ID   KAT2_ORYSJ              Reviewed;         601 AA.
AC   Q5QNI1;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Potassium channel KAT2;
GN   OrderedLocusNames=Os01g0210700, LOC_Os01g11250;
GN   ORFNames=P0031E09.16, P0466B10.26;
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 [MRNA].
RC   STRAIN=cv. Dongjin;
RA   Hwang H., Jeong M., Kim H., Lee H., Park H., Byun M., Kim B.;
RT   "Putative potassium channel mRNA.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [3]
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   [4]
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   [5]
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=ADJ67989.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC       Sequence=BAD73027.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAD73049.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAF04284.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; GQ386814; ADJ67989.1; ALT_SEQ; mRNA.
DR   EMBL; AP002092; BAD73027.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP002093; BAD73049.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008207; BAF04284.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015614092.1; XM_015758606.1.
DR   RefSeq; XP_015614100.1; XM_015758614.1.
DR   AlphaFoldDB; Q5QNI1; -.
DR   SMR; Q5QNI1; -.
DR   STRING; 4530.OS01T0210700-01; -.
DR   PRIDE; Q5QNI1; -.
DR   EnsemblPlants; Os01t0210700-02; Os01t0210700-02; Os01g0210700.
DR   GeneID; 4325560; -.
DR   Gramene; Os01t0210700-02; Os01t0210700-02; Os01g0210700.
DR   KEGG; osa:4325560; -.
DR   eggNOG; KOG0498; Eukaryota.
DR   InParanoid; Q5QNI1; -.
DR   OrthoDB; 464006at2759; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   ExpressionAtlas; Q5QNI1; baseline and differential.
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; 2.
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..601
FT                   /note="Potassium channel KAT2"
FT                   /id="PRO_0000410878"
FT   TOPO_DOM        1..42
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        43..63
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        64..71
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        93..112
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        134..144
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        166..179
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        201..227
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        228..247
FT                   /note="Pore-forming; Name=Segment H5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        248..251
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        273..601
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          530..601
FT                   /note="KHA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00823"
FT   BINDING         356..475
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
SQ   SEQUENCE   601 AA;  69807 MW;  B51B202A0C5F2C96 CRC64;
     METISNIFHN DPLPPLGARA NQSIKLRKFI ISPYDSRYRT WETFLLVLVV YSAWICPFEL
     AYLRNLSWKV SLVDNIIDSF FAIDIILTFF LAYLDQKSYL LVDDPKRIVA RYFSSWFLFD
     VCSTIPYQLL GQIFKKHENG LAYRLLSMLR LWRLRRLSEL FARLEKDIRL NYYWIRCTKL
     ISVTLFAVHC SGCFNYLIAD RYPNPARTWI GAAIPNYRSQ NLWVRYVTAI YWSITTLTTT
     GYGDLHAENQ REMLFSICYM LFNLGLTAYL IGNMTNLVVQ GSCRTRNFRD TIHAASQFAA
     RNQLPGHIKD EMLSHICLRY KTEGLKQKET LDSLPKGIRS SIACNLFLPV IEKVYLFHGV
     SFTCMIQLVT EMEAEYYPPR EVVILQNEAP RDVYILVSGA VEERVEIDGT EKVQEVLCNG
     EIFGEIGVIC SIPQPCAFHT IKVSQLLRLN TAVLKNIIKE NSDDRRVILN NLSQKMNQDH
     RFSTEVMEKS LQMMHQHFGE YNRCSALNQD NEKNELKANN GHSMALEWKR VTIHMYSQRN
     KRPEAPLAKV INLPGSLDKL FAIACQKFNN YRLTKLVNPE FAEIDDITVI RDGDHLFFME
     I