ID A0A1S2Y8V8_CICAR Unreviewed; 582 AA.
AC A0A1S2Y8V8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Potassium channel {ECO:0000256|RuleBase:RU369015};
GN Name=LOC101503528 {ECO:0000313|RefSeq:XP_004501265.1};
OS Cicer arietinum (Chickpea) (Garbanzo).
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; Hologalegina; IRL clade; Cicereae; Cicer.
OX NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_004501265.1};
RN [1] {ECO:0000313|RefSeq:XP_004501265.1}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004501265.1};
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|RuleBase:RU369015}; Multi-
CC pass membrane protein {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_004501265.1; XM_004501208.3.
DR AlphaFoldDB; A0A1S2Y8V8; -.
DR GeneID; 101503528; -.
DR OrthoDB; 38039at2759; -.
DR Proteomes; UP000087171; Chromosome Ca5.
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; 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 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_004501265.1};
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:UP000087171};
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 52..69
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 89..116
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT DOMAIN 338..457
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 514..582
FT /note="KHA"
FT /evidence="ECO:0000259|PROSITE:PS51490"
FT REGION 477..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 582 AA; 66654 MW; 650D88FC8F78DB51 CRC64;
MSLPSLDRRR SNGEIRNLAS ISSSLLPALG TTPDEGYFNL KKYIIAPYDR RYRLWQTFLV
ALVVYSAWSS PFELAFREMS IEPLLITDLF VDAFFAFDII LTFFVAYLDT STYFLVDDHK
KIAIRYVKHL HFPMDLASTL PFQQIYQVIA GTPHGRAGVF GFLNMLRLWR LRRVSELFSR
LEKDIRVSYS LTRASKLLCV TLFAVHFTGC MYFWLAFHHK SPENTWIGKQ VEDFKHGSVR
SGYTYSMYWS IVTLSTVGYG DLHAENTTEK RDAFNKILQY ASKNRLPEGL KEQMLAHTQL
KFKTAELQQE EVLQDLPKAI RAGIAQHLFH NVVEKTYLFK GLSDDFISQL VSDMKAEYYP
SKVDIILQNE MPAYFYILVS GSVDVLTYKN GSEQFLFKLE SGSMAGEIGV MFNIPQPYTV
RSRRLSQVIR INHHHFKQMV KPFSKDGKAI ISNFTQFLKG LGGGVLEEIP HVAEFLSDLP
DKRPTQNDST CDEDDQYKGQ TENSSPLSNL DPIRVKIHGH QPNEKIKNGT TPKLIILPDS
VEDLFRVAEK KFGKRGSKIV MADGSEVEDL SALRDNDELY IL
//
