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Protein

Endosomal/lysosomal potassium channel TMEM175

Gene

Tmem175

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Organelle-specific potassium channel specifically responsible for potassium conductance in endosomes and lysosomes. Forms a potassium-permeable leak-like channel, which regulates lumenal pH stability and is required for autophagosome-lysosome fusion. Constitutes the major lysosomal potassium channel.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei43Hydrophobic filter residue 1-1By similarity1
Sitei47Hydrophobic filter residue 2-1By similarity1
Sitei50Hydrophobic filter residue 3-1By similarity1
Sitei268Hydrophobic filter residue 1-2By similarity1
Sitei272Hydrophobic filter residue 2-2By similarity1
Sitei275Hydrophobic filter residue 3-2By similarity1

GO - Molecular functioni

  • potassium channel activity Source: UniProtKB
  • potassium ion leak channel activity Source: UniProtKB

GO - Biological processi

  • phagosome-lysosome fusion Source: UniProtKB
  • potassium ion transmembrane transport Source: UniProtKB
  • regulation of lysosomal lumen pH Source: UniProtKB

Keywordsi

Molecular functionIon channel, Potassium channel
Biological processIon transport, Potassium transport, Transport
LigandPotassium

Names & Taxonomyi

Protein namesi
Recommended name:
Endosomal/lysosomal potassium channel TMEM175By similarity
Alternative name(s):
Transmembrane protein 175
Short name:
mTMEM1751 Publication
Gene namesi
Name:Tmem175Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1919642. Tmem175.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 32CytoplasmicCuratedAdd BLAST32
Transmembranei33 – 53Helical; Name=TM1-1Sequence analysisAdd BLAST21
Topological domaini54 – 69LumenalCuratedAdd BLAST16
Transmembranei70 – 90Helical; Name=TM2-1Sequence analysisAdd BLAST21
Topological domaini91 – 107CytoplasmicCuratedAdd BLAST17
Transmembranei108 – 128Helical; Name=TM3-1Sequence analysisAdd BLAST21
Topological domaini129 – 134LumenalCurated6
Transmembranei135 – 155Helical; Name=TM4-1Sequence analysisAdd BLAST21
Topological domaini156 – 181CytoplasmicCuratedAdd BLAST26
Transmembranei182 – 202Helical; Name=TM5-1Sequence analysisAdd BLAST21
Topological domaini203 – 207LumenalCurated5
Transmembranei208 – 227Helical; Name=TM6-1Sequence analysisAdd BLAST20
Topological domaini228 – 257CytoplasmicCuratedAdd BLAST30
Transmembranei258 – 278Helical; Name=TM1-2Sequence analysisAdd BLAST21
Topological domaini279 – 306LumenalCuratedAdd BLAST28
Transmembranei307 – 327Helical; Name=TM2-2Sequence analysisAdd BLAST21
Topological domaini328 – 336CytoplasmicCurated9
Transmembranei337 – 357Helical; Name=TM3-2Sequence analysisAdd BLAST21
Topological domaini358 – 374LumenalCuratedAdd BLAST17
Transmembranei375 – 395Helical; Name=TM4-2Sequence analysisAdd BLAST21
Topological domaini396 – 413CytoplasmicCuratedAdd BLAST18
Transmembranei414 – 434Helical; Name=TM5-2Sequence analysisAdd BLAST21
Topological domaini435 – 449LumenalCuratedAdd BLAST15
Transmembranei450 – 470Helical; Name=TM6-2Sequence analysisAdd BLAST21
Topological domaini471 – 499CytoplasmicCuratedAdd BLAST29

Keywords - Cellular componenti

Endosome, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002825891 – 499Endosomal/lysosomal potassium channel TMEM175Add BLAST499

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei6PhosphothreonineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9CXY1.
MaxQBiQ9CXY1.
PaxDbiQ9CXY1.
PRIDEiQ9CXY1.

PTM databases

iPTMnetiQ9CXY1.
PhosphoSitePlusiQ9CXY1.

Expressioni

Gene expression databases

BgeeiENSMUSG00000013495.
CleanExiMM_TMEM175.
ExpressionAtlasiQ9CXY1. baseline and differential.
GenevisibleiQ9CXY1. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9CXY1.
SMRiQ9CXY1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni55 – 60Short helix H1-1By similarity6
Regioni62 – 68Short helix H2-1By similarity7
Regioni285 – 293Short helix H1-2By similarity9
Regioni295 – 301Short helix H2-2By similarity7

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi32 – 38RxxxFSD motif 1By similarity7
Motifi257 – 263RxxxFSD motif 2By similarity7

