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Q02280

- KCNAE_DROME

UniProt

Q02280 - KCNAE_DROME

Protein

Potassium voltage-gated channel protein eag

Gene

eag

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (21 Jun 2005)
      Previous versions | rss
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    Functioni

    Structural component of a potassium channel. Mediates the potassium permeability of membranes; potassium current is regulated by CaMKII and CASK. Has a role in growth of the perineurial glial layer of the larval peripheral nerve.4 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi571 – 688118cNMPAdd
    BLAST

    GO - Molecular functioni

    1. phosphorelay sensor kinase activity Source: InterPro
    2. protein binding Source: IntAct
    3. voltage-gated cation channel activity Source: FlyBase
    4. voltage-gated potassium channel activity Source: FlyBase

    GO - Biological processi

    1. behavioral response to ether Source: FlyBase
    2. courtship behavior Source: FlyBase
    3. flight behavior Source: FlyBase
    4. learning Source: FlyBase
    5. learning or memory Source: FlyBase
    6. perineurial glial growth Source: FlyBase
    7. potassium ion transmembrane transport Source: RefGenome
    8. potassium ion transport Source: FlyBase
    9. protein oligomerization Source: FlyBase
    10. regulation of heart contraction Source: FlyBase
    11. regulation of membrane potential Source: RefGenome
    12. sensory perception of smell Source: FlyBase

    Keywords - Molecular functioni

    Developmental protein, Ion channel, Potassium channel, Voltage-gated channel

    Keywords - Biological processi

    Differentiation, Ion transport, Neurogenesis, Potassium transport, Transport

    Keywords - Ligandi

    Potassium

    Enzyme and pathway databases

    ReactomeiREACT_180793. Voltage gated Potassium channels.

    Protein family/group databases

    TCDBi1.A.1.20.6. the voltage-gated ion channel (vic) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Potassium voltage-gated channel protein eag
    Alternative name(s):
    Ether-a-go-go protein
    Gene namesi
    Name:eag
    ORF Names:CG10952
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0000535. eag.

    Subcellular locationi

    Membrane 1 Publication; Multi-pass membrane protein 1 Publication
    Note: Eag recruits CASK to the plasma membrane.

    GO - Cellular componenti

    1. plasma membrane Source: FlyBase
    2. voltage-gated potassium channel complex Source: FlyBase

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Increased growth of the perineurial glial layer of the larval peripheral nerve. Hyperexcitability at the larval neuromuscular junction (NMJ) and memory formation defects in the adult.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi787 – 7871T → A: Reduced eag channel amplitude and accelerated inactivation. Does not affect binding with CASK. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11741174Potassium voltage-gated channel protein eagPRO_0000053964Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi262 – 2621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi412 – 4121N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi424 – 4241N-linked (GlcNAc...)Sequence Analysis
    Modified residuei787 – 7871Phosphothreonine; by CaMK21 Publication

    Post-translational modificationi

    When in complex with CASK, the efficiency of Thr-787 phosphorylation is increased.1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ02280.

    Expressioni

    Tissue specificityi

    Expressed in the axon and the terminal boutons of motor neurons.1 Publication

    Gene expression databases

    BgeeiQ02280.

    Interactioni

    Subunit structurei

    The voltage-dependent potassium channel is a heterotetramer of potassium channel proteins By similarity. Interaction with CASK.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CASKQ2421010EBI-85304,EBI-214423

    Protein-protein interaction databases

    BioGridi58786. 5 interactions.
    IntActiQ02280. 3 interactions.
    STRINGi7227.FBpp0110308.

