ID   KAT4_ORYSJ              Reviewed;         591 AA.
AC   Q652U9;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Potassium channel KAT4;
GN   OrderedLocusNames=Os06g0254200, LOC_Os06g14310;
GN   ORFNames=P0046H10.36, P0592E11.6;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
CC   -!- FUNCTION: Probable inward-rectifying potassium channel. Assuming opened
CC       or closed conformations in response to the voltage difference across
CC       the membrane, the channel is activated by hyperpolarization (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- DOMAIN: The KHA domain (rich in hydrophobic and acidic residues)
CC       present in the C-terminal part is likely to be important for
CC       tetramerization. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the potassium channel family. Plant (TC 1.A.1.4)
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD45227.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAD46168.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AP003490; BAD45227.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP005518; BAD46168.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP014962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q652U9; -.
DR   SMR; Q652U9; -.
DR   STRING; 4530.OS06T0254200-00; -.
DR   PaxDb; Q652U9; -.
DR   PRIDE; Q652U9; -.
DR   eggNOG; KOG0498; Eukaryota.
DR   HOGENOM; CLU_005746_8_2_1; -.
DR   InParanoid; Q652U9; -.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
DR   Genevisible; Q652U9; OS.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   CDD; cd00038; CAP_ED; 1.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR   InterPro; IPR045319; KAT/AKT.
DR   InterPro; IPR021789; KHA_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR45743; PTHR45743; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF11834; KHA; 1.
DR   PRINTS; PR01463; EAGCHANLFMLY.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; SSF51206; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS51490; KHA; 1.
PE   3: Inferred from homology;
KW   Ion channel; Ion transport; Membrane; Potassium; Potassium channel;
KW   Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..591
FT                   /note="Potassium channel KAT4"
FT                   /id="PRO_0000410880"
FT   TOPO_DOM        1..32
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..53
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        54..63
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        85..109
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        131..137
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..172
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        194..220
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        221..240
FT                   /note="Pore-forming; Name=Segment H5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        241..246
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        268..591
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          521..591
FT                   /note="KHA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00823"
FT   BINDING         349..469
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
SQ   SEQUENCE   591 AA;  67394 MW;  D8A142974428D5FC CRC64;
     MAARSELLRP AFGEASPSLG RFVINPHSCS YRWWHMFLIM LVLYSAWASP FELSMEKAAS
     IALVVTDLVV DVFFAIDIAL SFFVAYRDTS TGLLITDRRK ITMRYLKRPC FALDVASTIP
     LQIIYQLVTG KRQGLWGLLN LLRLWRLRRV SKLFARVEKD IRFNYLWTRL IKLLCVTLFA
     LHFAACIYLW MAFNYKIKEL TWIGSQIHSF EDRSVWFCYT CAVYWSITTL ATVGYGDLHA
     TNIGEMLFSI AFMLFNMGLT SYIIGNITNL VVRETSNTFK MRDMVQRVSE FGRMNRLPEA
     MREQMLASVQ LRFRTDEQLQ QEMLSELPKA VRSGVMKHMF KSAIESCYLF QGVSDSLIVQ
     LVAEMKAEFF PPKANVILEN ETSTDCYIII SGEVEALTTL ADGTEKHVKR IGPRGMAGEI
     GVMFSIPQPF TIRSRRLTQV VRISHIHLLQ AVRPNTADGY IVFSNFIQYL ESLKVQTKDV
     AFVSDHLWNG NSMVLRRATE VAVDESKEAA HKMLPCKEPK RVVIHEQLPN ATSTALHPSP
     GKLVLLPDSM QELMKLSEKK FGKAVRGILT VEGAEVEDIE VIRDGDHLLF S