Domaini

Composed of two modules of six transmembranes, forming a homodimer with a tetrameric architecture (By similarity). The six transmembrane regions of each module are tightly packed within each subunit without undergoing domain swapping (By similarity). Transmembranes TM1-TM3 of each module are positioned on the inner circle of the channel tetramer and participate in inter-subunit interactions that are central to the assembly of the ion conduction pore (By similarity). The RxxxFSD motifs within transmembranes TM1 coordinate a network of specific inter- and intra-subunit interactions with other conserved residues on TM2 and TM3 and play a key role in the tetrameric assembly of the channel (By similarity). Transmembranes TM4-TM6 are positioned on the periphery of the channel and do not contribute contacts with neighboring subunits (By similarity). Transmembranes TM1 and TM2 are linked by an extended strand-like tail and two short helices (H1 and H2) which protrude outwards from the main body of the transmembrane domain and enclose the external open entrance of the ion conduction pore in the channel tetramer (By similarity). Transmembranes TM1 form the pore-lining inner helix at the center of the channel, creating an hourglass-shaped ion permeation pathway in the channel tetramer (By similarity). Three hydrophobic residues on the C-terminal half of the TM1 helices form a bottleneck along the ion conduction pathway and serve as the selectivity filter of the channel (By similarity). Ile-43 (and Ile-268) are probably responsible for channel selectivity (By similarity).By similarity

Sequence similaritiesi

Belongs to the TMEM175 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IIWE. Eukaryota.
ENOG410ZP3B. LUCA.
GeneTreeiENSGT00390000015667.
HOGENOMiHOG000154616.
HOVERGENiHBG059914.
InParanoidiQ9CXY1.
OMAiACMMLIT.
OrthoDBiEOG091G05QO.
PhylomeDBiQ9CXY1.
TreeFamiTF328838.

Family and domain databases

InterProiView protein in InterPro
IPR010617. TMEM175.
PfamiView protein in Pfam
PF06736. DUF1211. 2 hits.

Sequencei

Sequence statusi: Complete.

Q9CXY1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRLQTEEQA VDSEGDSSLH RRNEEGTQSS HRMLGFSDAL LSIIATVMIL
60 70 80 90 100
PVTHTEISPE QQFDKSIQKL LATRIAVYLM TFLIVTVAWT AHTRLFQVVG
110 120 130 140 150
KIDDTLALLN LACMMTITLL PYTFSLMVTF PDVPLGIFLF CVCVIAIGSV
160 170 180 190 200
QAMIVGYAFH FPHLLNPQIQ CSTHRDLSRR HILHLVLRGP ALCFVAAVFS
210 220 230 240 250
LFFFPLSYLL MVTVIFLPHI SKATTWCKDK LMGQRESPAH DMEPFSIDLH
260 270 280 290 300
APLSKERVEA FSDGVYAIVA TLLILDICED NVPDPKDVQE KFSGSLVAAL
310 320 330 340 350
GAYGPQFLAY FGSFATVGLL WFAHHSLFLH VRKATQTMGL LNILSLAFVG
360 370 380 390 400
GLPLAYQQTS AFARQPHDEL ERVRVSCAII FFASIFQFAI WTTALLHQTE
410 420 430 440 450
TLQPAVQFGG QEHAFMFAKL ALYPCASLLA FAATCLLSRF STAIFHLMQI
460 470 480 490
SVPFAFLLLR LLVRLALAGL QVLRGLWPHH PQQDQSEPEA QSQLLPDPC
Length:499
Mass (Da):55,578
Last modified:April 3, 2007 - v2
Checksum:iBDED3561EF10EB92
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti174H → R in AAH05542 (PubMed:15489334).Curated1
Sequence conflicti197A → S in BAE41678 (PubMed:16141072).Curated1
Sequence conflicti324H → R in BAE41678 (PubMed:16141072).Curated1
Sequence conflicti475G → R in BAB29031 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013879 mRNA. Translation: BAB29031.1.
AK170273 mRNA. Translation: BAE41678.1.
BC005542 mRNA. Translation: AAH05542.1.
CCDSiCCDS19514.1.
RefSeqiNP_001157004.1. NM_001163532.1.
NP_082499.3. NM_028223.3.
XP_006535292.1. XM_006535229.2.
XP_006535293.1. XM_006535230.3.
UniGeneiMm.258324.

Genome annotation databases

EnsembliENSMUST00000063272; ENSMUSP00000068607; ENSMUSG00000013495.
ENSMUST00000078323; ENSMUSP00000077437; ENSMUSG00000013495.
ENSMUST00000120327; ENSMUSP00000112780; ENSMUSG00000013495.
GeneIDi72392.
KEGGimmu:72392.
UCSCiuc008yoq.2. mouse.

Similar proteinsi

Entry informationi

Entry nameiTM175_MOUSE
AccessioniPrimary (citable) accession number: Q9CXY1
Secondary accession number(s): Q3TDC4, Q99K00
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: October 25, 2017
This is version 96 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families