    Structurei

    3D structure databases

    ProteinModelPortaliQ02280.
    SMRiQ02280. Positions 12-154, 499-697.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 226226CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini247 – 26822ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini292 – 31322CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini336 – 3427ExtracellularSequence Analysis
    Topological domaini370 – 3712CytoplasmicSequence Analysis
    Topological domaini394 – 44148ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini468 – 4703ExtracellularSequence Analysis
    Topological domaini494 – 1174681CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei442 – 46726Pore-forming; Name=Segment H5Sequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei227 – 24620Helical; Name=Segment S1Sequence AnalysisAdd
    BLAST
    Transmembranei269 – 29123Helical; Name=Segment S2Sequence AnalysisAdd
    BLAST
    Transmembranei314 – 33522Helical; Name=Segment S3Sequence AnalysisAdd
    BLAST
    Transmembranei343 – 36927Helical; Voltage-sensor; Name=Segment S4Sequence AnalysisAdd
    BLAST
    Transmembranei372 – 39322Helical; Name=Segment S5Sequence AnalysisAdd
    BLAST
    Transmembranei471 – 49323Helical; Name=Segment S6Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini43 – 9755PASPROSITE-ProRule annotationAdd
    BLAST
    Domaini113 – 16553PACPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi453 – 4586Selectivity filterBy similarity

    Sequence similaritiesi

    Contains 1 cyclic nucleotide-binding domain.PROSITE-ProRule annotation
    Contains 1 PAC (PAS-associated C-terminal) domain.PROSITE-ProRule annotation
    Contains 1 PAS (PER-ARNT-SIM) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2202.
    GeneTreeiENSGT00680000099663.
    InParanoidiQ02280.
    KOiK05322.
    OrthoDBiEOG7QG43V.
    PhylomeDBiQ02280.

