ID A0A314LE53_NICAT Unreviewed; 566 AA.
AC A0A314LE53;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Potassium channel {ECO:0000256|RuleBase:RU369015};
DE Flags: Fragment;
GN Name=KAT3_2 {ECO:0000313|EMBL:OIT39935.1};
GN ORFNames=A4A49_59084 {ECO:0000313|EMBL:OIT39935.1};
OS Nicotiana attenuata (Coyote 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=49451 {ECO:0000313|EMBL:OIT39935.1, ECO:0000313|Proteomes:UP000187609};
RN [1] {ECO:0000313|EMBL:OIT39935.1, ECO:0000313|Proteomes:UP000187609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UT {ECO:0000313|Proteomes:UP000187609};
RC TISSUE=Leaves {ECO:0000313|EMBL:OIT39935.1};
RA Xu S., Brockmoeller T., Gaquerel E., Navarro A., Kuhl H., Gase K., Ling Z.,
RA Zhou W., Kreitzer C., Stanke M., Tang H., Lyons E., Pandey P., Pandey S.P.,
RA Timmermann B., Baldwin I.T.;
RT "The genome of Nicotiana attenuata.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OIT39935.1}.
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DR EMBL; MJEQ01000067; OIT39935.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A314LE53; -.
DR STRING; 49451.A0A314LE53; -.
DR EnsemblPlants; OIT39935; OIT39935; A4A49_59084.
DR Gramene; OIT39935; OIT39935; A4A49_59084.
DR Proteomes; UP000187609; Unassembled WGS sequence.
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; 2.60.120.10; Jelly Rolls; 1.
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:SF27; POTASSIUM CHANNEL KAT3; 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; cAMP-binding domain-like; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51490; KHA; 1.
PE 3: Inferred from homology;
KW Ion channel {ECO:0000256|RuleBase:RU369015, ECO:0000313|EMBL:OIT39935.1};
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:UP000187609};
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 41..64
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 141..162
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 190..209
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 221..243
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT DOMAIN 320..439
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 497..566
FT /note="KHA"
FT /evidence="ECO:0000259|PROSITE:PS51490"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OIT39935.1"
SQ SEQUENCE 566 AA; 64490 MW; 3CD9FA778E8CE96D CRC64;
RIWQTFLVVL VAYSGWSSPF ELAFKKVASE GLLPLDIMVD AFFAIDILLT FFVAYLDKST
YLLVDDHKKI ALRYVIHLGF PMDVASTVPF QTIYQILDGK KQGEDVFGFL NLLRLWRLRR
VNKFFSRLEK DIQFSYFWTR FCKLICVTLF AVHSVGCLYY WLATHYHTAE NTWIGSNVTN
FQERSISLGY TYSMYWSVAT LTTVGYGDLR AHNTGEKIFS IFYMLFNIGL TAYLIGNITN
LIVHGIARTF AMRDAINKTL RYASKNRLPE DIKEQMLAHL TLKFKTAELQ QEEVIRDLPK
AIRCSIAQYL FHTTIENTYL FKGVSEDFLV QLVSEIKAEY FPPKVDIVIQ NEIPTDFYII
VSGAVEVVTY KNGIEQFLSK LESPELFGEV GVIFNTPQPF TVRSKRLSQV VRISHHHFKQ
LVQPLNADGK IILSNFLQHL KGMGKEELQE IPLISELLSD LNSEAGTVSR VQNHEGHSQD
GNRFCVTGIT TTTLPVRVII HGHHPHEKTK EGGIAGKLIH LPQSVEDLLI IAGKRFGKRG
STVLMADGSP MEDLGALREN DHLYIV
//
