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P08510 (KCNAS_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 168. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Potassium voltage-gated channel protein Shaker
Alternative name(s):
Protein minisleep
Gene names
Name:Sh
Synonyms:mns
ORF Names:CG12348
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length655 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Voltage-dependent potassium channel involved in regulation of sleep need or efficiency. Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. Ref.13

Subunit structure

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

Subcellular location

Membrane; Multi-pass membrane protein.

Domain

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

Disruption phenotype

Reduced sleep. Flies sleep for one-third of the wild-type amount. They perform normally in a number of tasks, have preserved sleep homeostasis, but are not impaired by sleep deprivation. They also have a reduced lifespan. Ref.13

Sequence similarities

Belongs to the potassium channel family. A (Shaker) (TC 1.A.1.2) subfamily. Shaker sub-subfamily. [View classification]

RNA editing

Edited at positions 178, 360, 464, 489 and 491.
Partially edited. Ref.1 Ref.3 Ref.8 Ref.12

Sequence caution

The sequence AAA70217.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
   Biological processIon transport
Potassium transport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
RNA editing
   DomainTransmembrane
Transmembrane helix
   LigandPotassium
   Molecular functionIon channel
Potassium channel
Voltage-gated channel
   PTMGlycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaction potential

Inferred from mutant phenotype PubMed 16763031. Source: FlyBase

axon extension

Inferred from mutant phenotype PubMed 14960616. Source: FlyBase

behavioral response to ether

Non-traceable author statement PubMed 11715043. Source: FlyBase

courtship behavior

Non-traceable author statement PubMed 11715043. Source: FlyBase

detection of visible light

Inferred from mutant phenotype PubMed 16168982. Source: FlyBase

flight behavior

Inferred from mutant phenotype PubMed 17248760. Source: FlyBase

larval locomotory behavior

Inferred from mutant phenotype PubMed 16763031. Source: FlyBase

learning or memory

Non-traceable author statement PubMed 11715043. Source: FlyBase

mating behavior, sex discrimination

Inferred from direct assay PubMed 22292044. Source: FlyBase

potassium ion transport

Traceable author statement PubMed 10798390. Source: FlyBase

proboscis extension reflex

Inferred from mutant phenotype PubMed 16121192. Source: FlyBase

protein homooligomerization

Inferred from electronic annotation. Source: InterPro

regulation of circadian sleep/wake cycle, sleep

Inferred from mutant phenotype PubMed 16753559. Source: FlyBase

regulation of synaptic activity

Inferred from mutant phenotype PubMed 16763031. Source: FlyBase

sensory perception of taste

Non-traceable author statement PubMed 11715043. Source: FlyBase

sleep

Inferred from mutant phenotype PubMed 19038223. Source: FlyBase

   Cellular_componentintegral component of membrane

Inferred from direct assay PubMed 17488813. Source: FlyBase

voltage-gated potassium channel complex

Inferred from physical interaction PubMed 8968587. Source: FlyBase

   Molecular_functiondelayed rectifier potassium channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

voltage-gated cation channel activity

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

voltage-gated potassium channel activity

Non-traceable author statement PubMed 7542775. Source: FlyBase

Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform E (identifier: P08510-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Alpha (identifier: P08510-2)

Also known as: B; Adult;

The sequence of this isoform differs from the canonical sequence as follows:
     453-463: VWGKIVGSLCA → FWGKIVGSLCV
     506-655: PYLPGTLGQH...ALAVSIETDV → SYLPGALGQH...AMAVSIETDV
Isoform Beta (identifier: P08510-3)

Also known as: C; I; J; Late population;

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: MAAVAGLYGL...LQRNSLDGYG → MTMWQSGGMG...SGSNERNLNQ
Isoform Delta (identifier: P08510-5)

Also known as: Larval; A; H;

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: MAAVAGLYGL...LQRNSLDGYG → MAHITTTHGSLSQATR
     349-349: D → V
     350-655: Missing.
Isoform Epsilon (identifier: P08510-6)

Also known as: Larval; F;

The sequence of this isoform differs from the canonical sequence as follows:
     349-349: D → V
     350-655: Missing.
Isoform D (identifier: P08510-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: MAAVAGLYGL...LQRNSLDGYG → MAHITTTHGSLSQATR
     453-463: VWGKIVGSLCA → FWGKIVGSLCV
     506-655: PYLPGTLGQH...ALAVSIETDV → SYLPGALGQH...AMAVSIETDV
Note: No experimental confirmation available.
Isoform N (identifier: P08510-8)

