ID Q9FS92_SAMSA Unreviewed; 841 AA.
AC Q9FS92;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Potassium channel {ECO:0000256|RuleBase:RU369015};
GN Name=spork1 {ECO:0000313|EMBL:CAC10514.1};
OS Samanea saman (Rain tree) (Mimosa saman).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Caesalpinioideae; mimosoid clade;
OC Ingeae; Samanea.
OX NCBI_TaxID=76910 {ECO:0000313|EMBL:CAC10514.1};
RN [1] {ECO:0000313|EMBL:CAC10514.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pulvinus {ECO:0000313|EMBL:CAC10514.1};
RA Becker D., Moshelion M., Moran N., Hedrich R.;
RT "Molecular characterisation of an outwardly rectifying potassium channel
RT from Samanea saman pulvini.";
RL Submitted (SEP-2000) 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}.
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DR EMBL; AJ299019; CAC10514.1; -; mRNA.
DR AlphaFoldDB; Q9FS92; -.
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; 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:SF3; POTASSIUM CHANNEL SKOR; 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; PR01415; ANKYRIN.
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; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51490; KHA; 1.
PE 2: Evidence at transcript level;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
KW Ion channel {ECO:0000256|RuleBase:RU369015, ECO:0000313|EMBL:CAC10514.1};
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 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 102..121
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 133..151
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 232..254
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 286..305
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 317..342
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT DOMAIN 417..520
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REPEAT 593..625
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 626..658
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 770..841
FT /note="KHA"
FT /evidence="ECO:0000259|PROSITE:PS51490"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 841 AA; 96383 MW; 190D642897579DA7 CRC64;
MAGDRVTEEA VRDEREEKRK RMFSSSRSSS SSSSDNREYE VQDLRDRLKS SRGSRFRLIE
DELKELNQRK LSRYVLDGIR GFSKDFIIHP EKNRWYQAWT KFILLWAIYS SFFTPMEFGF
FRGLDKDLFI LDIIGQVAFL VDIVVQFCLA YRDSQTYRMI YKPSSIALRY LKSSFIFDLL
GCMPWDIIYK ASGRKEGVRY LLLIRLYRVR KVIEFFQRME KDIRINYMFT RIVKLLVVEL
YCTHTAACIF YYLATTLPAS QEGYTWIGSL KLGDYSYMNF RDIDLWKRYT TSLYFAIVTM
ATVGYGDIHA VNMREMIFIM IYVSFDMVLG AYLIGNMTAL IVKGSKTEKF RDRMTDLLKY
MNRNRLGRDI REQLKSHMRL QYESSYTEPA AIQDLPISVR SKISQELYLP CIEKVPLFKG
CSLEFINQIV IRPHEEFSLP GEVILEQGNV VDQLYSVCHG VLEEVGPSEN GSEETVSLLE
PNSSFAHISI LCNIPQPYTV RVCELCRLLR LDKQSFTDIL DIYFFDGRKV LNNLLEGKDS
SRGKQLESEI TFHIGKQEAE LALKVNNAAL NGDLNHLKGF IRAGADPNKT DYDGRSPLHL
AASRGYEEIT LFLIQEGVEI DKRDNFGNTP LLEAVKNGHD QVASLLVGQG ASMDIEDAGS
VLCNAIVKGD SDYLKRLLAK GRDPNRKDRI TEVLFMWLVE SEGLFLMAKL LVEAGASVFI
QDRWGNTPLD EAKMCGNNNI IKLLEDIRST QLSKFPHLSS ELTGKFHSKK GTIFPFHPWD
PKEHRRYGIV LWVPHTIEEL IKTAAEQLGV SSDCSIILSE DAGKITNTNL IMDGAKAVSS
P
//