    Family and domain databases

    Gene3Di2.60.120.10. 1 hit.
    InterProiIPR018490. cNMP-bd-like.
    IPR000595. cNMP-bd_dom.
    IPR005821. Ion_trans_dom.
    IPR003949. K_chnl_volt-dep_EAG.
    IPR003938. K_chnl_volt-dep_EAG/ELK/ERG.
    IPR001610. PAC.
    IPR000014. PAS.
    IPR000700. PAS-assoc_C.
    IPR014710. RmlC-like_jellyroll.
    [Graphical view]
    PfamiPF00027. cNMP_binding. 1 hit.
    PF00520. Ion_trans. 1 hit.
    PF13426. PAS_9. 1 hit.
    [Graphical view]
    PRINTSiPR01463. EAGCHANLFMLY.
    PR01464. EAGCHANNEL.
    SMARTiSM00100. cNMP. 1 hit.
    SM00086. PAC. 1 hit.
    SM00091. PAS. 1 hit.
    [Graphical view]
    SUPFAMiSSF51206. SSF51206. 1 hit.
    SSF55785. SSF55785. 1 hit.
    PROSITEiPS50042. CNMP_BINDING_3. 1 hit.
    PS50113. PAC. 1 hit.
    PS50112. PAS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q02280-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPGGRRGLVA PQNTFLENII RRSNSQPDSS FLLANAQIVD FPIVYCNESF     50
    CKISGYNRAE VMQKSCRYVC GFMYGELTDK ETVGRLEYTL ENQQQDQFEI 100
    LLYKKNNLQC GCALSQFGKA QTQETPLWLL LQVAPIRNER DLVVLFLLTF 150
    RDITALKQPI DSEDTKGVLG LSKFAKLARS VTRSRQFSAH LPTLKDPTKQ 200
    SNLAHMMSLS ADIMPQYRQE APKTPPHILL HYCAFKAIWD WVILCLTFYT 250
    AIMVPYNVAF KNKTSEDVSL LVVDSIVDVI FFIDIVLNFH TTFVGPGGEV 300
    VSDPKVIRMN YLKSWFIIDL LSCLPYDVFN AFDRDEDGIG SLFSALKVVR 350
    LLRLGRVVRK LDRYLEYGAA MLILLLCFYM LVAHWLACIW YSIGRSDADN 400
    GIQYSWLWKL ANVTQSPYSY IWSNDTGPEL VNGPSRKSMY VTALYFTMTC 450
    MTSVGFGNVA AETDNEKVFT ICMMIIAALL YATIFGHVTT IIQQMTSATA 500
    KYHDMLNNVR EFMKLHEVPK ALSERVMDYV VSTWAMTKGL DTEKVLNYCP 550
    KDMKADICVH LNRKVFNEHP AFRLASDGCL RALAMHFMMS HSAPGDLLYH 600
    TGESIDSLCF IVTGSLEVIQ DDEVVAILGK GDVFGDQFWK DSAVGQSAAN 650
    VRALTYCDLH AIKRDKLLEV LDFYSAFANS FARNLVLTYN LRHRLIFRKV 700
    ADVKREKELA ERRKNEPQLP QNQDHLVRKI FSKFRRTPQV QAGSKELVGG 750
    SGQSDVEKGD GEVERTKVFP KAPKLQASQA TLARQDTIDE GGEVDSSPPS 800
    RDSRVVIEGA AVSSATVGPS PPVATTSSAA AGAGVSGGPG SGGTVVAIVT 850
    KADRNLALER ERQIEMASSR ATTSDTYDTG LRETPPTLAQ RDLIATVLDM 900
    KVDVRLELQR MQQRIGRIED LLGELVKRLA PGAGSGGNAP DNSSGQTTPG 950
    DEICAGCGAG GGGTPTTQAP PTSAVTSPVD TVITISSPGA SGSGSGTGAG 1000
    AGSAVAGAGG AGLLNPGATV VSSAGGNGLG PLMLKKRRSK SRKAPAPPKQ 1050
    TLASTAGTAT AAPAGVAGSG MTSSAPASAD QQQQHQSTAD QSPTTPGAEL 1100
    LHLRLLEEDF TAAQLPSTSS GGAGGGGGSG SGATPTTPPP TTAGGSGSGT 1150
    PTSTTATTTP TGSGTATRGK LDFL 1174
    Length:1,174
    Mass (Da):126,371
    Last modified:June 21, 2005 - v2
    Checksum:iB8F86ACBB5627FD3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti548 – 5481Y → C in AAA28495. (PubMed:1840699)Curated
    Sequence conflicti567 – 5671N → D in AAA28495. (PubMed:1840699)Curated
    Sequence conflicti571 – 5711A → T in AAA28495. (PubMed:1840699)Curated
    Sequence conflicti699 – 6991K → R in AAA28495. (PubMed:1840699)Curated
    Sequence conflicti769 – 7691F → L in AAA28495. (PubMed:1840699)Curated
    Sequence conflicti894 – 8941I → V in AAA28495. (PubMed:1840699)Curated
    Sequence conflicti934 – 9341G → S in AAA28495. (PubMed:1840699)Curated
    Sequence conflicti1015 – 10151N → D in AAA28495. (PubMed:1840699)Curated
    Sequence conflicti1042 – 10421R → G in AAA28495. (PubMed:1840699)Curated
    Sequence conflicti1049 – 10491K → E in AAA28495. (PubMed:1840699)Curated
    Sequence conflicti1088 – 10881T → A in AAA28495. (PubMed:1840699)Curated
    Sequence conflicti1142 – 11421T → I in AAA28495. (PubMed:1840699)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M61157 mRNA. Translation: AAA28495.1.
    AE014298 Genomic DNA. Translation: AAF48410.1.
    PIRiA40853.
    RefSeqiNP_511158.2. NM_078603.4.
    UniGeneiDm.2914.

    Genome annotation databases

    EnsemblMetazoaiFBtr0073955; FBpp0073772; FBgn0000535.
    GeneIDi32428.
    KEGGidme:Dmel_CG10952.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M61157 mRNA. Translation: AAA28495.1 .
    AE014298 Genomic DNA. Translation: AAF48410.1 .
    PIRi A40853.
    RefSeqi NP_511158.2. NM_078603.4.
    UniGenei Dm.2914.