The sequence of this isoform differs from the canonical sequence as follows:
     407-655: VVLFSSAVYF...ALAVSIETDV → KFHTVNKKKK...IKTTTKDTYI
Note: No experimental confirmation available.
Isoform L (identifier: P08510-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: MAAVAGLYGL...LQRNSLDGYG → MTMWQSGGMG...SGSNERNLNQ
     512-512: L → LV
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 655655Potassium voltage-gated channel protein Shaker
PRO_0000053963

Regions

Topological domain1 – 227227Cytoplasmic Potential
Transmembrane228 – 24619Helical; Name=Segment S1
Topological domain247 – 27832Extracellular Potential
Transmembrane279 – 30022Helical; Name=Segment S2
Topological domain301 – 31111Cytoplasmic Potential
Transmembrane312 – 33221Helical; Name=Segment S3
Topological domain333 – 36028Extracellular Potential
Transmembrane361 – 38020Helical; Voltage-sensor; Name=Segment S4
Topological domain381 – 39515Cytoplasmic Potential
Transmembrane396 – 41520Helical; Name=Segment S5
Transmembrane457 – 47822Helical; Name=Segment S6
Topological domain479 – 616138Cytoplasmic Potential
Motif442 – 4476Selectivity filter
Compositional bias15 – 5339Gln-rich
Compositional bias558 – 61962Gln-rich
Compositional bias625 – 6306Poly-Ala

Amino acid modifications

Glycosylation2591N-linked (GlcNAc...) Ref.14
Glycosylation2631N-linked (GlcNAc...) Ref.14

Natural variations

Alternative sequence1 – 6161MAAVA…LDGYG → MTMWQSGGMGGHGSQNNPWM KLMGIVHKERRHTENVQSQS GSNERNLNQ in isoform Beta and isoform L.
VSP_000954
Alternative sequence1 – 6161MAAVA…LDGYG → MAHITTTHGSLSQATR in isoform Delta and isoform D.
VSP_000956
Alternative sequence3491D → V in isoform Delta and isoform Epsilon.
VSP_000957
Alternative sequence350 – 655306Missing in isoform Delta and isoform Epsilon.
VSP_000958
Alternative sequence407 – 655249VVLFS…IETDV → KFHTVNKKKKNNIPHLLIDL RVLFKQHQKQKRNTAKRLRP SRQTYPRYPAPSKDIFSTTS HCPKVLIHILTVNRSKTTYN YSGIVQRSRIKTTTKDTYI in isoform N.
VSP_054719
Alternative sequence453 – 46311VWGKIVGSLCA → FWGKIVGSLCV in isoform Alpha and isoform D.
VSP_017889
Alternative sequence506 – 655150PYLPG…IETDV → SYLPGALGQHLKKSSLSESS SDIMDLDDGIDATTPGLTDH TGRHMVPFLRTQQSFEKQQL QLQLQLQQQSQSPHGQQMTQ QQQLGQNGLRSTNSLQLRHN NAMAVSIETDV in isoform Alpha and isoform D.
VSP_000959
Alternative sequence5121L → LV in isoform L.
VSP_054720
Natural variant1781K → E in RNA edited version.
Natural variant1781K → G in RNA edited version.
Natural variant1781K → R in RNA edited version.
Natural variant3601I → M in RNA edited version.
Natural variant4641I → V in RNA edited version.
Natural variant4891T → A in RNA edited version.
Natural variant4911Q → R in RNA edited version.

Experimental info

Mutagenesis2481T → I in mns; flies display reduced sleep. Ref.13
Sequence conflict5631Q → QQ in CAA29917. Ref.4
Sequence conflict583 – 5842QL → HV in CAA29917. Ref.4

Secondary structure

... 655
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform E [UniParc].

Last modified April 4, 2006. Version 3.
Checksum: 5833E3052C9D19B3

FASTA65574,193
        10         20         30         40         50         60 
MAAVAGLYGL GEDRQHRKKQ QQQQQHQKEQ LEQKEEQKKI AERKLQLREQ QLQRNSLDGY 

        70         80         90        100        110        120 
GSLPKLSSQD EEGGAGHGFG GGPQHFEPIP HDHDFCERVV INVSGLRFET QLRTLNQFPD 

       130        140        150        160        170        180 
TLLGDPARRL RYFDPLRNEY FFDRSRPSFD AILYYYQSGG RLRRPVNVPL DVFSEEIKFY 

       190        200        210        220        230        240 
ELGDQAINKF REDEGFIKEE ERPLPDNEKQ RKVWLLFEYP ESSQAARVVA IISVFVILLS 

       250        260        270        280        290        300 
IVIFCLETLP EFKHYKVFNT TTNGTKIEED EVPDITDPFF LIETLCIIWF TFELTVRFLA 

       310        320        330        340        350        360 
CPNKLNFCRD VMNVIDIIAI IPYFITLATV VAEEEDTLNL PKAPVSPQDK SSNQAMSLAI 

