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Q02280

- KCNAE_DROME

UniProt

Q02280 - KCNAE_DROME

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Protein

Potassium voltage-gated channel protein eag

Gene
eag, CG10952
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 226226Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei227 – 24620Helical; Name=Segment S1; Reviewed predictionAdd
BLAST
Topological domaini247 – 26822Extracellular Reviewed predictionAdd
BLAST
Transmembranei269 – 29123Helical; Name=Segment S2; Reviewed predictionAdd
BLAST
Topological domaini292 – 31322Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei314 – 33522Helical; Name=Segment S3; Reviewed predictionAdd
BLAST
Topological domaini336 – 3427Extracellular Reviewed prediction
Transmembranei343 – 36927Helical; Voltage-sensor; Name=Segment S4; Reviewed predictionAdd
BLAST
Topological domaini370 – 3712Cytoplasmic Reviewed prediction
Transmembranei372 – 39322Helical; Name=Segment S5; Reviewed predictionAdd
BLAST
Topological domaini394 – 44148Extracellular Reviewed predictionAdd
BLAST
Intramembranei442 – 46726Pore-forming; Name=Segment H5; Reviewed predictionAdd
BLAST
Topological domaini468 – 4703Extracellular Reviewed prediction
Transmembranei471 – 49323Helical; Name=Segment S6; Reviewed predictionAdd
BLAST
Topological domaini494 – 1174681Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

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

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...) Reviewed prediction
Glycosylationi412 – 4121N-linked (GlcNAc...) Reviewed prediction
Glycosylationi424 – 4241N-linked (GlcNAc...) Reviewed prediction
Modified residuei787 – 7871Phosphothreonine; by CaMK21 Publication

Post-translational modificationi

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

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.

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 9755PASAdd
BLAST
Domaini113 – 16553PACAdd
BLAST

Motif

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

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti548 – 5481Y → C in AAA28495. 1 Publication
Sequence conflicti567 – 5671N → D in AAA28495. 1 Publication
Sequence conflicti571 – 5711A → T in AAA28495. 1 Publication
Sequence conflicti699 – 6991K → R in AAA28495. 1 Publication
Sequence conflicti769 – 7691F → L in AAA28495. 1 Publication
Sequence conflicti894 – 8941I → V in AAA28495. 1 Publication
Sequence conflicti934 – 9341G → S in AAA28495. 1 Publication
Sequence conflicti1015 – 10151N → D in AAA28495. 1 Publication
Sequence conflicti1042 – 10421R → G in AAA28495. 1 Publication
Sequence conflicti1049 – 10491K → E in AAA28495. 1 Publication
Sequence conflicti1088 – 10881T → A in AAA28495. 1 Publication
Sequence conflicti1142 – 11421T → I in AAA28495. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 130 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

Similar proteinsi