TM175_CHICK
ID TM175_CHICK Reviewed; 501 AA.
AC Q5ZKY0; F1NKK7;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 2.
DT 03-AUG-2022, entry version 75.
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=RCJMB04_8l18 {ECO:0000303|PubMed:15642098};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
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-44 in the first module and Ile-271 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; AJ719954; CAG31613.1; -; mRNA.
DR EMBL; AC189115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001006582.1; NM_001006582.1.
DR AlphaFoldDB; Q5ZKY0; -.
DR SMR; Q5ZKY0; -.
DR STRING; 9031.ENSGALP00000024753; -.
DR PaxDb; Q5ZKY0; -.
DR PRIDE; Q5ZKY0; -.
DR Ensembl; ENSGALT00000024799; ENSGALP00000024753; ENSGALG00000015368.
DR GeneID; 427293; -.
DR KEGG; gga:427293; -.
DR CTD; 84286; -.
DR VEuPathDB; HostDB:geneid_427293; -.
DR eggNOG; ENOG502QR5C; Eukaryota.
DR GeneTree; ENSGT00390000015667; -.
DR InParanoid; Q5ZKY0; -.
DR OMA; FFFPVSY; -.
DR OrthoDB; 894975at2759; -.
DR PhylomeDB; Q5ZKY0; -.
DR TreeFam; TF328838; -.
DR PRO; PR:Q5ZKY0; -.
DR Proteomes; UP000000539; Chromosome Z.
DR Bgee; ENSGALG00000015368; Expressed in brain and 13 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 2: Evidence at transcript level;
KW Endosome; Ion channel; Ion transport; Lysosome; Membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..501
FT /note="Endosomal/lysosomal potassium channel TMEM175"
FT /id="PRO_0000282591"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 32..54
FT /note="Helical; Name=TM1-1"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TOPO_DOM 55..75
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 76..98
FT /note="Helical; Name=TM2-1"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TOPO_DOM 99..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 105..126
FT /note="Helical; Name=TM3-1"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TOPO_DOM 127..136
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 137..158
FT /note="Helical; Name=TM4-1"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TOPO_DOM 159..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 183..203
FT /note="Helical; Name=TM5-1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..208
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 209..228
FT /note="Helical; Name=TM6-1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 258..282
FT /note="Helical; Name=TM1-2"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TOPO_DOM 283..309
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 310..332
FT /note="Helical; Name=TM2-2"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TOPO_DOM 333..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 339..360
FT /note="Helical; Name=TM3-2"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TOPO_DOM 361..375
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 376..396
FT /note="Helical; Name=TM4-2"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TOPO_DOM 397..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 417..440
FT /note="Helical; Name=TM5-2"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TOPO_DOM 441..442
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TRANSMEM 443..469
FT /note="Helical; Name=TM6-2"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT TOPO_DOM 470..501
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..61
FT /note="Short helix H1-1"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT REGION 63..69
FT /note="Short helix H2-1"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT REGION 288..296
FT /note="Short helix H1-2"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT REGION 298..304
FT /note="Short helix H2-2"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT MOTIF 33..39
FT /note="RxxxFSD motif 1"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT MOTIF 260..266
FT /note="RxxxFSD motif 2"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT SITE 44
FT /note="Hydrophobic filter residue 1-1"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT SITE 48
FT /note="Hydrophobic filter residue 2-1"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT SITE 51
FT /note="Hydrophobic filter residue 3-1"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT SITE 271
FT /note="Hydrophobic filter residue 1-2"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA9"
FT SITE 275
FT /note="Hydrophobic filter residue 2-2"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT SITE 278
FT /note="Hydrophobic filter residue 3-2"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT CONFLICT 68
FT /note="V -> I (in Ref. 1; CAG31613)"
SQ SEQUENCE 501 AA; 56098 MW; 8B51D8AC4E157659 CRC64;
MAAPRAATPG PGGGARKPEL DLELGSSTQT SHRLLAYSDA LLSIIATVMI LPVAHTKIHP
DQKLGESVQQ LLLTKIAVYL MTFLIVTVAW AAHVRLFQVI ELIDDVLALL NLACMMIITF
LPYTFSLMAS FPGVPFGIFL FSVCAVVIGL IQAVIVVYGF YHPHLLNQQI QVSENQNFYK
RHILKIILRG PALCFLAAIF SFFFIPLSYL LLGLVIVFPH LSRFITWCKT KIVGHRDEEE
ASYSLETFSF YLSEPLSKER VEAFSDGVYA IVATLLILDI CEDNVPDPRE VGEKFHGSLL
EALSEYGPNY LAYFGSFVTI GLLWFVHHSL FLYVTKATRL MGLLNILSLA FIGGLPLAYQ
LTSEFAEKSH NEIEAIQVSC VITFFASIFQ FAIWTTALLH ERETLHPFAR YGGKEHAFMF
AKLALYPCVS LGAFFLTCLL SEFSTEIFHL MQIVIPFAFL ALRIFVRISL TVIKSVMSLS
RRKVVLLEEE EACLSPTETH S
