ID A0A3B4AUR4_9GOBI Unreviewed; 723 AA.
AC A0A3B4AUR4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Potassium voltage-gated channel, subfamily H (eag-related), member 3 {ECO:0008006|Google:ProtNLM};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000020873.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000020873.1}
RP IDENTIFICATION.
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 AlphaFoldDB; A0A3B4AUR4; -.
DR Ensembl; ENSPMGT00000022255.1; ENSPMGP00000020873.1; ENSPMGG00000016195.1.
DR Proteomes; UP000261520; Unplaced.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
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 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 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 298..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 443..467
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..77
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 80..132
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 545..662
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
SQ SEQUENCE 723 AA; 81787 MW; 063A262F05B4A3E3 CRC64;
MPLTLNLCLL STDSNFVLGN AQVQSLYPIV YCSDGFCELT GFARGELMQK SCMCHFLYGS
ETSENLTTQM QKALDERKEF KTEIILYKKS GCKFWCLLDI VPIKNEKSDV VLFLVSHKDI
TENKNIDHAN ESETGESDAH RQKHLSLYNS QRRRSRAVLY QLSGHLQKQD KTKSKLKINN
SVLTANANPI PEYKVADIQK SRFILLHYGA FKAGWDWLIL LATFYVAITV PYNVCFTAVE
IREDGVASAR NPPTVSDILV EILFIIDIVL NFRTTFVSTS GQVVYDARSI CIHYVTSWLF
VDLIAALPFD LLYAFNISVN FGVHLLKTVR LLRLLRLLQK LDRYSQYSAV VLTLLMSTFA
LLAHWMACVW YFIGRSEIES NSASSWDIGW LHELAKRLGT PYFLTPGGPS VRSSYVTSLY
FALSSLTSVG FGNVSANTDS EKIFSICTML IGALMHAVVF GNVTAIIQRM YSRRSLYHTR
TKDLKDFIRV HRLPTALEQR VMECFQTTWA VNNGIDVSEL LKDFPDELRA DIAMHLNKEL
LQLPLFESAS RGCLRSLSLI IKTSFCAPGE FLIRQGDALQ AIYFVCSGSM EVLKDNTVLA
ILGRGDLIGS DCLTQEEVIK TNACVKALTY CDLQYISLRG LAEVLTLYPD YAQRFVNEIR
HDLTYNLRQG RNCQLPANMY FSFQLFFFPQ TATLNSCKTM INICSTSTTT TTTTTTTTTG
FRY
//