Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Endosomal/lysomomal 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

GO - Molecular functioni

  • 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/lysomomal 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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 32CytoplasmicCuratedAdd BLAST32
Transmembranei33 – 53Helical; Name=IS1Sequence analysisAdd BLAST21
Topological domaini54 – 69LumenalCuratedAdd BLAST16
Transmembranei70 – 90Helical; Name=IS2Sequence analysisAdd BLAST21
Topological domaini91 – 107CytoplasmicCuratedAdd BLAST17
Transmembranei108 – 128Helical; Name=IS3Sequence analysisAdd BLAST21
Topological domaini129 – 134LumenalCurated6
Transmembranei135 – 155Helical; Name=IS4Sequence analysisAdd BLAST21
Topological domaini156 – 181CytoplasmicCuratedAdd BLAST26
Transmembranei182 – 202Helical; Name=IS5Sequence analysisAdd BLAST21
Topological domaini203 – 207LumenalCurated5
Transmembranei208 – 227Helical; Name=IS6Sequence analysisAdd BLAST20
Topological domaini228 – 257CytoplasmicCuratedAdd BLAST30
Transmembranei258 – 278Helical; Name=IIS1Sequence analysisAdd BLAST21
Topological domaini279 – 306LumenalCuratedAdd BLAST28
Transmembranei307 – 327Helical; Name=IIS2Sequence analysisAdd BLAST21
Topological domaini328 – 336CytoplasmicCurated9
Transmembranei337 – 357Helical; Name=IIS3Sequence analysisAdd BLAST21
Topological domaini358 – 374LumenalCuratedAdd BLAST17
Transmembranei375 – 395Helical; Name=IIS4Sequence analysisAdd BLAST21
Topological domaini396 – 413CytoplasmicCuratedAdd BLAST18
Transmembranei414 – 434Helical; Name=IIS5Sequence analysisAdd BLAST21
Topological domaini435 – 449LumenalCuratedAdd BLAST15
Transmembranei450 – 470Helical; Name=IIS6Sequence analysisAdd BLAST21
Topological domaini471 – 499CytoplasmicCuratedAdd BLAST29

GO - Cellular componenti

Keywords - Cellular componenti

Endosome, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002825891 – 499Endosomal/lysomomal 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.

Structurei

3D structure databases

ProteinModelPortaliQ9CXY1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi36 – 38FSD motif 1By similarity3
Motifi261 – 263FSD motif 2By similarity3

Domaini

Probably forms a two-repeat structure, with each repeat containing 6 transmembrane regions. The first transmembrane region of each repeat (named IS1 and IIS1, repectively), which contain the invariant FSD motif probably form the ion filter. Negatively charged residues (Asp/Glu) within the helices may interact with potassium ions to achieve the potassium selectivity.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: July 5, 2017
This is version 95 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