KCNK4_HUMAN
ID KCNK4_HUMAN Reviewed; 393 AA.
AC Q9NYG8; B5TJL1; Q96T94;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Potassium channel subfamily K member 4;
DE AltName: Full=TWIK-related arachidonic acid-stimulated potassium channel protein {ECO:0000303|PubMed:23341632};
DE Short=TRAAK {ECO:0000303|PubMed:23341632};
DE AltName: Full=Two pore potassium channel KT4.1;
DE Short=Two pore K(+) channel KT4.1;
GN Name=KCNK4; Synonyms=TRAAK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11042359; DOI=10.1016/s0169-328x(00)00183-2;
RA Chapman C.G., Meadows H.J., Godden R.J., Campbell D.A., Duckworth M.,
RA Kelsell R.E., Murdock P.R., Randall A.D., Rennie G.I., Gloger I.S.;
RT "Cloning, localisation and functional expression of a novel human,
RT cerebellum specific, two pore domain potassium channel.";
RL Brain Res. Mol. Brain Res. 82:74-83(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LEU-328.
RC TISSUE=Frontal cortex;
RA Gray A.T.;
RT "Assignment of KCNK4 encoding the human potassium channel TRAAK to
RT chromosome 11.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10767409; DOI=10.1016/s0014-5793(00)01388-0;
RA Lesage F., Maingret F., Lazdunski M.;
RT "Cloning and expression of human TRAAK, a polyunsaturated fatty acids-
RT activated and mechano-sensitive K(+) channel.";
RL FEBS Lett. 471:137-140(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=12191490; DOI=10.1016/s0169-328x(02)00157-2;
RA Ozaita A., Vega-Saenz de Miera E.;
RT "Cloning of two transcripts, HKT4.1a and HKT4.1b, from the human two-pore
RT K+ channel gene KCNK4. Chromosomal localization, tissue distribution and
RT functional expression.";
RL Brain Res. Mol. Brain Res. 102:18-27(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [8]
RP FUNCTION, ACTIVITY REGULATION, INVOLVEMENT IN FHEIG, VARIANTS FHEIG GLU-172
RP AND PRO-244, AND CHARACTERIZATION OF VARIANTS FHEIG GLU-172 AND PRO-244.
RX PubMed=30290154; DOI=10.1016/j.ajhg.2018.09.001;
RA Bauer C.K., Calligari P., Radio F.C., Caputo V., Dentici M.L., Falah N.,
RA High F., Pantaleoni F., Barresi S., Ciolfi A., Pizzi S., Bruselles A.,
RA Person R., Richards S., Cho M.T., Claps Sepulveda D.J., Pro S., Battini R.,
RA Zampino G., Digilio M.C., Bocchinfuso G., Dallapiccola B., Stella L.,
RA Tartaglia M.;
RT "Mutations in KCNK4 that affect gating cause a recognizable
RT neurodevelopmental syndrome.";
RL Am. J. Hum. Genet. 103:621-630(2018).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.31 ANGSTROMS) OF 1-274, FUNCTION, ACTIVITY
RP REGULATION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION, AND
RP DISULFIDE BOND.
RX PubMed=22282805; DOI=10.1126/science.1213808;
RA Brohawn S.G., del Marmol J., MacKinnon R.;
RT "Crystal structure of the human K2P TRAAK, a lipid- and mechano-sensitive
RT K+ ion channel.";
RL Science 335:436-441(2012).
RN [10] {ECO:0007744|PDB:4I9W}
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-274, SUBCELLULAR LOCATION,
RP SUBUNIT, TOPOLOGY, AND DISULFIDE BOND.
RX PubMed=23341632; DOI=10.1073/pnas.1218950110;
RA Brohawn S.G., Campbell E.B., MacKinnon R.;
RT "Domain-swapped chain connectivity and gated membrane access in a Fab-
RT mediated crystal of the human TRAAK K+ channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:2129-2134(2013).
RN [11] {ECO:0007744|PDB:4WFE}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-264, FUNCTION, SUBCELLULAR
RP LOCATION, SUBUNIT, TOPOLOGY, DISULFIDE BOND, AND DOMAIN.
