ID A0A0K0D4V9_ANGCA Unreviewed; 467 AA.
AC A0A0K0D4V9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Ion channel {ECO:0000313|WBParaSite:ACAC_0000510401-mRNA-1};
OS Angiostrongylus cantonensis (Rat lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000510401-mRNA-1};
RN [1] {ECO:0000313|Proteomes:UP000035642}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:ACAC_0000510401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) 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; A0A0K0D4V9; -.
DR STRING; 6313.A0A0K0D4V9; -.
DR WBParaSite; ACAC_0000510401-mRNA-1; ACAC_0000510401-mRNA-1; ACAC_0000510401.
DR Proteomes; UP000035642; 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:SF343; TWIK FAMILY OF POTASSIUM CHANNELS PROTEIN 18; 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:UP000035642};
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 12..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 107..162
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT DOMAIN 223..295
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
SQ SEQUENCE 467 AA; 52755 MW; 72176AE64A02D2D6 CRC64;
MAHLGIIQLQ FIYYYCFIVL LALLPLLGLL LYTLLGAVLF CELEGPNEQY ELAQLKKQRE
ELFESTVYRL NNVRAMQPMA ALNHTRKNLL RFQQKLGIEP VNLEDIRWNF WGAVFYCMTV
YTTIGYGNIV PTTTAGRVLT ILYAFIGIPF AVLTLFALGT IFAKLCKTLW KMLIKSTTVV
SKDLERKVTK AVGFDEEAQL LQSSTTLSDE DLLSFPISFL VLLTILWVFF CAFVFTLLED
WSYGTSLYFT LISFTTIGFG DVLPSEYDYI VVVGFLLLIG LSLVSTVLTL LQQQIEALAT
GVQSDVDREY KKALVEAANE GEISPDLKKT MTSNANSMET ISSPAQSHEV DHRSMDAILS
RMPLKQRVLY RVMPKSAKKR LANELRLKTS RRNEAVQTDM FLLQALLHEE ILKMELNNEL
PSVRQMTSSP SRLVTSGINV KSTHPVSISH DIPKPTVKTT ALREDEV
//
