ID A0A1S3T8W4_VIGRR Unreviewed; 717 AA.
AC A0A1S3T8W4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Potassium channel {ECO:0000256|RuleBase:RU369015};
GN Name=LOC106752947 {ECO:0000313|RefSeq:XP_014490211.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014490211.1};
RN [1] {ECO:0000313|RefSeq:XP_014490211.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014490211.1};
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}.
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 RefSeq; XP_014490211.1; XM_014634725.2.
DR AlphaFoldDB; A0A1S3T8W4; -.
DR STRING; 3916.A0A1S3T8W4; -.
DR GeneID; 106752947; -.
DR KEGG; vra:106752947; -.
DR OrthoDB; 38039at2759; -.
DR Proteomes; UP000087766; 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; 1.10.287.630; Helix hairpin bin; 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:SF6; POTASSIUM CHANNEL KAT1; 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,
KW ECO:0000313|RefSeq:XP_014490211.1};
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:UP000087766};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
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 64..84
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 96..115
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 198..220
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 274..300
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT DOMAIN 377..496
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 643..717
FT /note="KHA"
FT /evidence="ECO:0000259|PROSITE:PS51490"
FT REGION 522..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 717 AA; 83632 MW; 642DD711DDC4B2F3 CRC64;
MPFCSGQKFF KRFCVDEFQM ASLPYSSFLS NDLLPSLGAR INQETRLRRC TVSPFDPRYR
AWEMLLIVFV VYSAWICPFE FAFLHQKHDT LFIIDNIVNA FFAIDIVLTF FVAYLDHHSY
LLVDNPKKIA IRYLSTWFIF DVCSTAPFES ISLLFTDNRS EIGFKILNML RLWRLRRVSS
LFARLEKDIR FNYFWTRCFK LIAVTLFVVH FAGCFNYLIA DRYSDPKRTW IGSVFPNFKE
ESLWDRYVTS MYWSIVTLTT TGYGDLHATN TREMLFFIFY ILFNLGLTSY IIGNMTNLVV
HWTSRTRNFR DTVRAASEFA SRNHLPHHIQ EQMLSHLCLK FKTEGVKQQE TLNGLPKAIR
ASIAHHLFFS LLQRLYLFQG VSDDFLFQLV TEMEALYFPP KEDVILQNES PTDLYILVSG
AVDMIRYVDS NEKILKKANA EDIFGEIGVL YCRPQPFTVR TTELSQILRL SRTSLMNSLH
GYPEAAQIIM KNLFMRIKGH EGLDFECSPR EPQMHEMDNI DTSVPDSSAS NSHKETRLHI
PEDGKGDFDA TFRKDHAQME ENEKNQGPIR WKQKSLIDQQ QNKRLSDLAV NHENRKIVDE
HIINFLEPEI PFNYPLGKIY SNSYSSASNH RTQRETERFS KKRVVIHFLS KHKTSLQEHG
KLIMLPDSLQ ELLHIAGEKF GVSKLTKVIT IENAEIDDIS VIRDGDHLFF VCSDTEN
//