RX PubMed=25471887; DOI=10.1038/nature14013;
RA Brohawn S.G., Campbell E.B., MacKinnon R.;
RT "Physical mechanism for gating and mechanosensitivity of the human TRAAK K+
RT channel.";
RL Nature 516:126-130(2014).
RN [12] {ECO:0007744|PDB:4RUE, ECO:0007744|PDB:4RUF}
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-274 OF MUTANTS ILE-98 AND
RP SER-236, FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, SUBUNIT,
RP TOPOLOGY, DISULFIDE BOND, DOMAIN, AND MUTAGENESIS OF GLY-98 AND TRP-236.
RX PubMed=25500157; DOI=10.1016/j.neuron.2014.11.017;
RA Lolicato M., Riegelhaupt P.M., Arrigoni C., Clark K.A., Minor D.L. Jr.;
RT "Transmembrane helix straightening and buckling underlies activation of
RT mechanosensitive and thermosensitive K(2P) channels.";
RL Neuron 84:1198-1212(2014).
CC -!- FUNCTION: Voltage-insensitive potassium channel (PubMed:22282805).
CC Channel opening is triggered by mechanical forces that deform the
CC membrane (PubMed:22282805, PubMed:25471887, PubMed:25500157,
CC PubMed:30290154). Channel opening is triggered by raising the
CC intracellular pH to basic levels (By similarity). The channel is
CC inactive at 24 degrees Celsius (in vitro); raising the temperature to
CC 37 degrees Celsius increases the frequency of channel opening, with a
CC further increase in channel activity when the temperature is raised to
CC 42 degrees Celsius (By similarity). Plays a role in the perception of
CC pain caused by heat (By similarity). Plays a role in the sensory
CC perception of pain caused by pressure (By similarity).
CC {ECO:0000250|UniProtKB:G3V8V5, ECO:0000250|UniProtKB:O88454,
CC ECO:0000269|PubMed:22282805, ECO:0000269|PubMed:25471887,
CC ECO:0000269|PubMed:25500157, ECO:0000269|PubMed:30290154}.
CC -!- ACTIVITY REGULATION: Activated by arachidonic acid.
CC {ECO:0000269|PubMed:22282805, ECO:0000269|PubMed:25500157,
CC ECO:0000269|PubMed:30290154}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:22282805,
CC ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
CC ECO:0000269|PubMed:25500157}.
CC -!- INTERACTION:
CC Q9NYG8-2; Q9NYG8-2: KCNK4; NbExp=2; IntAct=EBI-15965944, EBI-15965944;
CC Q9NYG8-2; Q9P0S3: ORMDL1; NbExp=3; IntAct=EBI-15965944, EBI-1054848;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22282805,
CC ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
CC ECO:0000269|PubMed:25500157}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22282805, ECO:0000269|PubMed:23341632,
CC ECO:0000269|PubMed:25471887, ECO:0000269|PubMed:25500157}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=KT4.1a;
CC IsoId=Q9NYG8-1; Sequence=Displayed;
CC Name=2; Synonyms=KT4.1b;
CC IsoId=Q9NYG8-2; Sequence=VSP_006689;
CC -!- DOMAIN: Channel opening is brought about by a conformation change that
CC involves buckling of the second transmembrane helix and affects the
CC position and orientation of the fourth transmembrane helix.
CC {ECO:0000269|PubMed:25471887, ECO:0000269|PubMed:25500157}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:22282805}.
CC -!- DISEASE: Facial dysmorphism, hypertrichosis, epilepsy, intellectual and
CC developmental delay, and gingival overgrowth syndrome (FHEIG)
CC [MIM:618381]: An autosomal dominant syndrome characterized by delayed
CC motor and intellectual development, poor speech, seizures, generalized
CC hypertrichosis and facial dysmorphic features, including hypotonic
CC facies, bitemporal narrowing, micrognathia, deep-set eyes, bushy
CC eyebrows and long eyelashes, low-set ears, short deep philtrum,
CC gingival overgrowth, prominent upper and lower vermilion, and everted
CC upper lip. {ECO:0000269|PubMed:30290154}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000305}.
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DR EMBL; AF248242; AAG31731.1; -; mRNA.
