ID A0A3P9Q7E3_POERE Unreviewed; 1190 AA.
AC A0A3P9Q7E3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Potassium voltage-gated channel subfamily H member 8-like {ECO:0000313|Ensembl:ENSPREP00000029919.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000029919.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000029919.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000029919.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC heterotetrameric complex of pore-forming alpha subunits that can
CC associate with modulating beta subunits.
CC {ECO:0000256|ARBA:ARBA00011552}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR RefSeq; XP_017157512.1; XM_017302023.1.
DR AlphaFoldDB; A0A3P9Q7E3; -.
DR STRING; 8081.ENSPREP00000029919; -.
DR Ensembl; ENSPRET00000030260.1; ENSPREP00000029919.1; ENSPREG00000020257.1.
DR GeneID; 103481844; -.
DR CTD; 23416; -.
DR GeneTree; ENSGT00940000165242; -.
DR OMA; DSSQWNV; -.
DR OrthoDB; 66005at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000020257; Expressed in head.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0106151; F:CNBH domain intrinsic ligand binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:Ensembl.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IEA:Ensembl.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.1200.260; -; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR003950; K_chnl_volt-dep_ELK.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR10217:SF641; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY H MEMBER 3 ISOFORM X1; 1.
DR PANTHER; PTHR10217; VOLTAGE AND LIGAND GATED POTASSIUM CHANNEL; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR PRINTS; PR01465; ELKCHANNEL.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00086; PAC; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000242638};
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 231..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 358..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 473..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 503..527
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..90
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 93..145
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 605..722
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 750..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 857..891
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 974..1025
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1190 AA; 130789 MW; 049EDCC274015FF2 CRC64;
MPVMRGLLAP QNTFLDTIAT RFDGTHSNFV LGNAQVQSLY PIVYCSDGFC ELTGYARAEL
MQKSCACHFL YGPETSDRST AQIQGALDDR REFKTELVFY KKEGTKFWCL LDIVPIKNEK
GEVVLFLVSH KDITDKKMEQ DPEQGPETDE ETGLQVHQVT RPPGFNANRR RSRAVLYQLS
GHLQKQDKSK LKINNNMFGQ KPPIPEYKVA AIQKSRFILL HYGTFKAGWD WLILLATFYV
AVTVPYNVCF SGGRDEGGTS RNPPSVSDIL VEILFILDIV LNFRTTFVST SGQVVYDARS
ICVHYVTTWL FVDLVAALPF DLLYAFNVTV NFRVHLLKTV RLLRLLRLLQ KLERYSQYSA
VVLTLLMSMF ALLAHWMACV WYYIGRKEIE SLGSSDIGWL YELAKRLGTP YFMSPLTTQT
PPAVSSLPAN STQWSASGSE VAGQGPWNSS QDYGNISGSG GLKMLGGGPS TRSSYVTALY
FALSSLTSVG FGNVSANTDS EKIFSICTML IGALMHAVVF GNVTAIIQRM YSRRSLYHTR
TKDLKDFIRV HRLPKALEQR MLECFQTTWS VNNGIDVNEL LKDFPDELRA DIAMHLNKEL
LQLPLFESAS RGCLRSLSLI IKTSFCAPGE FLIRQGDALQ AIYFVCSGSM EVLKDNTVLA
ILGKGDLIGS DSLTKEQVIK TNANVKALTY CDLQYISLKG LREVLRLYPE YAQKFVSEIQ
HDLTYNLREG HGADDWESNG GLVKKLPSIR EDEEGDEEQS SVSRAPRSPL HLSRGLSSPL
RSPLLAPRPF RAPTEHSRPS TLQIPVVSFC SAPPELSPRF VDGIETESIS TSSQKFEFSP
SLSHAAPPYP YAGMREHSEI KQSVTKLTEE MNSLSKQVSN LSQELREMAC LLKPLLQAAP
QPILMSAVPN LAPPQGSANQ LLSSPWFPAV APAVAPAAAS RSPQREDADS LLDSGDPEGE
GLQRCLLPTH HSPKRPDSSP SASAQRPASP LATGSSFPSS KAEALQGSPV CQSPQVSPSN
GILLPSLEDQ PALRSSTPSL SLSFSVSLSS SQSFSPCPSR PTSCGSRGLL PPPPSQDTPP
PLSSHRSAPS SVSSSPGGRR LRPSLSIPFA STAAPVRPST LSLPVSLDFG SSAKRDAHTP
ARCNLQRRHE EARAAAGPQE VEMEEWGRRG EESKTSMEDL SFIDEDDPGL
//
