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KCNG2_HUMAN
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   03-AUG-2022, entry version 161.
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}.
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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; 1.
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   PaxDb; Q9UJ96; -.
DR   PeptideAtlas; Q9UJ96; -.
DR   PRIDE; Q9UJ96; -.
DR   Antibodypedia; 59003; 147 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   CTD; 26251; -.
DR   DisGeNET; 26251; -.
DR   GeneCards; KCNG2; -.
DR   HGNC; HGNC:6249; KCNG2.
DR   HPA; ENSG00000178342; Tissue enriched (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; HLEWCCK; -.
DR   OrthoDB; 818306at2759; -.
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 1061 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 84 other tissues.
DR   Genevisible; Q9UJ96; HS.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.350; -; 1.
DR   Gene3D; 3.30.710.10; -; 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; IPR028325; VG_K_chnl.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR11537; PTHR11537; 1.
DR   Pfam; PF02214; BTB_2; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   PRINTS; PR01492; KV6CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
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
 
 
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