ID A0A3B3TGB5_9TELE Unreviewed; 743 AA.
AC A0A3B3TGB5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Potassium voltage-gated channel subfamily B member 2-like {ECO:0000313|Ensembl:ENSPKIP00000041700.1};
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:ENSPKIP00000041700.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000041700.1}
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}. Perikaryon
CC {ECO:0000256|ARBA:ARBA00004484}.
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DR AlphaFoldDB; A0A3B3TGB5; -.
DR STRING; 1676925.ENSPKIP00000041700; -.
DR Ensembl; ENSPKIT00000022738.1; ENSPKIP00000041700.1; ENSPKIG00000018061.1.
DR GeneTree; ENSGT00940000161902; -.
DR OrthoDB; 1478695at2759; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
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; IPR003973; K_chnl_volt-dep_Kv2.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537:SF134; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY B MEMBER 2; 1.
DR PANTHER; PTHR11537; VOLTAGE-GATED POTASSIUM CHANNEL; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF03521; Kv2channel; 1.
DR PRINTS; PR00169; KCHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01495; SHABCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 4: Predicted;
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
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 182..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 253..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..132
FT /note="BTB"
FT /evidence="ECO:0000259|SMART:SM00225"
FT REGION 540..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 83184 MW; AB52A9DE323E560F CRC64;
MAETGASEAP ELVEIIRAKS QCRRVRINVG GLMHEVLWRT LDRLPRTRLG RLRDCDSPGS
LLEICDDYNL SEEEFFFDRH PGAFTSILNF YRTGKLHMME EMCALSFSQE LEYWGIDEIY
LESCCQARYH QKKEQMNEEL RREAESLREK EGEDFDNNCC PEKRKKLWDL LEKPSSSVAA
KILAIISILF IVMSTVALSL NTLPDLQDVD EFGHPTDNPK LAHVEAICIA WFTMEYLLRF
LSSPSKWKFF KGPLNIIDLL AILPFYITIF LTESNKDVLQ FQNVRRVVQI FRIMRILRIL
KLARHSTGLQ SLGFTLRRSY NELGLLILFL AMGIMIFSSL VFFAEKDEDA TKFTSIPASF
WWATITMTTV GYGDIYPQTL LGKIIGGLCC IAGVLVIALP IPIIVNNFSE FYKEQKRQEK
AIKRREALER AKRNGSIVSM NMKDSFAHNE DLMDIVVDEE DKKQDLDNHL SPKHVPPTSP
KASGVKYQVA QLHSPSTSPQ HLSVQTLENR YNKMTQSPPY SPGLAKLSVL ISAEECNKAL
EKSTNSPVDR PVTDGRSTSS NESYTSCSTE FVEDDKVLNG REQAKHPRAP PPLDLSQISS
LECGGAPYSG LYDSGHPSHQ PIPLTLVGGT LRSSLRGSHQ VAKGLKVNFS ESPGTDTESP
ISGASTIFQP ESGASHCSSP YFDNSIQSSS LGSQFELVSL SKDPHGKNYL DSPKHSTQNC
SQGVAHSTGA GKTERKGENP LFT
//