    3D structure databases

    ProteinModelPortali Q02280.
    SMRi Q02280. Positions 12-154, 499-697.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 58786. 5 interactions.
    IntActi Q02280. 3 interactions.
    STRINGi 7227.FBpp0110308.

    Protein family/group databases

    TCDBi 1.A.1.20.6. the voltage-gated ion channel (vic) superfamily.

    Proteomic databases

    PaxDbi Q02280.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0073955 ; FBpp0073772 ; FBgn0000535 .
    GeneIDi 32428.
    KEGGi dme:Dmel_CG10952.

    Organism-specific databases

    CTDi 32428.
    FlyBasei FBgn0000535. eag.

    Phylogenomic databases

    eggNOGi COG2202.
    GeneTreei ENSGT00680000099663.
    InParanoidi Q02280.
    KOi K05322.
    OrthoDBi EOG7QG43V.
    PhylomeDBi Q02280.

    Enzyme and pathway databases

    Reactomei REACT_180793. Voltage gated Potassium channels.

    Miscellaneous databases

    GenomeRNAii 32428.
    NextBioi 778416.
    PROi Q02280.

    Gene expression databases

    Bgeei Q02280.

    Family and domain databases

    Gene3Di 2.60.120.10. 1 hit.
    InterProi IPR018490. cNMP-bd-like.
    IPR000595. cNMP-bd_dom.
    IPR005821. Ion_trans_dom.
    IPR003949. K_chnl_volt-dep_EAG.
    IPR003938. K_chnl_volt-dep_EAG/ELK/ERG.
    IPR001610. PAC.
    IPR000014. PAS.
    IPR000700. PAS-assoc_C.
    IPR014710. RmlC-like_jellyroll.
    [Graphical view ]
    Pfami PF00027. cNMP_binding. 1 hit.
    PF00520. Ion_trans. 1 hit.
    PF13426. PAS_9. 1 hit.
    [Graphical view ]
    PRINTSi PR01463. EAGCHANLFMLY.
    PR01464. EAGCHANNEL.
    SMARTi SM00100. cNMP. 1 hit.
    SM00086. PAC. 1 hit.
    SM00091. PAS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51206. SSF51206. 1 hit.
    SSF55785. SSF55785. 1 hit.
    PROSITEi PS50042. CNMP_BINDING_3. 1 hit.
    PS50113. PAC. 1 hit.
    PS50112. PAS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A distinct potassium channel polypeptide encoded by the Drosophila eag locus."
      Warmke J., Drysdale R.A., Ganetzky B.
      Science 252:1560-1562(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE.
      Tissue: Head.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. "Control of Drosophila perineurial glial growth by interacting neurotransmitter-mediated signaling pathways."
      Yager J., Richards S., Hekmat-Scafe D.S., Hurd D.D., Sundaresan V., Caprette D.R., Saxton W.M., Carlson J.R., Stern M.
      Proc. Natl. Acad. Sci. U.S.A. 98:10445-10450(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Calcium/calmodulin-dependent protein kinase II phosphorylates and regulates the Drosophila eag potassium channel."
      Wang Z., Wilson G.F., Griffith L.C.
      J. Biol. Chem. 277:24022-24029(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT THR-787, MUTAGENESIS OF THR-787, TISSUE SPECIFICITY.
    6. "Camguk/CASK enhances Ether-a-go-go potassium current by a phosphorylation-dependent mechanism."
      Marble D.D., Hegle A.P., Snyder E.D. II, Dimitratos S., Bryant P.J., Wilson G.F.
      J. Neurosci. 25:4898-4907(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CASK, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiKCNAE_DROME
    AccessioniPrimary (citable) accession number: Q02280
    Secondary accession number(s): Q9VXZ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: June 21, 2005
    Last modified: October 1, 2014
    This is version 131 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Miscellaneous

    The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.
    The segment H5 is thought to line the channel pore.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3