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Database: UniProt
Entry: A0A0K0DXH0_STRER
LinkDB: A0A0K0DXH0_STRER
Original site: A0A0K0DXH0_STRER 
ID   A0A0K0DXH0_STRER        Unreviewed;      1117 AA.
AC   A0A0K0DXH0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Potassium channel subfamily K member 18 {ECO:0000313|WBParaSite:SSTP_0000193500.1};
OS   Strongyloides stercoralis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000193500.1};
RN   [1] {ECO:0000313|WBParaSite:SSTP_0000193500.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC       1.A.1.8) family. {ECO:0000256|ARBA:ARBA00006666,
CC       ECO:0000256|RuleBase:RU003857}.
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DR   AlphaFoldDB; A0A0K0DXH0; -.
DR   STRING; 6248.A0A0K0DXH0; -.
DR   WBParaSite; SSTP_0000193500.1; SSTP_0000193500.1; SSTP_0000193500.
DR   Proteomes; UP000035681; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005267; F:potassium channel activity; IEA:InterPro.
DR   Gene3D; 1.10.287.70; -; 1.
DR   InterPro; IPR003280; 2pore_dom_K_chnl.
DR   InterPro; IPR013099; K_chnl_dom.
DR   PANTHER; PTHR11003; POTASSIUM CHANNEL, SUBFAMILY K; 1.
DR   PANTHER; PTHR11003:SF86; TWIK FAMILY OF POTASSIUM CHANNELS; 1.
DR   Pfam; PF07885; Ion_trans_2; 2.
DR   PRINTS; PR01333; 2POREKCHANEL.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 2.
PE   3: Inferred from homology;
KW   Ion channel {ECO:0000256|RuleBase:RU003857};
KW   Ion transport {ECO:0000256|RuleBase:RU003857};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003857};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003857}.
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        260..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        293..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        382..403
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        436..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          255..315
FT                   /note="Potassium channel"
FT                   /evidence="ECO:0000259|Pfam:PF07885"
FT   DOMAIN          388..462
FT                   /note="Potassium channel"
FT                   /evidence="ECO:0000259|Pfam:PF07885"
FT   REGION          1044..1073
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1117 AA;  128111 MW;  7C04FECFF2614916 CRC64;
     MDIFTKIRHF DISSYKKVKT IQEEENGFFK GHYVEKNYQK KENNKLQCIP IILPIIGQSL
     ENIEGTKTIN QDDGRVSRYD NVSRPFSRLS LSTGDISLRS KDTGTILEEG NNKKGFWSDF
     LYGSRRSIFN SLMNVSRKDI SNNEDCSRKK SKYYSPIYLK IKIFYDRFNL RHFAPFLILL
     IYAFLGAGLF YYIEHTNEIE MKQLEENQLN ILRNKTLDRL KNIMLDDVIT LKSKLITAKD
     IFNHYEKELL RLKGEQRLDW DFIGALYYVG SIMTTIGYGN IYCRTNIGRG FTIIYSVISI
     PLVLAILSHC GRTLTTFFSN KWIRYRNRLK KKKQNLLKNK KIDKNNSGVG IKNGDTFITI
     NDEDNDKSII ENHIRESRTI PIWLALFLCI GWICFCAGLF CIWEKKWSYY TSLYFFFISL
     STIGLGDVVP DHPHMLVLLF CLVIIGLSIV SMLLSVIQIK IEEWFYDLMM KMQEEYRKAM
     ENGDTEKANE IREHLLDGEP WYMKQMASHL LSDNQNTKLD EVAEKYEMVM KSTNTRYVQT
     DNTIKSKNIG TGSGIIELQS NDTISIIEDI PEIIDDYEKQ QNCKIESDYS SVDEFEEDNS
     SIADALSLPY DGTEEVSVNI NSLTEEEKLI NSLIKKIELC DNNVETLLKN EESNIMEIDD
     NKNINNNECQ KMVNRSVENL YSEINPRKKY NELGTMTLLN LAEDETQTSE KCYYDKECST
     IGLIEVCDAN NGTSKINSRT ISLNTDFINV STSIDENFDC CEDRSQQTSI REDNKISEMT
     KKYELEISEM KGRLAEMEKL YSSTLSIQSP AHSDTSVQCH SLSGSPGPSL IHIAISTTPP
     PESVDVGMMT TLTSNHIKKM ENVNKNKKKN NNIKKENDKI DEIKKPIKHD LIIQTDDSYL
     KIARRLNEYK TQKSTNLSVV AAKPLNANEI NSLNYNGNIP PSERREYSKE PNSIRKKFGT
     IKRKLQRSKG VRSPDNEIQA MSVSYCGVNE EAKYNLIPDR MFCSDDGSGM DFDNKNDDIT
     VGDGNIRHNA SNITLCGSLN VSSNEEKNFS SSESKGSISR KASISSIDRQ KSLPPNIQRG
     KVLEYITQHE KGVHDPGTEK GRRKSLITII DMRDQNC
//
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