ID I3IXS4_ORENI Unreviewed; 1186 AA.
AC I3IXS4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Potassium voltage-gated channel subfamily H member 4 {ECO:0000313|Ensembl:ENSONIP00000001414.2};
GN Name=kcnh4 {ECO:0000313|Ensembl:ENSONIP00000001414.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000001414.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000001414.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC heterotetrameric complex of pore-forming alpha subunits that can
CC associate with modulating beta subunits.
CC {ECO:0000256|ARBA:ARBA00011552}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR RefSeq; XP_005468906.1; XM_005468849.3.
DR AlphaFoldDB; I3IXS4; -.
DR STRING; 8128.ENSONIP00000001414; -.
DR Ensembl; ENSONIT00000001413.2; ENSONIP00000001414.2; ENSONIG00000001117.2.
DR GeneID; 100703420; -.
DR KEGG; onl:100703420; -.
DR CTD; 100148126; -.
DR eggNOG; KOG0498; Eukaryota.
DR GeneTree; ENSGT00940000156363; -.
DR HOGENOM; CLU_005746_6_0_1; -.
DR InParanoid; I3IXS4; -.
DR OMA; VDHKLPY; -.
DR OrthoDB; 66005at2759; -.
DR TreeFam; TF313130; -.
DR Proteomes; UP000005207; Linkage group LG4.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.1200.260; -; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 3.30.450.20; PAS domain; 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; IPR003950; K_chnl_volt-dep_ELK.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR10217:SF630; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY H MEMBER 4; 1.
DR PANTHER; PTHR10217; VOLTAGE AND LIGAND GATED POTASSIUM CHANNEL; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR PRINTS; PR01465; ELKCHANNEL.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00086; PAC; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT TRANSMEM 219..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 454..478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..90
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 93..145
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 556..657
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 1070..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 855..882
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1186 AA; 132959 MW; 6E9914D8EF57F86D CRC64;
MPVMKGLLAP QNTFLDTIAN HFDGTHCNFL LGNTQGSCGY PIVYCSDGFC ELTGFVRTEV
MQKTCTCRFL HGAETSENVI QQVDKALEGQ QEYQGEVCFY RKNGNPFRCL LDIVPIKNEK
GEVVLFLLSF KDVSESHGKK HRCTQRDGML ETAHQSRKSG QSHFFQSRKR GRTILHHLNR
LFTKRNKKKL PNSVFQKPSL PEYKVAAVKR SRFILLHYSM FKALWDWLIL LATFYVALTV
PYNVCFVSHD ESGDHRPLVS RSTIGSDIAV EMLFILDILL NFRTTFVSQS GQVVYDTRSI
CLHYCTTWFF VDLIAALPFD LLYAFNITVT SLVHLLKTVR LLRLLRLLQK LDRYSQYSAV
VLTLLMSVFA LLAHWMACVW YIIGRKEIES GDPVTWDIGW LQELGKRLET PYINSTMGGP
SLPSAYIASL YFTLSSLTSV GFGNVCANTD AEKIFSICIM LMGALMHAVV FGNVTAIIQR
MYSRRSLYHT RMKDLKDFIR VHRLPQQLKQ RMLEYFQATW SVNNGINTNE LLHDFPDELR
ADITMHLNKD ILQLPVFERA SRGCLRSLSL HIKTSFCAPG EYLIRQGDAL QANYFVCSGS
LEVLKDGMVL AILGKGDLIG ADLPEHDKVI KTNADVKALT YCDLQYISVR ALREVLGLYP
EYSSRFSLDI HHNLTYNLRE GSEADGVTRF QLTPRQSQFM DHKLPYIIQG ADAKHTDNVN
YSQHRRLPLL QSMGSPVHQP CLSTLLGEEL RHISALQLCR LPAQGSRGCS PSPQPFFSEE
LSPSPLPSLT SDLDLNHRPA KLMPSGSCIS PLNLSPRVVD GIEDNDHTFQ FNMEQSEAKT
NVADRLHVCN LLLETEEMRQ SVSKLSKEVI NLNQDVSNLA KELHDIMHFL HSHMTMLHNN
SPASTCSCGT QVLPNPSVTT CSHWQPDVPL NISTGLPTVH EMISHPARNT WHSSGIPSQC
TSSALLYSSS TMPSCSHLGC SDRDTTQRLQ CFSSPFQTPR TSPGSPYMTF SHAHGGPSLL
GISSAFSGYP LSCQASHMVS SAQIHTISST HSLCSTVNCG YSQPPLSVQT NSDSLHNQTK
SQTPIHLSTT PSAQPQYHTA FSSLTPSRAH TLIYTGYEDQ RGTVEGSRQN DPVGSSPVHQ
TQDLASSLME QVPNMDCKAS LYKERTETME SHSTGDSILD MKERPH
//
