KAT3_ORYSJ
ID KAT3_ORYSJ Reviewed; 502 AA.
AC Q5JM04; A0A0P0V8B7;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Potassium channel KAT3;
GN OrderedLocusNames=Os01g0756700, LOC_Os01g55200; ORFNames=OJ1414_E05.9;
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=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 [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 MRNA].
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 -!- SIMILARITY: Belongs to the potassium channel family. Plant (TC 1.A.1.4)
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP003375; BAD87503.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF06204.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS74411.1; -; Genomic_DNA.
DR EMBL; AK100739; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015632943.1; XM_015777457.1.
DR AlphaFoldDB; Q5JM04; -.
DR SMR; Q5JM04; -.
DR STRING; 4530.OS01T0756700-01; -.
DR PaxDb; Q5JM04; -.
DR PRIDE; Q5JM04; -.
DR EnsemblPlants; Os01t0756700-01; Os01t0756700-01; Os01g0756700.
DR GeneID; 4325143; -.
DR Gramene; Os01t0756700-01; Os01t0756700-01; Os01g0756700.
DR KEGG; osa:4325143; -.
DR eggNOG; KOG0498; Eukaryota.
DR HOGENOM; CLU_005746_8_2_1; -.
DR InParanoid; Q5JM04; -.
DR OMA; YIGINNP; -.
DR OrthoDB; 464006at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q5JM04; 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; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45743; PTHR45743; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 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..502
FT /note="Potassium channel KAT3"
FT /id="PRO_0000410879"
FT TOPO_DOM 1..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..95
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..169
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..204
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..252
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 253..272
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..502
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 381..500
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT CONFLICT 467
FT /note="K -> E (in Ref. 5; AK100739)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 58008 MW; 7D4742FCDC8FC41F CRC64;
MPRSSRMNLW PHCFPCFDDG DRSGNRFSTV CNFPDDLLPS LGATAHQPPK LRKYLVSPYD
PRYKVWETFL IILVVYSAWI CPLEFAFLRY LPSAPFVVDD VVNGFFAVDI MLTFFVPFVD
KKSYLLVNDP KKIAVRYLSS WFVFDVCSTV PFHSISLLFN EHGHDLGFKF LNVLRLWRLR
RVSSMFARLE KDIRFNYAVI RCTKLISVTL FAIHCAGCIN YLIADRYPDP RRTWIGAVMP
NFREDGLWIR YVTAMYWSIT TLTTTGYGDL HAENAREMLF GICYMLFNLW LTAYLIGNMT
NLVVHSTSRT RDFRDVVQAA SEFAARNQLP QQIEEQMLNH ICLRYKTDGL KQQETLDVLP
KAMRSSISHY LFFRVVQGAY LFKGVSSRFI QQLVTEMQAE YFAPKEDIIL QNDSPSDLYL
LVSGAVDILV FLDGTEQVYR RAAEGELLGE IGVLCNKPQS FTFRTTKLSQ ILRISRTKLL
GIIQENREDG DIIRSNLQQV NV