       370        380        390        400        410        420 
LRVIRLVRVF RIFKLSRHSK GLQILGRTLK ASMRELGLLI FFLFIGVVLF SSAVYFAEAG 

       430        440        450        460        470        480 
SENSFFKSIP DAFWWAVVTM TTVGYGDMTP VGVWGKIVGS LCAIAGVLTI ALPVPVIVSN 

       490        500        510        520        530        540 
FNYFYHRETD QEEMQSQNFN HVTSCPYLPG TLGQHMKKSS LSESSSDMMD LDDGVESTPG 

       550        560        570        580        590        600 
LTETHPGRSA VAPFLGAQQQ QQQPVASSLS MSIDKQLQHP LQQLTQTQLY QQQQQQQQQQ 

       610        620        630        640        650 
QNGFKQQQQQ TQQQLQQQQS HTINASAAAA TSGSGSSGLT MRHNNALAVS IETDV 

« Hide

Isoform Alpha (B) (Adult) [UniParc].

Checksum: B6453435442CB513
Show »

FASTA61670,281
Isoform Beta (C) (I) (J) (Late population) [UniParc].

Checksum: E1F358B5555496D2
Show »

FASTA64372,501
Isoform Delta (Larval) (A) (H) [UniParc].

Checksum: 05898ADD605604B5
Show »

FASTA30434,946
Isoform Epsilon (Larval) (F) [UniParc].

Checksum: B509504C2D3EE550
Show »

FASTA34940,493
Isoform D [UniParc].

Checksum: 7CFF19956D54D599
Show »

FASTA57164,734
Isoform N [UniParc].

Checksum: 5F0D4BCB5FA4F23D
Show »

FASTA50558,751
Isoform L [UniParc].

Checksum: A9B6FD52794B82C3
Show »

FASTA64472,600

References

« Hide 'large scale' references
[1]"Sequence of a probable potassium channel component encoded at Shaker locus of Drosophila."
Tempel B.L., Papazian D.M., Schwarz T.L., Jan Y.N., Jan L.Y.
Science 237:770-775(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), RNA EDITING OF POSITIONS 464; 489 AND 491.
[2]"Molecular organization of the maternal effect region of the Shaker complex of Drosophila: characterization of an I(A) channel transcript with homology to vertebrate Na(+) channel."
Baumann A., Krah-Jentgens I., Mueller R., Mueller-Holtkamp F., Seidel R., Kecskemethy N., Casal J., Ferrus A., Pongs O.
EMBO J. 6:3419-3429(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA).
Strain: Canton-S and Oregon-R.
[3]"Shaker encodes a family of putative potassium channel proteins in the nervous system of Drosophila."
Pongs O., Kecskemethy N., Mueller R., Krah-Jentgens I., Baumann A., Kiltz H.H., Canal I., Llamazares S., Ferrus A.
EMBO J. 7:1087-1096(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA; DELTA AND EPSILON), RNA EDITING OF POSITIONS 464; 489 AND 491.
Strain: Canton-S.
Tissue: Larva.
[4]"Multiple potassium-channel components are produced by alternative splicing at the Shaker locus in Drosophila."
Schwarz T.L., Tempel B.L., Papazian D.M., Jan Y.N., Jan L.Y.
Nature 331:137-142(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND E).
[5]Erratum
Schwarz T.L., Tempel B.L., Papazian D.M., Jan Y.N., Jan L.Y.
Nature 332:740-740(1988)
[6]"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.
[7]"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, ALTERNATIVE SPLICING.
Strain: Berkeley.
[8]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D), RNA EDITING OF POSITION 360.
Strain: Berkeley.
Tissue: Embryo.
[9]Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.
Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
Strain: Berkeley.
[10]"Molecular characterization of Shaker, a Drosophila gene that encodes a potassium channel."
Kamb A., Iverson L.E., Tanouye M.A.
Cell 50:405-413(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-257 (ISOFORM BETA).
Tissue: Larva.
[11]"Multiple products of the Drosophila Shaker gene may contribute to potassium channel diversity."
Kamb A., Tseng-Crank J., Tanouye M.A.
Neuron 1:421-430(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 450-534.
Strain: H4.
[12]"Nervous system targets of RNA editing identified by comparative genomics."
Hoopengardner B., Bhalla T., Staber C., Reenan R.
Science 301:832-836(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA EDITING.
[13]"Reduced sleep in Drosophila Shaker mutants."
Cirelli C., Bushey D., Hill S., Huber R., Kreber R., Ganetzky B., Tononi G.
Nature 434:1087-1092(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF THR-248.
[14]"Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster."
Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L., Panin V.
Glycobiology 17:1388-1403(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-259 AND ASN-263, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Oregon-R.
Tissue: Head.
[15]"Three-dimensional structure of the S4-S5 segment of the Shaker potassium channel."
Ohlenschlaeger O., Hojo H., Ramachandran R., Goerlach M., Haris P.I.
Biophys. J. 82:2995-3002(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 378-397.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17211 mRNA. Translation: AAA28417.1.
X06184 mRNA. Translation: CAA29549.1.
X07131 mRNA. Translation: CAA30143.1.
X07132 mRNA. Translation: CAA30144.1.
X07133 mRNA. Translation: CAA30145.1.
X07134 mRNA. Translation: CAA30146.1.
X06742 mRNA. Translation: CAA29917.1.
AE014298 Genomic DNA. Translation: AAF48785.3.
AE014298 Genomic DNA. Translation: AAF48786.3.
AE014298 Genomic DNA. Translation: AAF48790.2.
AE014298 Genomic DNA. Translation: AAN09451.1.
AE014298 Genomic DNA. Translation: AAN09452.1.
AE014298 Genomic DNA. Translation: AAS65395.2.
AE014298 Genomic DNA. Translation: AAS65396.1.
AE014298 Genomic DNA. Translation: ADV37750.1.
AE014298 Genomic DNA. Translation: AFH07440.1.
AE014298 Genomic DNA. Translation: AGB95507.1.
AY118398 mRNA. Translation: AAM48427.1.
BT050432 mRNA. Translation: ACJ13139.1.
M17155 mRNA. Translation: AAA70217.1. Frameshift.
X78908 Genomic DNA. Translation: CAA55519.1.
PIRA27159.
JH0193.
S00480.
S02284.
RefSeqNP_001162788.1. NM_001169317.1. [P08510-5]
NP_001188668.1. NM_001201739.1. [P08510-3]
NP_001245727.1. NM_001258798.1. [P08510-9]
NP_001259665.1. NM_001272736.1. [P08510-8]
NP_523393.3. NM_078669.5. [P08510-2]
NP_728120.1. NM_167592.4. [P08510-7]
NP_728122.1. NM_167594.3. [P08510-3]
NP_728123.1. NM_167595.4. [P08510-1]
NP_728124.1. NM_167596.4. [P08510-5]
NP_996497.1. NM_206774.2. [P08510-6]
NP_996498.2. NM_206775.4. [P08510-3]
UniGeneDm.7088.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HO2NMR-A378-397[»]
1HO7NMR-A378-397[»]
DisProtDP00267.
ProteinModelPortalP08510.
SMRP08510. Positions 96-489.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid59101. 10 interactions.
IntActP08510. 5 interactions.
MINTMINT-317832.

