ID H2LIZ2_ORYLA Unreviewed; 1035 AA.
AC H2LIZ2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Potassium voltage-gated channel subfamily H member 8 {ECO:0000313|Ensembl:ENSORLP00000005975.2};
GN Name=KCNH8 {ECO:0000313|Ensembl:ENSORLP00000005975.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000005975.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000005975.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000005975.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000005975.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000005975.2};
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_011479155.1; XM_011480853.1.
DR AlphaFoldDB; H2LIZ2; -.
DR STRING; 8090.ENSORLP00000005975; -.
DR Ensembl; ENSORLT00000005976.2; ENSORLP00000005975.2; ENSORLG00000004750.2.
DR GeneID; 101170602; -.
DR KEGG; ola:101170602; -.
DR CTD; 131096; -.
DR eggNOG; KOG0498; Eukaryota.
DR GeneTree; ENSGT00940000156869; -.
DR HOGENOM; CLU_005746_2_3_1; -.
DR InParanoid; H2LIZ2; -.
DR OrthoDB; 66005at2759; -.
DR TreeFam; TF313130; -.
DR Proteomes; UP000001038; Chromosome 11.
DR Bgee; ENSORLG00000004750; Expressed in brain.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
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:SF380; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY H MEMBER 8; 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 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:UP000001038};
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 223..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 421..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 451..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..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 553..670
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 711..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1026
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1035 AA; 115469 MW; 07AEC819E5F55650 CRC64;
MPVMKGLLAP QNTFLDTIAT RFDGTHSNFI LANAQVSKGF PIVYCSDGFC ELTGFSRAEV
MQKSCACKFL YGPETSESII LSIDEALEER KEFKDEIMFY SKTAVLFWCL LDIVPIKNEK
GDVVLFLASF KDITDTKAKA IHEDRREERR RGRVKTGSPF STARLRSGTV LYHISGHLHS
REKSKIKLNK NVFGDPPALP EYKVADAKKS KFILLHYSTF KAGWDWLILL ATFYVAVTVP
YNVCFIGDDD DLTRSTTVSD IAVEILFIID IIFNFRTTYV SKSGQVIFDA RQICIHYLTT
WFIIDLVAAL PFDLLYAVRV SVVSVVHLLK TVRLLRLLRL LQKMDRYSQH STVVLTLLMS
MFALLAHWMA CIWYIIGKME IEANSYNWDI GWLHELGKRL ESPYHAMAEV NGTTSGPSIR
SVYIASLYFT LSSLTSVGFG NVSANTDAEK IFSICVMLIG ALMHALVFGN VTAIIQRMYS
RWSQYHTRTK DLKDFIRIHH LPQSLKQRML EYFQTTWSVN NGIDCNELLK DFPDELRSDI
TMHLNKEILE LSLFASASRG CLRSLSLHIK TSFCAPGEYL LRQGDALQAI FFVCSGSMEV
LKDDMVLAIL GKGDLIGANL SLDNRVIKTN ADVKALTYCD LQCINLKGLY EVLDLYPEYS
HHFVQDIQQD LTYNLREGHE TQVKVRLPTT TTTPETQLRV SKNGRAVQGH ITETQDEEDA
DMEERHQTGA ASPRYTGEKS PLTSSSQTTM AQILSKSQKK IQESTFTTLD PCNLSPRIVD
GTEDSEDKES FHTFSFSTSR GCPVNTPTRA TADTLHISTV ELAAKAEETR GQLHNLDQQV
GTLRKEVADL GQVMKRMAQL METLIPSVQP PTIVCPAHYS PAHHMCLRPA TPTRSCPSPS
PSKTASIWTE APMPLTSPSL AAAQQHSVMC HTDFLIHRPQ SLQAACPAMP SSASPLTPDS
YQLQPASVIS ELPMPSSSCS LHDIPCCEVQ APTPIMSSVD SSPPQDGGQR GLYHSSGSSP
QTGLGLVHRC PNQGL
//
