ID   AKT2_ORYSJ              Reviewed;         855 AA.
AC   Q75HP9; Q0DHZ5; Q5TKJ4;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Potassium channel AKT2;
GN   OrderedLocusNames=Os05g0428700, LOC_Os05g35410;
GN   ORFNames=OsJ_18626, OSJNBb0048I21.3, P0636F09.19;
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=16261349; DOI=10.1007/s00438-005-0039-y;
RA   Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA   Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA   Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT   "A fine physical map of the rice chromosome 5.";
RL   Mol. Genet. Genomics 274:337-345(2005).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 290-855.
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   -!- SUBUNIT: The potassium channel is probably a homo- or heterotetrameric
CC       complex of pore-forming subunits. {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=AAV59417.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAF17528.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC130600; AAV59417.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC135429; AAS90668.1; -; Genomic_DNA.
DR   EMBL; AP008211; BAF17528.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM000142; EEE63802.1; -; Genomic_DNA.
DR   EMBL; AK061594; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015637942.1; XM_015782456.1.
DR   AlphaFoldDB; Q75HP9; -.
DR   SMR; Q75HP9; -.
DR   STRING; 4530.OS05T0428700-01; -.
DR   PaxDb; Q75HP9; -.
DR   PRIDE; Q75HP9; -.
DR   GeneID; 4338867; -.
DR   KEGG; osa:4338867; -.
DR   eggNOG; KOG0498; Eukaryota.
DR   HOGENOM; CLU_005746_8_3_1; -.
DR   InParanoid; Q75HP9; -.
DR   OrthoDB; 281394at2759; -.
DR   Proteomes; UP000000763; Chromosome 5.
DR   Proteomes; UP000007752; Chromosome 5.
DR   Proteomes; UP000059680; Chromosome 5.
DR   Genevisible; Q75HP9; 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; 1.25.40.20; -; 2.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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; PF12796; Ank_2; 2.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF11834; KHA; 1.
DR   PRINTS; PR01463; EAGCHANLFMLY.
DR   SMART; SM00248; ANK; 5.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF51206; SSF51206; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS51490; KHA; 1.
PE   2: Evidence at transcript level;
KW   ANK repeat; Ion channel; Ion transport; Membrane; Potassium;
KW   Potassium channel; Potassium transport; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..855
FT                   /note="Potassium channel AKT2"
FT                   /id="PRO_0000410875"
FT   TOPO_DOM        1..75
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..105
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        127..149
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        171..179
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        201..214
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        236..262
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        263..282
FT                   /note="Pore-forming; Name=Segment H5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        283..285
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        307..855
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          536..565
FT                   /note="ANK 1"
FT   REPEAT          569..598
FT                   /note="ANK 2"
FT   REPEAT          602..631
FT                   /note="ANK 3"
FT   REPEAT          634..663
FT                   /note="ANK 4"
FT   REPEAT          667..696
FT                   /note="ANK 5"
FT   DOMAIN          768..855
FT                   /note="KHA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00823"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          744..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         391..511
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
SQ   SEQUENCE   855 AA;  94784 MW;  F37C097D3EEA7F2F CRC64;
     MKTSSFESAS SSGGSGGGGG GGGGEGSGSF NLRNLSKLIL PPLGVPAGGH AQSGHAGPND
     RRVISPLDSR YRCWDTFMVV LVAYSAWVYP FEVAFMNASP KGGLEVADIV VDLFFAVDIV
     LTFFVAYIDS RTQLLVRDRR RIATRYLSTF FIMDVASTIP FQGLAYIVTG EVRESPAFSL
     LGILRLWRLR KVKQFFTRLE KDIRFNYFWI RCARLIAVTL FLVHCAGCLY YLIADRYPHR
     EKTWIGAVIP DFQEASLWIR YTSSVYWSIT TMTTVGYGDM HAQNTVEMIF NIFYMLFNLG
     LTAYLIGNMT NLVVEGTRRT MEFRNSIRAA SNFVGRNHLP PRLKQQILAY MCLKFRAESL
     NQQQLMDQLP KSICKGICEY LFLPVVKDVY LFKGVSREVL LLMVTKMKPE YIPPKEDVIV
     QNEAPDDVYI VVSGEVEVIY SDGEAEERVV ATLGTRGVFG EVSALSDRPQ SFTLRTRTLC
     QLLRLRQAAL KEAMQSKPED SVVIIKNFLK HQIEMHDMKV EDLLGEDAAG EYDHGNIPCN
     LLTVAATGNS SFLEDLLKVG MDPDVGDSKG RTALHIAASK GYEDCVLVLL KQACNVNIKD
     AQGNTALWNA IAARHHKIFN ILYHFARVSS PHHAAGDLLC LAARRGDLDT LRELLKHGLA
     VDSEDRDGAT ALRVALAEGH ADVARLLVLN GASVDRAASH NEQQAAAAVS VDELRELMKT
     RELAHPVTIV VDSPSPAAAA VIREVGSSGD SRNGRRQSAR SDGAHWPRVS IYRGHPFVRN
     RSSEAGKLIN LPGTMEEFRI IIEEKLKVDA RKTLIMNDEG AEIDSIDVIR DNDKLFIVTE
     EHMTAVASMD SVSGS