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Database: UniProt
Entry: E2B0Y1_CAMFO
LinkDB: E2B0Y1_CAMFO
Original site: E2B0Y1_CAMFO 
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
//
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