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 24-JAN-2024, entry version 110.
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; 39947.Q652U9; -.
DR PaxDb; 39947-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:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
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; 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; POTASSIUM CHANNEL AKT1; 1.
DR PANTHER; PTHR45743:SF27; POTASSIUM CHANNEL KAT3; 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; cAMP-binding domain-like; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 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
//