DR EMBL; AF247042; AAF64062.1; -; mRNA.
DR EMBL; AF259500; AAK49389.1; -; mRNA.
DR EMBL; AF259501; AAK49390.1; -; mRNA.
DR EMBL; EU978935; ACH86094.1; -; mRNA.
DR EMBL; CH471076; EAW74242.1; -; Genomic_DNA.
DR CCDS; CCDS8067.1; -. [Q9NYG8-1]
DR RefSeq; NP_001304019.1; NM_001317090.1. [Q9NYG8-1]
DR RefSeq; NP_201567.1; NM_033310.2. [Q9NYG8-1]
DR PDB; 3UM7; X-ray; 3.31 A; A/B=1-274.
DR PDB; 4I9W; X-ray; 2.75 A; A/B=1-274.
DR PDB; 4RUE; X-ray; 3.30 A; A/B=1-274.
DR PDB; 4RUF; X-ray; 3.40 A; A/B=1-274.
DR PDB; 4WFE; X-ray; 2.50 A; A/B=1-264.
DR PDB; 4WFF; X-ray; 2.50 A; A/B=1-264.
DR PDB; 4WFG; X-ray; 3.00 A; A/B=1-264.
DR PDB; 4WFH; X-ray; 3.01 A; A/B=1-264.
DR PDB; 7LJ4; X-ray; 2.78 A; A/B=1-264.
DR PDB; 7LJ5; X-ray; 2.26 A; A/B=1-264.
DR PDB; 7LJA; X-ray; 2.77 A; A/B=1-264.
DR PDB; 7LJB; X-ray; 2.97 A; A/B=1-264.
DR PDBsum; 3UM7; -.
DR PDBsum; 4I9W; -.
DR PDBsum; 4RUE; -.
DR PDBsum; 4RUF; -.
DR PDBsum; 4WFE; -.
DR PDBsum; 4WFF; -.
DR PDBsum; 4WFG; -.
DR PDBsum; 4WFH; -.
DR PDBsum; 7LJ4; -.
DR PDBsum; 7LJ5; -.
DR PDBsum; 7LJA; -.
DR PDBsum; 7LJB; -.
DR AlphaFoldDB; Q9NYG8; -.
DR SMR; Q9NYG8; -.
DR BioGRID; 119122; 10.
DR DIP; DIP-61343N; -.
DR IntAct; Q9NYG8; 4.
DR STRING; 9606.ENSP00000444948; -.
DR BindingDB; Q9NYG8; -.
DR ChEMBL; CHEMBL3714486; -.
DR GlyGen; Q9NYG8; 2 sites.
DR iPTMnet; Q9NYG8; -.
DR PhosphoSitePlus; Q9NYG8; -.
DR BioMuta; KCNK4; -.
DR DMDM; 13124080; -.
DR MassIVE; Q9NYG8; -.
DR PaxDb; Q9NYG8; -.
DR PeptideAtlas; Q9NYG8; -.
DR PRIDE; Q9NYG8; -.
DR ABCD; Q9NYG8; 1 sequenced antibody.
DR Antibodypedia; 29251; 132 antibodies from 27 providers.
DR DNASU; 50801; -.
DR Ensembl; ENST00000394525.6; ENSP00000378033.2; ENSG00000182450.13. [Q9NYG8-1]
DR Ensembl; ENST00000422670.7; ENSP00000402797.2; ENSG00000182450.13. [Q9NYG8-1]
DR Ensembl; ENST00000539216.1; ENSP00000444948.1; ENSG00000182450.13. [Q9NYG8-1]
DR GeneID; 50801; -.
DR KEGG; hsa:50801; -.
DR MANE-Select; ENST00000422670.7; ENSP00000402797.2; NM_033310.3; NP_201567.1.
DR UCSC; uc001nzj.2; human. [Q9NYG8-1]
DR CTD; 50801; -.
DR DisGeNET; 50801; -.
DR GeneCards; KCNK4; -.
DR HGNC; HGNC:6279; KCNK4.
DR HPA; ENSG00000182450; Tissue enriched (brain).
DR MalaCards; KCNK4; -.
DR MIM; 605720; gene.
DR MIM; 618381; phenotype.
