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Q02280 (KCNAE_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Potassium voltage-gated channel protein eag
Alternative name(s):
Ether-a-go-go protein
Gene names
Name:eag
ORF Names:CG10952
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1174 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.4 Ref.5 Ref.6

Subunit structure

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

Subcellular location

Membrane; Multi-pass membrane protein. Note: Eag recruits CASK to the plasma membrane. Ref.6

Tissue specificity

Expressed in the axon and the terminal boutons of motor neurons. Ref.5

Post-translational modification

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

Disruption phenotype

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. Ref.1

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.

Sequence similarities

Belongs to the potassium channel family. H (Eag) (TC 1.A.1.20) subfamily. Eag sub-subfamily. [View classification]

Contains 1 cyclic nucleotide-binding domain.

Contains 1 PAC (PAS-associated C-terminal) domain.

Contains 1 PAS (PER-ARNT-SIM) domain.

Ontologies

Keywords
   Biological processDifferentiation
Ion transport
Neurogenesis
Potassium transport
Transport
   Cellular componentMembrane
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandPotassium
   Molecular functionDevelopmental protein
Ion channel
Potassium channel
Voltage-gated channel
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral response to ether

Non-traceable author statement PubMed 11715043. Source: FlyBase

courtship behavior

Non-traceable author statement PubMed 11715043. Source: FlyBase

flight behavior

Inferred from mutant phenotype PubMed 17248760. Source: FlyBase

learning

Inferred from mutant phenotype PubMed 16135747. Source: FlyBase

learning or memory

Non-traceable author statement PubMed 11715043. Source: FlyBase

perineurial glial growth

Inferred from genetic interaction Ref.4. Source: FlyBase

potassium ion transmembrane transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

potassium ion transport

Inferred from direct assay PubMed 9497369. Source: FlyBase

protein oligomerization

Inferred from physical interaction PubMed 9497369. Source: FlyBase

regulation of heart contraction

Non-traceable author statement PubMed 11715043. Source: FlyBase

regulation of membrane potential

Inferred from Biological aspect of Ancestor. Source: RefGenome

sensory perception of smell

Non-traceable author statement PubMed 11715043. Source: FlyBase

   Cellular_componentplasma membrane

Inferred from direct assay PubMed 21059657. Source: FlyBase

voltage-gated potassium channel complex

Inferred from physical interaction PubMed 9497369. Source: FlyBase

   Molecular_functionphosphorelay sensor kinase activity

Inferred from electronic annotation. Source: InterPro

voltage-gated cation channel activity

Inferred from direct assay PubMed 12606713PubMed 21059657. Source: FlyBase

voltage-gated potassium channel activity

Inferred from direct assay PubMed 9497369. Source: FlyBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CASKQ2421010EBI-85304,EBI-214423

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11741174Potassium voltage-gated channel protein eag
PRO_0000053964

Regions

Topological domain1 – 226226Cytoplasmic Potential
Transmembrane227 – 24620Helical; Name=Segment S1; Potential
Topological domain247 – 26822Extracellular Potential
Transmembrane269 – 29123Helical; Name=Segment S2; Potential
Topological domain292 – 31322Cytoplasmic Potential
Transmembrane314 – 33522Helical; Name=Segment S3; Potential
Topological domain336 – 3427Extracellular Potential
Transmembrane343 – 36927Helical; Voltage-sensor; Name=Segment S4; Potential
Topological domain370 – 3712Cytoplasmic Potential
Transmembrane372 – 39322Helical; Name=Segment S5; Potential
Topological domain394 – 44148Extracellular Potential
Intramembrane442 – 46726Pore-forming; Name=Segment H5; Potential
Topological domain468 – 4703Extracellular Potential
Transmembrane471 – 49323Helical; Name=Segment S6; Potential
Topological domain494 – 1174681Cytoplasmic Potential
Domain43 – 9755PAS
Domain113 – 16553PAC
Nucleotide binding571 – 688118cNMP
Motif453 – 4586Selectivity filter By similarity

Amino acid modifications

Modified residue7871Phosphothreonine; by CaMK2 Ref.5
Glycosylation2621N-linked (GlcNAc...) Potential
Glycosylation4121N-linked (GlcNAc...) Potential
Glycosylation4241N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis7871T → A: Reduced eag channel amplitude and accelerated inactivation. Does not affect binding with CASK. Ref.5
Sequence conflict5481Y → C in AAA28495. Ref.1
Sequence conflict5671N → D in AAA28495. Ref.1
Sequence conflict5711A → T in AAA28495. Ref.1
Sequence conflict6991K → R in AAA28495. Ref.1
Sequence conflict7691F → L in AAA28495. Ref.1
Sequence conflict8941I → V in AAA28495. Ref.1
Sequence conflict9341G → S in AAA28495. Ref.1
Sequence conflict10151N → D in AAA28495. Ref.1
Sequence conflict10421R → G in AAA28495. Ref.1
Sequence conflict10491K → E in AAA28495. Ref.1
Sequence conflict10881T → A in AAA28495. Ref.1
Sequence conflict11421T → I in AAA28495. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q02280 [UniParc].

