ID A0A3B3SP21_9TELE Unreviewed; 868 AA.
AC A0A3B3SP21;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Potassium voltage-gated channel subfamily KQT member 2-like {ECO:0000313|Ensembl:ENSPKIP00000032103.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000032103.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000032103.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR AlphaFoldDB; A0A3B3SP21; -.
DR Ensembl; ENSPKIT00000012962.1; ENSPKIP00000032103.1; ENSPKIG00000012195.1.
DR GeneTree; ENSGT00940000160093; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:UniProt.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 6.10.140.1910; -; 2.
DR InterPro; IPR020969; Ankyrin-G_BS.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003937; K_chnl_volt-dep_KCNQ.
DR InterPro; IPR003947; K_chnl_volt-dep_KCNQ2.
DR InterPro; IPR013821; K_chnl_volt-dep_KCNQ_C.
DR PANTHER; PTHR47735:SF4; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 2; 1.
DR PANTHER; PTHR47735; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 4; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF16642; KCNQ2_u3; 1.
DR Pfam; PF03520; KCNQ_channel; 2.
DR Pfam; PF11956; KCNQC3-Ank-G_bd; 1.
DR PRINTS; PR00169; KCHANNEL.
DR PRINTS; PR01461; KCNQ2CHANNEL.
DR PRINTS; PR01459; KCNQCHANNEL.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 96..322
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 446..489
FT /note="Potassium channel voltage dependent KCNQ C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03520"
FT DOMAIN 497..652
FT /note="Potassium channel voltage dependent KCNQ C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03520"
FT REGION 422..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 868 AA; 96580 MW; 13DA857825820B86 CRC64;
MVEKPSNGGV YPGPAAEKKL KVGFVGLDAG AADTSRDGAL LIAGSEAIKR GSILSKPRSS
ISVARKPPKR NAFYRKLQNF LYNVLERPRG WAFIYHAYVF LLVFSCLVLS VFSTIKEYEK
SAEDALYILE IVTIVVFGVE YFVRIWAAGC CCRYRGWRGR LKFARKPFCV IDIMVLIASV
SVLAAGTQGN VFATSAIRSL RFLQILRMIR MDRRGGTWKL LGSVIYAHSK ELITAWYIGF
LCLILASFLV YLAEKEENKE FETYADALWW GLITLTTIGY GDKYPITWNG RLLAATFTLI
GVSFFALPAG ILGSGFALKV QEQHRQKHFE KRRNPAAGLI QAAWRFYATN LARTDLLSTW
EFYERCVAIP MYRLIPPLNQ LDLLRNLKSK SGLSFSNENS CAEKLCGCCP GTNSQKVSLK
ERVFSSPRSS ASKGKSSPQG PGVRRSPSAD QSVEDSPDKV PKSWSFTDRN RARQAFQLKG
SGSRQNSEVL IEMQDEELRL KSSPAIEGLI KASLPGEDIM DDNKSCHCEF VTQELTPGLK
VTIRAVCIMR FMVSKRKFKE SLRPYDVMDV IEQYSAGHLD MLSRIKSLQS RVDQIVGRGG
QMTDKDRPKG ATEGEVSEDP SMMGRLGKVE KQVVSMERKL DFLVNIYIQR LGIPQSETDA
YFGSKEPDPA PPYHSPVDSR EQMEKSNSIN KIIRSISTTG QKNFDPPPTS VAPQSHCPPS
TSWQQHPISE CYRLSLIASP IGDPSLVRIP PPPVHDRSSS SHSGIGRYVP EDRNQGIRLK
KSDTSISIPS VDHEELERSF SGFSISQSRE NLDFISSSYF GSMCAKVRPY IAEGESDTDS
DLCTPCVHSP LSGPGEGGYS DRGWSGTK
//