DR neXtProt; NX_Q9NYG8; -.
DR OpenTargets; ENSG00000182450; -.
DR PharmGKB; PA30061; -.
DR VEuPathDB; HostDB:ENSG00000182450; -.
DR eggNOG; KOG1418; Eukaryota.
DR GeneTree; ENSGT00940000160310; -.
DR HOGENOM; CLU_022504_1_1_1; -.
DR InParanoid; Q9NYG8; -.
DR OMA; ISNHSAW; -.
DR PhylomeDB; Q9NYG8; -.
DR TreeFam; TF313947; -.
DR PathwayCommons; Q9NYG8; -.
DR Reactome; R-HSA-1299503; TWIK related potassium channel (TREK).
DR Reactome; R-HSA-5576886; Phase 4 - resting membrane potential.
DR SignaLink; Q9NYG8; -.
DR BioGRID-ORCS; 50801; 46 hits in 1065 CRISPR screens.
DR GeneWiki; KCNK4; -.
DR GenomeRNAi; 50801; -.
DR Pharos; Q9NYG8; Tbio.
DR PRO; PR:Q9NYG8; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9NYG8; protein.
DR Bgee; ENSG00000182450; Expressed in nucleus accumbens and 49 other tissues.
DR ExpressionAtlas; Q9NYG8; baseline and differential.
DR Genevisible; Q9NYG8; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0034705; C:potassium channel complex; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0098782; F:mechanosensitived potassium channel activity; IDA:UniProtKB.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0005267; F:potassium channel activity; IDA:UniProtKB.
DR GO; GO:0022841; F:potassium ion leak channel activity; IBA:GO_Central.
DR GO; GO:0097604; F:temperature-gated cation channel activity; ISS:UniProtKB.
DR GO; GO:0071469; P:cellular response to alkaline pH; ISS:UniProtKB.
DR GO; GO:0071398; P:cellular response to fatty acid; IDA:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:UniProtKB.
DR GO; GO:0071502; P:cellular response to temperature stimulus; ISS:UniProtKB.
DR GO; GO:0050976; P:detection of mechanical stimulus involved in sensory perception of touch; ISS:UniProtKB.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; TAS:ProtInc.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
DR GO; GO:0050951; P:sensory perception of temperature stimulus; ISS:UniProtKB.
DR GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR008074; 2pore_dom_K_chnl_TRAAK.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11003; PTHR11003; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01691; TRAAKCHANNEL.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disease variant;
KW Disulfide bond; Epilepsy; Glycoprotein; Intellectual disability;
KW Ion channel; Ion transport; Membrane; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..393
FT /note="Potassium channel subfamily K member 4"
FT /id="PRO_0000101747"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22282805,
FT ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
FT ECO:0000269|PubMed:25500157"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:22282805,
FT ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
FT ECO:0000269|PubMed:25500157"
FT TOPO_DOM 25..87
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22282805,
FT ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
FT ECO:0000269|PubMed:25500157"
FT INTRAMEM 88..102
FT /note="Helical; Name=Pore helix 1"
FT /evidence="ECO:0000269|PubMed:22282805,
FT ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
FT ECO:0000269|PubMed:25500157"
FT INTRAMEM 103..109
FT /evidence="ECO:0000269|PubMed:22282805,
FT ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
FT ECO:0000269|PubMed:25500157"
FT TOPO_DOM 110..117
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22282805,
FT ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
FT ECO:0000269|PubMed:25500157"
FT TRANSMEM 118..150
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:22282805,
FT ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
FT ECO:0000269|PubMed:25500157"
FT TOPO_DOM 151..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22282805,
FT ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
FT ECO:0000269|PubMed:25500157"
FT TRANSMEM 173..194
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:22282805,
FT ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
FT ECO:0000269|PubMed:25500157"
FT TOPO_DOM 195..199
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22282805,