Last modified June 21, 2005. Version 2.
Checksum: B8F86ACBB5627FD3

FASTA1,174126,371
        10         20         30         40         50         60 
MPGGRRGLVA PQNTFLENII RRSNSQPDSS FLLANAQIVD FPIVYCNESF CKISGYNRAE 

        70         80         90        100        110        120 
VMQKSCRYVC GFMYGELTDK ETVGRLEYTL ENQQQDQFEI LLYKKNNLQC GCALSQFGKA 

       130        140        150        160        170        180 
QTQETPLWLL LQVAPIRNER DLVVLFLLTF RDITALKQPI DSEDTKGVLG LSKFAKLARS 

       190        200        210        220        230        240 
VTRSRQFSAH LPTLKDPTKQ SNLAHMMSLS ADIMPQYRQE APKTPPHILL HYCAFKAIWD 

       250        260        270        280        290        300 
WVILCLTFYT AIMVPYNVAF KNKTSEDVSL LVVDSIVDVI FFIDIVLNFH TTFVGPGGEV 

       310        320        330        340        350        360 
VSDPKVIRMN YLKSWFIIDL LSCLPYDVFN AFDRDEDGIG SLFSALKVVR LLRLGRVVRK 

       370        380        390        400        410        420 
LDRYLEYGAA MLILLLCFYM LVAHWLACIW YSIGRSDADN GIQYSWLWKL ANVTQSPYSY 

       430        440        450        460        470        480 
IWSNDTGPEL VNGPSRKSMY VTALYFTMTC MTSVGFGNVA AETDNEKVFT ICMMIIAALL 

       490        500        510        520        530        540 
YATIFGHVTT IIQQMTSATA KYHDMLNNVR EFMKLHEVPK ALSERVMDYV VSTWAMTKGL 

       550        560        570        580        590        600 
DTEKVLNYCP KDMKADICVH LNRKVFNEHP AFRLASDGCL RALAMHFMMS HSAPGDLLYH 

       610        620        630        640        650        660 
TGESIDSLCF IVTGSLEVIQ DDEVVAILGK GDVFGDQFWK DSAVGQSAAN VRALTYCDLH 

       670        680        690        700        710        720 
AIKRDKLLEV LDFYSAFANS FARNLVLTYN LRHRLIFRKV ADVKREKELA ERRKNEPQLP 

       730        740        750        760        770        780 
QNQDHLVRKI FSKFRRTPQV QAGSKELVGG SGQSDVEKGD GEVERTKVFP KAPKLQASQA 

       790        800        810        820        830        840 
TLARQDTIDE GGEVDSSPPS RDSRVVIEGA AVSSATVGPS PPVATTSSAA AGAGVSGGPG 

       850        860        870        880        890        900 
SGGTVVAIVT KADRNLALER ERQIEMASSR ATTSDTYDTG LRETPPTLAQ RDLIATVLDM 

       910        920        930        940        950        960 
KVDVRLELQR MQQRIGRIED LLGELVKRLA PGAGSGGNAP DNSSGQTTPG DEICAGCGAG 

       970        980        990       1000       1010       1020 
GGGTPTTQAP PTSAVTSPVD TVITISSPGA SGSGSGTGAG AGSAVAGAGG AGLLNPGATV 

      1030       1040       1050       1060       1070       1080 
VSSAGGNGLG PLMLKKRRSK SRKAPAPPKQ TLASTAGTAT AAPAGVAGSG MTSSAPASAD 

      1090       1100       1110       1120       1130       1140 
QQQQHQSTAD QSPTTPGAEL LHLRLLEEDF TAAQLPSTSS GGAGGGGGSG SGATPTTPPP 

      1150       1160       1170 
TTAGGSGSGT PTSTTATTTP TGSGTATRGK LDFL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M61157 mRNA. Translation: AAA28495.1.
AE014298 Genomic DNA. Translation: AAF48410.1.
PIRA40853.
RefSeqNP_511158.2. NM_078603.4.
UniGeneDm.2914.

3D structure databases

ProteinModelPortalQ02280.
SMRQ02280. Positions 12-154, 440-491, 499-697.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid58786. 5 interactions.
IntActQ02280. 3 interactions.
STRING7227.FBpp0110308.

Protein family/group databases

TCDB1.A.1.20.6. the voltage-gated ion channel (vic) superfamily.

Proteomic databases

PaxDbQ02280.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0073955; FBpp0073772; FBgn0000535.
GeneID32428.
KEGGdme:Dmel_CG10952.

Organism-specific databases

CTD32428.
FlyBaseFBgn0000535. eag.

Phylogenomic databases

eggNOGCOG2202.
GeneTreeENSGT00680000099663.
InParanoidQ02280.
KOK05322.
OrthoDBEOG7QG43V.
PhylomeDBQ02280.

Gene expression databases

BgeeQ02280.

Family and domain databases

Gene3D2.60.120.10. 1 hit.
InterProIPR018490. 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]
PfamPF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
PF13426. PAS_9. 1 hit.
[Graphical view]
PRINTSPR01463. EAGCHANLFMLY.
PR01464. EAGCHANNEL.
SMARTSM00100. cNMP. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 1 hit.
[Graphical view]
SUPFAMSSF51206. SSF51206. 1 hit.
SSF55785. SSF55785. 1 hit.
PROSITEPS50042. CNMP_BINDING_3. 1 hit.
PS50113. PAC. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi32428.
NextBio778416.
PROQ02280.

Entry information

Entry nameKCNAE_DROME
AccessionPrimary (citable) accession number: Q02280
Secondary accession number(s): Q9VXZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: June 21, 2005
Last modified: April 16, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase