KAT6_ORYSJ
ID KAT6_ORYSJ Reviewed; 593 AA.
AC A2ZX97;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Potassium channel KAT6;
GN OrderedLocusNames=Os01g0718700, LOC_Os01g52070; ORFNames=OsJ_03266;
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 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).
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}.
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DR EMBL; AP008207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP014957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000138; EAZ13344.1; -; Genomic_DNA.
DR AlphaFoldDB; A2ZX97; -.
DR SMR; A2ZX97; -.
DR STRING; 4530.OS01T0718700-00; -.
DR PaxDb; A2ZX97; -.
DR PRIDE; A2ZX97; -.
DR eggNOG; KOG0498; Eukaryota.
DR InParanoid; A2ZX97; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
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..593
FT /note="Potassium channel KAT6"
FT /id="PRO_0000410882"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..64
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..129
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..221
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 222..241
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..247
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..593
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 522..593
FT /note="KHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00823"
FT BINDING 350..470
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
SQ SEQUENCE 593 AA; 66839 MW; C148183A2DAEDD56 CRC64;
MAASRSELLR PAFGEPSPSL GPFVVNPHTC SYRWWQKFLI VLVLYTAWAS PFELAMEKSA
SAALAVTELV VDAFFAVDIA VSFFVAYRDA STGLLVTDRK KIATRHLARP CLALDVASTI
PLQMIYRIVS GKRQALYGLL NLLRLWRLRR VSKLFARLEK DIRFSYLWTR LIKLLYVTLF
AVHFASCIYL WMAFHHKAKE LTWIGSQFHG FEDRSVWFCY TCAVYWSITT LATVGYGDLH
AANTGEMLFS IAFMLFNMGL TSYIIGNITN LVVHETTNTF KMRDMVQRTS VFGRTNRLPV
AMREQMMESL QLRFRAEEQL QQEMLSELPK AVRSGIAQHM FRGAVQSCYL FQGVSDKLVL
PLVAEMKAES FPPKADIILE NEASTDCYII VSGEVEVLTT LEDGTEKQVM RIGPRGMAGE
IGVMFNIPQP FTIRSRKLTQ LVRISHSHMV STIRPNTADG VVVFSNFVLY LESLKVKAKE
TAFVRDHLRN GYSTVLGSAT MFDVDESKES AHKMLPCKEP KRVSIHEHLL NGTGTALNGS
SGKLVILPDS MQDLMKLSEK KFGKAARGIL TVGGAEVEDI EVIRDGDHLF FSW