FT ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
FT ECO:0000269|PubMed:25500157"
FT INTRAMEM 200..213
FT /note="Helical; Name=Pore helix 2"
FT /evidence="ECO:0000269|PubMed:22282805,
FT ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
FT ECO:0000269|PubMed:25500157"
FT INTRAMEM 214..219
FT /evidence="ECO:0000269|PubMed:22282805,
FT ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
FT ECO:0000269|PubMed:25500157"
FT TOPO_DOM 220..233
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22282805,
FT ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
FT ECO:0000269|PubMed:25500157"
FT TRANSMEM 234..260
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:22282805,
FT ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
FT ECO:0000269|PubMed:25500157"
FT TOPO_DOM 261..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22282805,
FT ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
FT ECO:0000269|PubMed:25500157"
FT REGION 103..108
FT /note="Selectivity filter 1"
FT /evidence="ECO:0000269|PubMed:22282805,
FT ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
FT ECO:0000269|PubMed:25500157"
FT REGION 212..217
FT /note="Selectivity filter 2"
FT /evidence="ECO:0000269|PubMed:22282805,
FT ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
FT ECO:0000269|PubMed:25500157"
FT REGION 285..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..335
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:22282805,
FT ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
FT ECO:0000269|PubMed:25500157"
FT VAR_SEQ 1
FT /note="M -> MTTAPQEPPARPLQAGSGAGPAPGRAM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12191490"
FT /id="VSP_006689"
FT VARIANT 172
FT /note="A -> E (in FHEIG; gain-of-function variant resulting
FT in highly increased basal potassium currents; impaired
FT sensitivity to arachidonic acid)"
FT /evidence="ECO:0000269|PubMed:30290154"
FT /id="VAR_082119"
FT VARIANT 244
FT /note="A -> P (in FHEIG; gain-of-function variant resulting
FT in highly increased basal potassium currents; impaired
FT sensitivity to arachidonic acid)"
FT /evidence="ECO:0000269|PubMed:30290154"
FT /id="VAR_082120"
FT VARIANT 328
FT /note="P -> L (in dbSNP:rs953778)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_020206"
FT MUTAGEN 98
FT /note="G->I: Strongly increases basal level of channel
FT activity, decreases further activation by pressure and
FT abolishes further activation by arachidonic acid."
FT /evidence="ECO:0000269|PubMed:25500157"
FT MUTAGEN 236
FT /note="W->S: Increases basal level of channel activity and
FT decreases further activation by pressure, but has little
FT effect on further activation by arachidonic acid."
FT /evidence="ECO:0000269|PubMed:25500157"
FT HELIX 3..28
FT /evidence="ECO:0007829|PDB:7LJ5"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:7LJ5"
FT HELIX 34..49
FT /evidence="ECO:0007829|PDB:7LJ5"
FT HELIX 55..70
FT /evidence="ECO:0007829|PDB:7LJ5"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:4WFE"
FT HELIX 90..101
FT /evidence="ECO:0007829|PDB:7LJ5"
FT HELIX 114..158
FT /evidence="ECO:0007829|PDB:7LJ5"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:7LJ5"
FT HELIX 164..183
FT /evidence="ECO:0007829|PDB:7LJ5"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:7LJ5"
FT HELIX 199..210
FT /evidence="ECO:0007829|PDB:7LJ5"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:7LJ5"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:4WFE"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:7LJ5"
FT HELIX 231..259
FT /evidence="ECO:0007829|PDB:7LJ5"
SQ SEQUENCE 393 AA; 42704 MW; 7F18E53A0A9AD57D CRC64;
MRSTTLLALL ALVLLYLVSG ALVFRALEQP HEQQAQRELG EVREKFLRAH PCVSDQELGL
LIKEVADALG GGADPETNST SNSSHSAWDL GSAFFFSGTI ITTIGYGNVA LRTDAGRLFC
IFYALVGIPL FGILLAGVGD RLGSSLRHGI GHIEAIFLKW HVPPELVRVL SAMLFLLIGC
LLFVLTPTFV FCYMEDWSKL EAIYFVIVTL TTVGFGDYVA GADPRQDSPA YQPLVWFWIL
LGLAYFASVL TTIGNWLRVV SRRTRAEMGG LTAQAASWTG TVTARVTQRA GPAAPPPEKE
QPLLPPPPCP AQPLGRPRSP SPPEKAQPPS PPTASALDYP SENLAFIDES SDTQSERGCP
LPRAPRGRRR PNPPRKPVRP RGPGRPRDKG VPV
