KAT1_ORYSJ
ID KAT1_ORYSJ Reviewed; 718 AA.
AC Q6K3T2; Q0E2F2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Potassium channel KAT1;
GN OrderedLocusNames=Os02g0245800, LOC_Os02g14840;
GN ORFNames=OJ1134_F06.17, OSJNBa0090H18.7;
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=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-539.
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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=BAF08336.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP004117; BAD27742.1; -; Genomic_DNA.
DR EMBL; AP005614; BAD19939.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF08336.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK100808; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015623358.1; XM_015767872.1.
DR AlphaFoldDB; Q6K3T2; -.
DR SMR; Q6K3T2; -.
DR STRING; 4530.OS02T0245800-01; -.
DR PaxDb; Q6K3T2; -.
DR PRIDE; Q6K3T2; -.
DR EnsemblPlants; Os02t0245800-01; Os02t0245800-01; Os02g0245800.
DR GeneID; 4328864; -.
DR Gramene; Os02t0245800-01; Os02t0245800-01; Os02g0245800.
DR KEGG; osa:4328864; -.
DR eggNOG; KOG0498; Eukaryota.
DR HOGENOM; CLU_005746_8_2_1; -.
DR InParanoid; Q6K3T2; -.
DR OrthoDB; 247304at2759; -.
DR PlantReactome; R-OSA-3899351; Abscisic acid (ABA) mediated signaling.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6K3T2; 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 2: Evidence at transcript level;
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..718
FT /note="Potassium channel KAT1"
FT /id="PRO_0000410877"
FT TOPO_DOM 1..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..88
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..245
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 246..265
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..269
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..718
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 647..718
FT /note="KHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00823"
FT REGION 560..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 374..493
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
SQ SEQUENCE 718 AA; 82975 MW; 4B67BAEF978773A3 CRC64;
MTQAHSKSCF HQFWDGLQIK RSSDSFTVEL LPSLGATINH SNKLQKFIIS PYDPRYRSWE
LFLIVLVVYS AWICPFELAF LRDLPSKLLL VENIVDIFFA IDIVLTFFVA YVDSKTHLLV
DDRKRIAMRY LSTWFIFDVC STAPFQPIIL LFTHKGNDIA FKVLNLLRLW RLHRVSSLFA
RLEKDIRFNY FWTRCSKLIS VTLFAVHCAG CFNYMIADRY PNPEKTWIGA VMSTFRSESL
WTRYITALYW SITTLTTTGY GDLHAENPTE MLFDIVYMMF NLGLTAYLIG NMTNLVVHGT
SRTRKFRDSI QAASEFAARN QLPENIKQQV LSHFCLQFKT EGLNQQVMLD CLPKGIRSSI
AYSLFFPIIR QAYLFNGVSG NFIAELVMEV QAEYFPPKED IILQNEGEAD VYIVVSGAVN
IITTIHGNEQ VYEKIAEGEM FGEVGSLCNI PQPFTCRTAE LSQLLRISKT RLREIIEENR
EDSNILMNNL VQKLKLRESL PDMNQPDRRF LSKYELFHVP REAWLLKKSQ LHYTEHTSRD
SSNNTPVFGG DRYSRQLLGE ATRSSASENE NSSMTDKEEN HDEVHTNCEI KKRTEEHCIQ
INSEDSSSTY SQRTMNATVQ TGSPHKTEEN ITRRIPDEYY IKEANKRVTI HKYRHNSTVS
AAQNGKLIKL PTSLEELFKI GSQKFQGFHP RKVVSRDYAE IDDVSVIRDG DHLFLLEM
