KOR1_ORYSJ
ID KOR1_ORYSJ Reviewed; 858 AA.
AC Q653P0; A0A0N7KLV3; Q0DD66;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Potassium channel KOR1;
DE AltName: Full=K(+) outward-rectifying channel 1;
GN OrderedLocusNames=Os06g0250600, LOC_Os06g14030;
GN ORFNames=OSJNBa0091G06.35, P0431E05.11;
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; TISSUE=Embryo;
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].
RC STRAIN=cv. Nipponbare;
RG The rice full-length cDNA consortium;
RT "Oryza sativa full length cDNA.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable outward-rectifying potassium channel. {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=BAF19207.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP004651; BAD45736.1; -; Genomic_DNA.
DR EMBL; AP005107; BAD45977.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF19207.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014962; BAS97057.1; -; Genomic_DNA.
DR EMBL; AK242807; BAH01347.1; -; mRNA.
DR RefSeq; XP_015644419.1; XM_015788933.1.
DR AlphaFoldDB; Q653P0; -.
DR SMR; Q653P0; -.
DR STRING; 4530.OS06T0250600-01; -.
DR PaxDb; Q653P0; -.
DR PRIDE; Q653P0; -.
DR EnsemblPlants; Os06t0250600-01; Os06t0250600-01; Os06g0250600.
DR GeneID; 4340653; -.
DR Gramene; Os06t0250600-01; Os06t0250600-01; Os06g0250600.
DR KEGG; osa:4340653; -.
DR eggNOG; KOG0498; Eukaryota.
DR HOGENOM; CLU_005746_8_3_1; -.
DR InParanoid; Q653P0; -.
DR OMA; PDTYRMV; -.
DR OrthoDB; 160363at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q653P0; 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; 1.
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; 4.
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; 3.
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..858
FT /note="Potassium channel KOR1"
FT /id="PRO_0000410883"
FT TOPO_DOM 1..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..130
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..201
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 293..312
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 313..316
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..858
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 559..592
FT /note="ANK 1"
FT REPEAT 596..625
FT /note="ANK 2"
FT REPEAT 629..658
FT /note="ANK 3"
FT REPEAT 660..689
FT /note="ANK 4"
FT REPEAT 693..722
FT /note="ANK 5"
FT REPEAT 726..756
FT /note="ANK 6"
FT DOMAIN 772..858
FT /note="KHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00823"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 419..539
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
SQ SEQUENCE 858 AA; 97379 MW; 65F50E52C0B0455A CRC64;
MGRGIGSKRR VEDDDGENMP GRKKKEEEEE EEDDDGEEEY EVDVVRDRIG SSRGSRLALF
GSDLRLGRFR PRRRRVAPVD GDDGIFQDFV IDPDNKWYRL WTRFILVWAV YSSFFTPLEF
GFFRGLPRNL FFLDIAGQIA FLIDIVLRFF VAYRDPDTYR MVHNPTSIAL RYCKSSFIFD
LLGCFPWDAI YKACGSKEEV RYLLWIRLTR AMKVTEFFRS MEKDIRINYL FTRIVKLIVV
ELYCTHTAAC IFYYLATTLP ESMEGYTWIG SLQLGDYSYS HFREIDLTKR YMTSLYFAIV
TMATVGYGDI HAVNVREMIF IMIYVSFDMI LGAYLIGNMT ALIVKGSRTE RFRDKMKEVI
RYMNRNKLGK DIREQIKGHL RLQYESSYTE ASVLQDIPVS IRAKISQTLY KPYIESIPLF
KGCSAEFIQQ IVIRLQEEFF LPGEVILEQG SAVDQLYFVC HGALEGVGIG EDGQEETILM
LEPESSFGEI AVLCNIPQPF TVRVCELCRL LRLDKQSFTN ILEIFFVDGR RILSNLSESS
EYGSRIKQLE SDITFHIGKQ EAELTLRVNN AAFYGDMHQL KSLIRAGADP KNTDYDGRSP
LHLAACKGFE DVVQFLLHEG VDIDLSDKFG NTPLLEAVKQ GHDRVATLLF SKGAKLSLEN
AGSHLCTAVA RGDTDFVRRA LAYGGDPNAR DYDHRAPLHI AAAEGLYLMA KLLVDAGASV
FATDRWGTTP LDEGRRCGSR TMVQLLEAAK SGELSRYPER GEEVRDKMHP RRCSVFPHHP
WDGGERRREG VVVWIPHTIE GLVSSAQEKL GLAGSGEGLR LLGEDGARVL DVDMVHDGQK
LYLVVGGGGD DGGTEARQ
