ID A0A016W2V1_9BILA Unreviewed; 1082 AA.
AC A0A016W2V1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Potassium channel domain-containing protein {ECO:0000259|Pfam:PF07885};
GN Name=Acey_s0002.g884 {ECO:0000313|EMBL:EYC33592.1};
GN Synonyms=Acey-twk-31 {ECO:0000313|EMBL:EYC33592.1};
GN ORFNames=Y032_0002g884 {ECO:0000313|EMBL:EYC33592.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC33592.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYC33592.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JARK01001338; EYC33592.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016W2V1; -.
DR Proteomes; UP000024635; 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:UP000024635};
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 95..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 180..236
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT DOMAIN 307..381
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT REGION 908..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1082 AA; 123377 MW; 3467DD3B8CE9A1B7 CRC64;
MLLNGYELVN VPFAHHLLDV FSFSRPTSAQ SGTSLGSKIR FSFDSLLSRP DHADIMLGQR
RRSSQYDEMI RRDRGPPKSW LGKAKYYYDK YNCRYFAPFL LLFFYSLLGA WIFYLVEYNN
EKEMKVKEEW DLNRLRNSTF QRIVGVFQTR TRMERATKSR NLLLWYEKEL QRVKLPEALE
WDMWGALFYV GTIFTTIGYG NIVPRTITGR ALSVVYAIIG IPLVLAILSR FGQFLEHTIT
RAWLRHRDRI KDAREKTRKR FIAKSKEGKS LESLEEGKLT SPTPSEFLEE HLIEDSRTIP
IWLALLFCIS WICACAALFL IWEKRWTFFT SLYFFFISLS TIGLGDVVPD HPHMLILMFW
LVIIGLSIVS MLLTVIQIKF EECLYNLMIR MQEEYHKNLA SGTPFDHEEI RRRAMEHQPF
LMKLFGPDLM SEDQREKIEE KAEQFERVIR ITNNKNIQTE PPAAFGAATQ MEKNANSMAC
DPMSESDHIR VVNGETQWSR QYPSMMAEEH SSDSDDHDSM SDATSLPMDS ISFSARRHTD
RSQKKVAFCT GCASHDSSAR NGLLRDASKA VDENVQTDIA QFQIDEIVLR LAALQANRPR
PNLVDRGIEA SLLCTGKRGK KRGRTESIED KSVKDMTDKE ILTTMLQVMT QSMETDPIAP
KSTKDLGVNT IPHSMASCGV STNPISCRTQ SIETDANDVM NKSIATDAAM LMDKTTETSR
SDQVDPTAKM SWDEKLRHDI MTSPLLRRLV MKTSGISRNP SFDVDDHSQQ TSLIIDPKRA
DADRSQQTSL IIDRPHPEVD RSLQTSPNFD KDLNDRSVQF APDYADRMTS PMPGDPLHRS
FQTASDEMTD RSQQTSRHMV DRTQETSRVE MVTQGVGTDQ EPGGYNPGTD WHRGSASMYE
GRMTDSMTAS TQYSPPMSRS VTTQNGDNLD VKNGKARSLS TSGLGTSAYE DESRQEVIIQ
TDDSYLKIAR RLDEYRSNRT QFLPVVAASP LCSRDIEPFK TDRPSERRGF YIDVKGLQRK
RSSVKARRKM SHHKNRLGGN AEAQTGSSMD HELEPIPSSE SDTSQRKHSS ENPRKHGASA
AY
//