ID A0A0D9V4I7_9ORYZ Unreviewed; 387 AA.
AC A0A0D9V4I7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Potassium channel domain-containing protein {ECO:0000259|Pfam:PF07885};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR01G23650.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR01G23650.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR01G23650.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR01G23650.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-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.1.7) family. {ECO:0000256|ARBA:ARBA00010159}.
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DR AlphaFoldDB; A0A0D9V4I7; -.
DR STRING; 77586.A0A0D9V4I7; -.
DR EnsemblPlants; LPERR01G23650.1; LPERR01G23650.1; LPERR01G23650.
DR Gramene; LPERR01G23650.1; LPERR01G23650.1; LPERR01G23650.
DR eggNOG; KOG1418; Eukaryota.
DR HOGENOM; CLU_033675_1_0_1; -.
DR Proteomes; UP000032180; Chromosome 1.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProt.
DR GO; GO:0005267; F:potassium channel activity; IEA:InterPro.
DR Gene3D; 1.10.287.70; -; 2.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11003:SF303; OS01G0696100 PROTEIN; 1.
DR PANTHER; PTHR11003; POTASSIUM CHANNEL, SUBFAMILY K; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 108..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 229..248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 112..185
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT DOMAIN 237..297
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 387 AA; 42845 MW; D394EE9719C13CD7 CRC64;
MSSMEEHLLP LVHRDQIYSS RQDRRKSSDV PNRRATSIYP SADIKGNPNT PNHPSPTSGN
ANSVSTQTFQ RVHSSPSMFT SVKEIPCADE FDEQNHAAQH VPSFARQAIV SVILYISIGV
LVYITNVDGF KGRSTLKLVD GLYFTIISLC TIGYGDIVPC TTFTKVFTCL FLLIGVRFVD
IVLNGLLTNV LDKQRTVLLS TMDDNKLNKV FDTYMIDAEK KRSRGRMKVL LALGVVAGTI
SICTIIVHEV EGLNWTDSFY LSVISVTTVG YGDYGFSTPA GRLSATVCLL VSTLAVAKAF
LFLTDLRMDT RNRKTTKWIL QKKMDNEPLA ADLHHDASVS RSDFLIYKLK EIGKIDDKDI
ATTSDQFDQL GLAKCGKITL ADIIGKL
//
