ID E2B0Y1_CAMFO Unreviewed; 928 AA.
AC E2B0Y1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE SubName: Full=Potassium voltage-gated channel subfamily H member 8 {ECO:0000313|EMBL:EFN60684.1};
DE Flags: Fragment;
GN ORFNames=EAG_14908 {ECO:0000313|EMBL:EFN60684.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN60684.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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 EMBL; GL444701; EFN60684.1; -; Genomic_DNA.
DR AlphaFoldDB; E2B0Y1; -.
DR STRING; 104421.E2B0Y1; -.
DR InParanoid; E2B0Y1; -.
DR OMA; KGWFFVD; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
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 GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.1200.260; -; 1.
DR Gene3D; 1.10.287.70; -; 2.
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; IPR013099; K_chnl_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:SF637; EAG-LIKE K[+] CHANNEL, ISOFORM A; 1.
DR PANTHER; PTHR10217; VOLTAGE AND LIGAND GATED POTASSIUM CHANNEL; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF07885; Ion_trans_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000000311};
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 203..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 377..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..69
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 72..124
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 479..543
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 622..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..845
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFN60684.1"
SQ SEQUENCE 928 AA; 104225 MW; 09963E264B8A502A CRC64;
FLFTDSNFVL GNAQVPTIYP IVYCSDGFCE LTGFARAQIM QKGCACKFLY GPETKEEEKA
MIDKSLESKT ELKMEVVFYK KNGSPFDCLL DIVPIKNEKG DVVLFLASHK DITHTKNLQL
CELHDSDSNG NIDPEAPPSN YGRRRSRAVL YQLSGHYKQD NKHKIKLNNT LLHSTELPLP
EYKTSAIKKS QFILSHYGGF KSCWDWLILI ATFYVAIIVP YNASFINIDR PTMVSDVVVE
ALFIIDILLN FRTTYVSRKG EVVSNSRSIA VNYVKGWFFV DLVAALPFDF LYASDVYSGE
VRIFIRLQID LWASPLTSYR KWSLIYSWLH TLAERLKISV QNVTHTESYI TALYFTCSSL
TSVGFGNVSA NTFSEKFFSI CTMLIGALMH AVVFGNVTAI IQRMYSRRSL YQTKLRDLKD
FLVLHQIPEE LKQRMQDYFQ TIWSLNHGID IHETLKQFPE ELRGDVSMHL HREILSLPIF
ETASQGCLKL LSLHIRNNFC APGEFLIHKG DALSYIYYLC NGSMEVVQND MVVAILGKGD
LVGCDINVHQ QYGNNGGGTT GTGSVDVVVK SSCDVKALTY CDLKCIHMQG LVEVLRLYPE
YQHEFAHVIQ HDLTYNLREG YEAEQESDVN GPSLTLPSIS EDDENAVEEG ETSPLSPPNK
SPLHTSSSPR HAKFREDYRD GRRAARGVLV RGGRAAQVIV QESMEEHIRG SVERLDNQFS
TLHQDVATLS SEVRNAIQAL QMLACSPQSN PNLPTPAASR GSGVLARSSS HPPDAICWNP
PERLIDASTQ TDWPVDLFEA WVRANPRRSL KALGLDPNVV LRLPPPSPTP SPSSPPPPPY
EPLSPLVSSP QQSPSRSLTT GNDSYVFGIT RNASHIPRLY RPPNSTWDPD NKLWHRFSAG
DADNVSIYQA LRLPESRSIP SKFNPFDS
//