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Database: UniProt
Entry: A0A0D9UY73_9ORYZ
LinkDB: A0A0D9UY73_9ORYZ
Original site: A0A0D9UY73_9ORYZ 
ID   A0A0D9UY73_9ORYZ        Unreviewed;       542 AA.
AC   A0A0D9UY73;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Potassium channel {ECO:0000256|RuleBase:RU369015};
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:LPERR01G06690.5, ECO:0000313|Proteomes:UP000032180};
RN   [1] {ECO:0000313|EnsemblPlants:LPERR01G06690.5, 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:LPERR01G06690.5, 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:LPERR01G06690.5}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- FUNCTION: Potassium channel. {ECO:0000256|RuleBase:RU369015}.
CC   -!- SUBUNIT: The potassium channel is composed of a homo- or
CC       heterotetrameric complex of pore-forming subunits.
CC       {ECO:0000256|RuleBase:RU369015}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU369015}; Multi-
CC       pass membrane protein {ECO:0000256|RuleBase:RU369015}.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids. The pore-
CC       forming region H5 is enclosed by the transmembrane segments S5 and S6
CC       in the Shaker-type (1P/6TM) and contains the GYGD signature motif which
CC       seems to be involved in potassium selectivity.
CC       {ECO:0000256|RuleBase:RU369015}.
CC   -!- SIMILARITY: Belongs to the potassium channel family. Plant (TC 1.A.1.4)
CC       subfamily. {ECO:0000256|ARBA:ARBA00007929,
CC       ECO:0000256|RuleBase:RU369015}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU369015}.
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DR   AlphaFoldDB; A0A0D9UY73; -.
DR   EnsemblPlants; LPERR01G06690.5; LPERR01G06690.5; LPERR01G06690.
DR   Gramene; LPERR01G06690.5; LPERR01G06690.5; LPERR01G06690.
DR   Proteomes; UP000032180; Chromosome 1.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0034765; P:regulation of monoatomic ion transmembrane transport; IEA:UniProtKB-UniRule.
DR   CDD; cd00038; CAP_ED; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR045319; KAT/AKT.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR45743; POTASSIUM CHANNEL AKT1; 1.
DR   PANTHER; PTHR45743:SF6; POTASSIUM CHANNEL KAT1; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
PE   3: Inferred from homology;
KW   Ion channel {ECO:0000256|RuleBase:RU369015};
KW   Ion transport {ECO:0000256|RuleBase:RU369015};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU369015};
KW   Potassium {ECO:0000256|RuleBase:RU369015};
KW   Potassium channel {ECO:0000256|RuleBase:RU369015};
KW   Potassium transport {ECO:0000256|RuleBase:RU369015};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU369015};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU369015}; Transport {ECO:0000256|RuleBase:RU369015};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU369015}.
FT   TRANSMEM        44..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369015"
FT   TRANSMEM        75..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369015"
FT   TRANSMEM        190..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369015"
FT   TRANSMEM        221..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369015"
FT   DOMAIN          323..442
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
SQ   SEQUENCE   542 AA;  63010 MW;  03B1D6C7BB57CB05 CRC64;
     METISNIFHN DPLPPLGARA NQSIKLRKFI ISPYDTRYRT WETFLLVLVV YSAWICPFEL
     AYLRNLSWKV SLVDYTVDSF FAIDIILTFF LAYLDRKSYL LVDDPKRIAA RLLSMLRLWR
     LRRLSELFAR LEKDIRLNYY WIRCTKLISV TLFAVHCSGC FNYLIADRYH NPARTWIGAA
     IPNYRSESLW IRYITAIYWS ITTLTTTGYG DLHAENSREM LFSICYMLFN LGLTAYLIGN
     MTNLVVQGSC RTRNFRDTIH AASQFAARNQ LPEHIKIEML SHICLRYKTE GLKQKETLDS
     LPKGIRLSIA CNLFLPVIEK VYLFHGVSFT CMHQLVTEME AEYYPPREVV ILQNEAPTDV
     YILVSGQVEA RIEIDGTEKV QEVLCGGEMF GEIGGLCSIP QSCAFHTTKV SQLLRLNTAV
     LKNIIKENSE DRQIILNNLC QFFRTGQKMN QDHRFSTEVM EKSLHMLHHF GEYNKCSASN
     QANEIEVKSN NGHSMALEWK RVTIHMYPQK NKRPEKFNNY RPTKVFNPEF AEIDDITNFE
     AM
//
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