ID A0A158P8I2_ANGCA Unreviewed; 305 AA.
AC A0A158P8I2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Potassium channel subfamily K member 1 {ECO:0000313|WBParaSite:ACAC_0000710301-mRNA-1};
OS Angiostrongylus cantonensis (Rat lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Metastrongyloidea; Angiostrongylidae; Angiostrongylus.
OX NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000710301-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_0000710301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) 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 STRING; 6313.A0A158P8I2; -.
DR WBParaSite; ACAC_0000710301-mRNA-1; ACAC_0000710301-mRNA-1; ACAC_0000710301.
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; IPR005408; 2pore_dom_K_chnl_TWIK.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11003; POTASSIUM CHANNEL, SUBFAMILY K; 1.
DR PANTHER; PTHR11003:SF249; TWO PORE POTASSIUM CHANNEL PROTEIN SUP-9; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01586; TWIKCHANNEL.
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 125..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 91..149
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT DOMAIN 186..264
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
SQ SEQUENCE 305 AA; 34997 MW; AE8F419F0AA7FB7E CRC64;
MRENWTPSTA IPSLILNEEE WIYRFTASFS GNPTNFSAVE ELDNTLSKKD KLCSTFYNVD
VFLSESEVDQ LFADIRDAVL NGIWVEKNVT SSPNWSFGQA FFFAGTLIST VGYGRVSPRT
EYGKLFTIVY CVIGIPLTLA LLSATVVRLK RPSQILRGVL NRRLAHIFHA DQIQMFHLFI
VCLLLLIFVF IIPSWIFTNI ETDWTFLDAF YYCFVSLTTI GLGNYEPGDS PDQEYRSVYK
IIATVYLLIG LCCMMLFLAT LYEMPQFNLT RFFLKTDEEM RIRDDATHST LSMTVEKNXX
XXXXX
//