Protein family/group databases

TCDB1.A.1.2.6. the voltage-gated ion channel (vic) superfamily.

Proteomic databases

PaxDbP08510.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0089657; FBpp0088599; FBgn0003380. [P08510-1]
FBtr0089660; FBpp0088602; FBgn0003380. [P08510-7]
FBtr0089661; FBpp0088603; FBgn0003380. [P08510-3]
FBtr0302902; FBpp0292033; FBgn0003380. [P08510-3]
FBtr0302903; FBpp0292034; FBgn0003380. [P08510-3]
FBtr0308200; FBpp0300520; FBgn0003380. [P08510-9]
FBtr0332300; FBpp0304579; FBgn0003380. [P08510-8]
GeneID32780.
KEGGdme:Dmel_CG12348.

Organism-specific databases

CTD32780.
FlyBaseFBgn0003380. Sh.

Phylogenomic databases

eggNOGCOG1226.
GeneTreeENSGT00740000115291.
InParanoidP08510.
KOK05318.
OMACVSADAN.
OrthoDBEOG7M0NRD.
PhylomeDBP08510.

Gene expression databases

BgeeP08510.

Family and domain databases

Gene3D1.20.120.350. 1 hit.
3.30.710.10. 1 hit.
InterProIPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR003091. K_chnl.
IPR003968. K_chnl_volt-dep_Kv.
IPR003972. K_chnl_volt-dep_Kv1.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERPTHR11537. PTHR11537. 1 hit.
PfamPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSPR00169. KCHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSh. drosophila.
EvolutionaryTraceP08510.
GenomeRNAi32780.
NextBio780331.

Entry information

Entry nameKCNAS_DROME
AccessionPrimary (citable) accession number: P08510
Secondary accession number(s): A4V4Q2 expand/collapse secondary AC list , B6IDJ2, M9MSC0, M9NEM4, M9PF21, P08511, P08512, P08513, Q24277, Q24521, Q7KUW5, Q8IQY9, Q8MT41, Q9VWZ5, Q9VWZ9, Q9VX00
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: April 4, 2006
Last modified: July 9, 2014
This is version 168 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

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