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Database: UniProt
Entry: G3NS27_GASAC
LinkDB: G3NS27_GASAC
Original site: G3NS27_GASAC 
ID   G3NS27_GASAC            Unreviewed;       919 AA.
AC   G3NS27;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Potassium voltage-gated channel, subfamily H (eag-related), member 4b {ECO:0000313|Ensembl:ENSGACP00000008144.1};
GN   Name=KCNH4 {ECO:0000313|Ensembl:ENSGACP00000008144.1};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000008144.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000008144.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000008144.1}
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   AlphaFoldDB; G3NS27; -.
DR   STRING; 69293.ENSGACP00000008144; -.
DR   Ensembl; ENSGACT00000008163.1; ENSGACP00000008144.1; ENSGACG00000006152.1.
DR   eggNOG; KOG0498; Eukaryota.
DR   GeneTree; ENSGT00940000156363; -.
DR   InParanoid; G3NS27; -.
DR   OMA; KSQPTLC; -.
DR   TreeFam; TF313130; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
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   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:UP000007635};
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        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        314..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        358..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        424..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        453..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          14..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          555..655
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          139..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          678..731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          772..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..692
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..731
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        776..790
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   919 AA;  103280 MW;  AD6B9B3363E41195 CRC64;
     MPVMKGLLAP QNTFLDTIAT RFDGTHSNFL LGNAQGHRGY PIVYCSDAFC ELTGFTRTEV
     MQKNCSCRFL YGADTSEHVA HQMEKALEGR EEYQAEVHFY KKNGVAFWCF LDIVPIKNEK
     GEMVLFLFSF KDITDTYGRG HHNSKKEAGP EDKRRRRKSS PHFVEARRRG RTMLYQLTSQ
     FSRGGKRGLK AIQNVSKSMI AKPSIPEYKV AAVQKSRFIL LHYSISKALW DWLILLATFY
     VAVTVPYNVS FTPYDDTVTA ARSTIVSDIV VEMLFITDII LNFRTTYVSQ SGQVVYEARS
     ICIHYATTWF FVDLVAALPF DLLYAFNITV TSLVHLLKTV RLLRLLRLLQ KLDRYSQYSA
     MVLTLLMSVF ALLAHWMACI WYMIGRKEIA TNDTWDIGWL HELGKRLETP YTNSTAGGPT
     VRSAYIAALY FTLSSLTSVG FGNVCANTDA EKIFSICTML IGALMHALVF GNVTAIIQRM
     YSRRSLYHTR MTDLKDFIRV HRLPEQIKQR MLEYFQTTWS VNNGIDANEL LHDFPDELRA
     DIAMHLNKDI LQLPVFKGAS RGCLRSLSLH IKTSFCVPGE YLIRQGDALH ANYFVCSGSL
     EVLKDSMVLA ILGKGDLIGS DLPGTDQVIK TNADVKALTY CDLQYINVRG LREVLELYPE
     YASVFTSDIH NNLTYNLREG SQDESPQGLS RFSRSPRLPH PEAISKSVET RLPSIVETKG
     DDPDDSFHLS PAARSRRNLL LPNFSSPVRR TSLGNLLGDE LRQFNALRRC RSPNLSRGVH
     GQSSSPQPPS KKEHGPLKAA AASTLAQGGS EAEKKPSKLL IPTVTCFGPP DLSPRVVDGI
     EDNGHAFHFN VEHSRPDASA GGSTQDSTQA NANATMLHET QEVKQIISQL NQKMSTLNQA
     VSNLTKDLHH MMHLLQAHM
//
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