Name=TM4-2"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TOPO_DOM 414..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 434..457
FT /note="Helical; Name=TM5-2"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TOPO_DOM 458..459
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 460..486
FT /note="Helical; Name=TM6-2"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TOPO_DOM 487..520
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..79
FT /note="Short helix H1-1"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT REGION 81..87
FT /note="Short helix H2-1"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT REGION 305..313
FT /note="Short helix H1-2"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT REGION 315..321
FT /note="Short helix H2-2"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT MOTIF 51..57
FT /note="RxxxFSD motif 1"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT MOTIF 277..283
FT /note="RxxxFSD motif 2"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT SITE 62
FT /note="Hydrophobic filter residue 1-1"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT SITE 66
FT /note="Hydrophobic filter residue 2-1"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT SITE 69
FT /note="Hydrophobic filter residue 3-1"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT SITE 288
FT /note="Hydrophobic filter residue 1-2"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT SITE 292
FT /note="Hydrophobic filter residue 2-2"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT SITE 295
FT /note="Hydrophobic filter residue 3-2"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
SQ SEQUENCE 520 AA; 59013 MW; DD3991FE65DAE7B9 CRC64;
MGENDESEII EHHDDEEMEK RRPPRTHAQS FLESVASSVK EGHSSTQSSH RLLAYSDALI
SIIATVMILP VAHTKIQEDE ELKQSIQALL TTKIAVYLMT FLIVTVAWAA HIRLFQVIER
IDDTLALLNL ACMMLITFLP YTFSLMATFP NNILGILLFC ACVMVIGLIQ ALIVLYGFSH
PFLLNDQIQM SENQAYYKQH ILKVIMRVPI MCLFASIFSF IFFQLSYVLL AIVIFLPYIS
QCLKWIRSKA IGGQTDESPD SMPFYTYHPS EPLSKERVEA FSDGVFAIVA TLLILDICEG
NVPDPSVVKK KFDNSLIAAL QEYGPEYLAY FGSFVTVGLL WFVHHSLFLH VTKATRLMGL
FNTFSLAFVG GLPLAYQLTH ESPRGSRNEL EAVQISCVII FFASLFQLAI WVTALFTERE
TLHPYVRYGG REHTFMLAKL SLYPCVALGT FFITCILSRF SAPIFHMMEI CIPFAFLLLR
LLVRVALALL RWLFCSARND LERIPVEEEE SRLPINDIVT
