ID A0A1U7VZH0_NICSY Unreviewed; 834 AA.
AC A0A1U7VZH0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Potassium channel {ECO:0000256|RuleBase:RU369015};
GN Name=LOC104222255 {ECO:0000313|RefSeq:XP_009771768.1};
OS Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4096 {ECO:0000313|Proteomes:UP000189701, ECO:0000313|RefSeq:XP_009771768.1};
RN [1] {ECO:0000313|Proteomes:UP000189701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23773524; DOI=10.1186/gb-2013-14-6-r60;
RA Sierro N., Battey J.N., Ouadi S., Bovet L., Goepfert S., Bakaher N.,
RA Peitsch M.C., Ivanov N.V.;
RT "Reference genomes and transcriptomes of Nicotiana sylvestris and Nicotiana
RT tomentosiformis.";
RL Genome Biol. 14:R60.1-R60.17(2013).
RN [2] {ECO:0000313|RefSeq:XP_009771768.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_009771768.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Potassium channel. {ECO:0000256|RuleBase:RU369015}.
CC -!- SUBUNIT: The potassium channel is composed of a homo- or
CC heterotetrameric complex of pore-forming subunits.
CC {ECO:0000256|RuleBase:RU369015}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU369015}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU369015}.
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:0000256|RuleBase:RU369015}.
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.
CC {ECO:0000256|RuleBase:RU369015}.
CC -!- SIMILARITY: Belongs to the potassium channel family. Plant (TC 1.A.1.4)
CC subfamily. {ECO:0000256|ARBA:ARBA00007929,
CC ECO:0000256|RuleBase:RU369015}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU369015}.
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DR RefSeq; XP_009771768.1; XM_009773466.1.
DR AlphaFoldDB; A0A1U7VZH0; -.
DR STRING; 4096.A0A1U7VZH0; -.
DR GeneID; 104222255; -.
DR KEGG; nsy:104222255; -.
DR eggNOG; KOG0498; Eukaryota.
DR OrthoDB; 38039at2759; -.
DR Proteomes; UP000189701; Unplaced.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:UniProtKB-UniRule.
DR GO; GO:0034765; P:regulation of monoatomic ion transmembrane transport; IEA:UniProtKB-UniRule.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 1.10.287.630; Helix hairpin bin; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
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; POTASSIUM CHANNEL AKT1; 1.
DR PANTHER; PTHR45743:SF11; POTASSIUM CHANNEL DOMAIN-CONTAINING PROTEIN; 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; Ankyrin repeat; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51490; KHA; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
KW Ion channel {ECO:0000256|RuleBase:RU369015,
KW ECO:0000313|RefSeq:XP_009771768.1};
KW Ion transport {ECO:0000256|RuleBase:RU369015};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU369015};
KW Potassium {ECO:0000256|RuleBase:RU369015};
KW Potassium channel {ECO:0000256|RuleBase:RU369015};
KW Potassium transport {ECO:0000256|RuleBase:RU369015};
KW Reference proteome {ECO:0000313|Proteomes:UP000189701};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU369015};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU369015}; Transport {ECO:0000256|RuleBase:RU369015};
KW Voltage-gated channel {ECO:0000256|RuleBase:RU369015}.
FT TRANSMEM 83..102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 122..140
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 221..243
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 275..294
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 306..331
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT DOMAIN 406..527
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REPEAT 584..616
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 617..649
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 681..713
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 761..834
FT /note="KHA"
FT /evidence="ECO:0000259|PROSITE:PS51490"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 834 AA; 95114 MW; 2A70244EE94AE871 CRC64;
MDRGKGRGED SEDEEFKVED LQESSNSKKL ASNWKNRFKL LRNYSSLDTN NVSVRNGDQG
RDSTSRGGRR DHCYGFVIHP DNWWYLLWTQ FILIWAIYSS FFTPLEFGFF RGLPENLFLL
DIAGQIAFLI DIVVLFFVAY RDAHSYCMVY DRKLIALRYL KSRFLVDLLG CFPWDAIYKA
CGRKEPVRYL LWIRLSRALR VTEFFEKLEK DIRLNYLFTR IVKLLVVEVY CTHTAACIFY
YLATTLPPWE EGYTWIGSLK MGDYSYAHFR GIDLWTRYIT SLYFAIVTMA TVGYGEIHAV
NTKEMIFVMI YVSFDMILGA YLLGNMAALI VKGSKTEKFR DKMADLIKYM NRNRLGKRIS
KEIKDHVRLQ YESRYNESSV LQDIPASIRA KISQKLYEPY IRGVPLFRGC SHEFIKQIAI
KVHEEFFLPG EVIMEQGSMA DQLYFVCHGK VEEVRKPEEN ETEESLLDLH TYNSVGEISV
LCNIPVPYTV QVYELSRLLR IDKQALVEIL GIYFSDGRVI INNLLEGRES SLRSKILDSD
ITLNIAKHES ELTMRLNCAA HDGDLYRLSR IIGAGADPSR TDYDGRSPLH LAASKGHGDI
TVFLIQRGVE INARDKFGST ALLEAVKNGH DHVASLLMEA GALLGIDNDG TCLCEAVSKR
DLDYLRRLLD SGINPNSKNY DFRTPLHLAA SEGLFPISVL LLEAGASVFA VDRWGRTPLD
EARVGGNKNL IKLLEDAQGS QLSEFSTSFG KQDEGQRVRC RVFASDPRSL KDERRKVVLW
VPQSIDELIN TAKAQLRVSS ANCVVSEDGA KILDTDMISD GQKLFLVRES TLSL
//
