ID KCNG2_HUMAN Reviewed; 466 AA. AC Q9UJ96; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 170. DE RecName: Full=Potassium voltage-gated channel subfamily G member 2; DE AltName: Full=Cardiac potassium channel subunit; DE AltName: Full=Voltage-gated potassium channel subunit Kv6.2; GN Name=KCNG2; Synonyms=KCNF2; 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], AND CHARACTERIZATION. RX PubMed=10551266; RA Zhu X.-R., Netzer R., Boehlke K., Liu Q., Pongs O.; RT "Structural and functional characterization of Kv6.2, a new gamma-subunit RT of voltage-gated potassium channel."; RL Recept. Channels 6:337-350(1999). CC -!- FUNCTION: Potassium channel subunit. Modulates channel activity by CC shifting the threshold and the half-maximal activation to more negative CC values. CC -!- SUBUNIT: Heterodimer with KCNB1. Does not form homomultimers. CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Highly expressed in heart, liver, skeletal muscle, CC kidney and pancreas. Detected at low levels in brain, lung and CC placenta. CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is CC characterized by a series of positively charged amino acids at every CC third position. CC -!- MISCELLANEOUS: Heterodimers with KCNB1 are highly sensitive to CC inhibition by tetraethylammonium (TEA) and propafenone. CC -!- SIMILARITY: Belongs to the potassium channel family. G (TC 1.A.1.2) CC subfamily. Kv6.2/KCNG2 sub-subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ011021; CAB56834.1; -; mRNA. DR CCDS; CCDS12019.1; -. DR RefSeq; NP_036415.1; NM_012283.1. DR RefSeq; XP_011524220.1; XM_011525918.2. DR RefSeq; XP_011524222.1; XM_011525920.2. DR RefSeq; XP_016881194.1; XM_017025705.1. DR AlphaFoldDB; Q9UJ96; -. DR SMR; Q9UJ96; -. DR BioGRID; 117638; 2. DR STRING; 9606.ENSP00000315654; -. DR ChEMBL; CHEMBL2362996; -. DR DrugBank; DB00228; Enflurane. DR DrugBank; DB01110; Miconazole. DR DrugBank; DB01069; Promethazine. DR DrugCentral; Q9UJ96; -. DR iPTMnet; Q9UJ96; -. DR PhosphoSitePlus; Q9UJ96; -. DR BioMuta; KCNG2; -. DR DMDM; 24418480; -. DR MassIVE; Q9UJ96; -. DR PaxDb; 9606-ENSP00000315654; -. DR PeptideAtlas; Q9UJ96; -. DR Antibodypedia; 59003; 168 antibodies from 21 providers. DR DNASU; 26251; -. DR Ensembl; ENST00000316249.4; ENSP00000315654.3; ENSG00000178342.5. DR GeneID; 26251; -. DR KEGG; hsa:26251; -. DR MANE-Select; ENST00000316249.4; ENSP00000315654.3; NM_012283.2; NP_036415.1. DR UCSC; uc010xfl.2; human. DR AGR; HGNC:6249; -. DR CTD; 26251; -. DR DisGeNET; 26251; -. DR GeneCards; KCNG2; -. DR HGNC; HGNC:6249; KCNG2. DR HPA; ENSG00000178342; Tissue enhanced (brain). DR MIM; 605696; gene. DR neXtProt; NX_Q9UJ96; -. DR OpenTargets; ENSG00000178342; -. DR PharmGKB; PA30035; -. DR VEuPathDB; HostDB:ENSG00000178342; -. DR eggNOG; KOG3713; Eukaryota. DR GeneTree; ENSGT00940000160858; -. DR HOGENOM; CLU_011722_4_1_1; -. DR InParanoid; Q9UJ96; -. DR OMA; EHLEWCC; -. DR OrthoDB; 1478695at2759; -. DR PhylomeDB; Q9UJ96; -. DR TreeFam; TF313103; -. DR PathwayCommons; Q9UJ96; -. DR Reactome; R-HSA-1296072; Voltage gated Potassium channels. DR Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion. DR SignaLink; Q9UJ96; -. DR BioGRID-ORCS; 26251; 15 hits in 1140 CRISPR screens. DR ChiTaRS; KCNG2; human. DR GeneWiki; KCNG2; -. DR GenomeRNAi; 26251; -. DR Pharos; Q9UJ96; Tclin. DR PRO; PR:Q9UJ96; -. DR Proteomes; UP000005640; Chromosome 18. DR RNAct; Q9UJ96; Protein. DR Bgee; ENSG00000178342; Expressed in sural nerve and 85 other cell types or tissues. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central. DR GO; GO:0005251; F:delayed rectifier potassium channel activity; TAS:ProtInc. 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:0006813; P:potassium ion transport; TAS:ProtInc. DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro. DR GO; GO:0008016; P:regulation of heart contraction; TAS:ProtInc. DR CDD; cd18382; BTB_POZ_Kv6_KCNG; 1. DR Gene3D; 1.10.287.70; -; 1. DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1. DR InterPro; IPR000210; BTB/POZ_dom. DR InterPro; IPR005821; Ion_trans_dom. DR InterPro; IPR003968; K_chnl_volt-dep_Kv. DR InterPro; IPR003969; K_chnl_volt-dep_Kv6. DR InterPro; IPR011333; SKP1/BTB/POZ_sf. DR InterPro; IPR003131; T1-type_BTB. DR InterPro; IPR027359; Volt_channel_dom_sf. DR PANTHER; PTHR11537:SF90; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY G MEMBER 2; 1. DR PANTHER; PTHR11537; VOLTAGE-GATED POTASSIUM CHANNEL; 1. DR Pfam; PF02214; BTB_2; 1. DR Pfam; PF00520; Ion_trans; 1. DR PRINTS; PR00169; KCHANNEL. DR PRINTS; PR01492; KV6CHANNEL. DR PRINTS; PR01491; KVCHANNEL. DR SMART; SM00225; BTB; 1. DR SUPFAM; SSF54695; POZ domain; 1. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. DR Genevisible; Q9UJ96; HS. PE 1: Evidence at protein level; 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..466 FT /note="Potassium voltage-gated channel subfamily G member FT 2" FT /id="PRO_0000054074" FT TOPO_DOM 1..177 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 178..198 FT /note="Helical; Name=Segment S1" FT /evidence="ECO:0000255" FT TRANSMEM 218..238 FT /note="Helical; Name=Segment S2" FT /evidence="ECO:0000255" FT TRANSMEM 253..273 FT /note="Helical; Name=Segment S3" FT /evidence="ECO:0000255" FT TRANSMEM 288..308 FT /note="Helical; Voltage-sensor; Name=Segment S4" FT /evidence="ECO:0000255" FT TOPO_DOM 309..321 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 322..342 FT /note="Helical; Name=Segment S5" FT /evidence="ECO:0000255" FT INTRAMEM 357..377 FT /note="Pore-forming; Name=Segment H5" FT /evidence="ECO:0000255" FT TRANSMEM 385..405 FT /note="Helical; Name=Segment S6" FT /evidence="ECO:0000255" FT TOPO_DOM 406..466 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 131..155 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 416..466 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 369..374 FT /note="Selectivity filter" FT /evidence="ECO:0000250" FT COMPBIAS 416..450 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 466 AA; 51240 MW; 0D978934F5E71469 CRC64; MEPWPCSPGG GGGTRARHVI INVGGCRVRL AWAALARCPL ARLERLRACR GHDDLLRVCD DYDVSRDEFF FDRSPCAFRA IVALLRAGKL RLLRGPCALA FRDELAYWGI DEARLERCCL RRLRRREEEA AEARAGPTER GAQGSPARAL GPRGRLQRGR RRLRDVVDNP HSGLAGKLFA CVSVSFVAVT AVGLCLSTMP DIRAEEERGE CSPKCRSLFV LETVCVAWFS FEFLLRSLQA ESKCAFLRAP LNIIDILALL PFYVSLLLGL AAGPGGTKLL ERAGLVLRLL RALRVLYVMR LARHSLGLRS LGLTMRRCAR EFGLLLLFLC VAMALFAPLV HLAERELGAR RDFSSVPASY WWAVISMTTV GYGDMVPRSL PGQVVALSSI LSGILLMAFP VTSIFHTFSR SYSELKEQQQ RAASPEPALQ EDSTHSATAT EDSSQGPDSA GLADDSADAL WVRAGR //