ID A0A3Q1H9R0_ANATE Unreviewed; 643 AA.
AC A0A3Q1H9R0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Potassium voltage-gated channel subfamily D member 3-like {ECO:0000313|Ensembl:ENSATEP00000004184.2};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000004184.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000004184.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendrite
CC {ECO:0000256|ARBA:ARBA00004279}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR AlphaFoldDB; A0A3Q1H9R0; -.
DR Ensembl; ENSATET00000004220.2; ENSATEP00000004184.2; ENSATEG00000002911.2.
DR GeneTree; ENSGT00940000155343; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0030425; C:dendrite; 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 CDD; cd18419; BTB_POZ_KCND3; 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; IPR003975; K_chnl_volt-dep_Kv4.
DR InterPro; IPR004056; K_chnl_volt-dep_Kv4.3.
DR InterPro; IPR024587; K_chnl_volt-dep_Kv4_C.
DR InterPro; IPR021645; Shal-type_N.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537:SF182; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY D MEMBER 3; 1.
DR PANTHER; PTHR11537; VOLTAGE-GATED POTASSIUM CHANNEL; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF11879; DUF3399; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF11601; Shal-type; 1.
DR PRINTS; PR00169; KCHANNEL.
DR PRINTS; PR01518; KV43CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01497; SHALCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 4: Predicted;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
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 Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..643
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030079391"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 253..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..139
FT /note="BTB"
FT /evidence="ECO:0000259|SMART:SM00225"
FT REGION 522..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 643 AA; 72555 MW; 706A25DDDB8E5DF9 CRC64;
MAAGVAAWLP FARAAAIGWM PVANLPMPVA PTEKNKRQDE LIVLNVSGRR FQTWRNTLDR
YPDTLLGSSE KEFFYNEETK EYFFDRDPDV FRSVLNFYRT GKLHYPRYEC ISSYDEELAF
FGIVPEIIGD CCYEEYKDRK RENAERLMDD QEDNKDAKLP NMTFRETMWR AFENPHTSTM
ALVFYYVTGF FIAVSVITNV VETVPCGSAP NQKEVPCGER YTVAFFCMDT ACVMIFTVEY
LMRLFAAPSR YRFMRSVMSI IDVVAILPYY IGLVMTDNED VSGAFVTLRV FRVFRIFKFS
RHSQGLRILG YTLKSCASEL GFLLFSLTMA IIIFATVMFY AEKGSSSSKF TSIPASFWYT
IVTMTTLGYG DMVPKTIAGK IFGSICSLSG VLVIALPVPV IVSNFSRIYH QNQRADKRRA
QKKARLARIR ISKTGSSSAF LHSKRNGLFN EALELTSSTE DDQRLSKSTS LLESQHHHLL
HCLEKTTVSK VSDDILMNNH EFVDEQYYQQ SYLEAGLQNY PSRSPSLSSQ DGVTGTCCTR
RSKKHHSPLP NASAPAHIQP LTQTHTHQQG LQELSTIHIQ PLTTSIRSSL NMRVDDLAPL
NCQSSQITTA IISIPTPPVT TPEGDAHLPA GPTHQNIVKV SAL
//
