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Protein

Potassium voltage-gated channel protein Shaker

Gene

Sh

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

Functioni

Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Forms rapidly inactivating tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient and may contribute to A-type currents (PubMed:2448636). Plays a role in the regulation of sleep need or efficiency (PubMed:15858564).2 Publications

GO - Molecular functioni

  1. delayed rectifier potassium channel activity Source: GO_Central
  2. voltage-gated cation channel activity Source: FlyBase
  3. voltage-gated potassium channel activity Source: FlyBase

GO - Biological processi

  1. action potential Source: FlyBase
  2. axon extension Source: FlyBase
  3. behavioral response to ether Source: FlyBase
  4. courtship behavior Source: FlyBase
  5. detection of visible light Source: FlyBase
  6. flight behavior Source: FlyBase
  7. larval locomotory behavior Source: FlyBase
  8. learning or memory Source: FlyBase
  9. mating behavior, sex discrimination Source: FlyBase
  10. potassium ion transmembrane transport Source: GO_Central
  11. potassium ion transport Source: FlyBase
  12. proboscis extension reflex Source: FlyBase
  13. protein homooligomerization Source: InterPro
  14. regulation of circadian sleep/wake cycle, sleep Source: FlyBase
  15. regulation of synaptic activity Source: FlyBase
  16. sensory perception of taste Source: FlyBase
  17. sleep Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Enzyme and pathway databases

ReactomeiREACT_332720. Voltage gated Potassium channels.

Protein family/group databases

TCDBi1.A.1.2.6. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel protein Shaker
Alternative name(s):
Protein minisleep
Gene namesi
Name:Sh
Synonyms:mns
ORF Names:CG12348
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0003380. Sh.

Subcellular locationi

Cell membrane 1 Publication; Multi-pass membrane protein Curated

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 224224CytoplasmicBy similarityAdd
BLAST
Transmembranei225 – 24622Helical; Name=Segment S1By similarityAdd
BLAST
Topological domaini247 – 27832ExtracellularBy similarityAdd
BLAST
Transmembranei279 – 30022Helical; Name=Segment S2By similarityAdd
BLAST
Topological domaini301 – 31111CytoplasmicBy similarityAdd
BLAST
Transmembranei312 – 33221Helical; Name=Segment S3By similarityAdd
BLAST
Topological domaini333 – 35725ExtracellularBy similarityAdd
BLAST
Transmembranei358 – 37821Helical; Voltage-sensor; Name=Segment S4By similarityAdd
BLAST
Topological domaini379 – 39315CytoplasmicBy similarityAdd
BLAST
Transmembranei394 – 41522Helical; Name=Segment S5By similarityAdd
BLAST
Topological domaini416 – 42914ExtracellularBy similarityAdd
BLAST
Intramembranei430 – 44112Helical; Name=Pore helixBy similarityAdd
BLAST
Intramembranei442 – 4498By similarity
Topological domaini450 – 4567ExtracellularBy similarity
Transmembranei457 – 48529Helical; Name=Segment S6By similarityAdd
BLAST
Topological domaini486 – 655170CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi248 – 2481T → I in mns; flies display reduced sleep. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 655655Potassium voltage-gated channel protein ShakerPRO_0000053963Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi259 – 2591N-linked (GlcNAc...)1 Publication
Glycosylationi263 – 2631N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP08510.

Expressioni

Gene expression databases

BgeeiP08510.

Interactioni

Subunit structurei

Homotetramer or heterotetramer of potassium channel proteins.Curated

Protein-protein interaction databases

BioGridi59101. 10 interactions.
DIPiDIP-41151N.
IntActiP08510. 5 interactions.
MINTiMINT-317832.

Structurei

Secondary structure

1
655
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi380 – 39415Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HO2NMR-A378-397[»]
1HO7NMR-A378-397[»]
DisProtiDP00267.
ProteinModelPortaliP08510.
SMRiP08510. Positions 96-489.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08510.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 188188Tetramerization domainBy similarityAdd
BLAST
Regioni380 – 39314S4-S5 linkerBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi442 – 4476Selectivity filterBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi15 – 5339Gln-richAdd
BLAST
Compositional biasi558 – 61962Gln-richAdd
BLAST
Compositional biasi625 – 6306Poly-Ala

Domaini

The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118846.
InParanoidiP08510.
KOiK05318.
OMAiEQECCER.
OrthoDBiEOG7M0NRD.
PhylomeDBiP08510.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
InterProiIPR000210. 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]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform E (identifier: P08510-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAVAGLYGL GEDRQHRKKQ QQQQQHQKEQ LEQKEEQKKI AERKLQLREQ
60 70 80 90 100
QLQRNSLDGY GSLPKLSSQD EEGGAGHGFG GGPQHFEPIP HDHDFCERVV
110 120 130 140 150
INVSGLRFET QLRTLNQFPD TLLGDPARRL RYFDPLRNEY FFDRSRPSFD
160 170 180 190 200
AILYYYQSGG RLRRPVNVPL DVFSEEIKFY ELGDQAINKF REDEGFIKEE
210 220 230 240 250
ERPLPDNEKQ RKVWLLFEYP ESSQAARVVA IISVFVILLS IVIFCLETLP
260 270 280 290 300
EFKHYKVFNT TTNGTKIEED EVPDITDPFF LIETLCIIWF TFELTVRFLA
310 320 330 340 350
CPNKLNFCRD VMNVIDIIAI IPYFITLATV VAEEEDTLNL PKAPVSPQDK
360 370 380 390 400
SSNQAMSLAI LRVIRLVRVF RIFKLSRHSK GLQILGRTLK ASMRELGLLI
410 420 430 440 450
FFLFIGVVLF SSAVYFAEAG SENSFFKSIP DAFWWAVVTM TTVGYGDMTP
460 470 480 490 500
VGVWGKIVGS LCAIAGVLTI ALPVPVIVSN FNYFYHRETD QEEMQSQNFN
510 520 530 540 550
HVTSCPYLPG TLGQHMKKSS LSESSSDMMD LDDGVESTPG LTETHPGRSA
560 570 580 590 600
VAPFLGAQQQ QQQPVASSLS MSIDKQLQHP LQQLTQTQLY QQQQQQQQQQ
610 620 630 640 650
QNGFKQQQQQ TQQQLQQQQS HTINASAAAA TSGSGSSGLT MRHNNALAVS

IETDV
Length:655
Mass (Da):74,193
Last modified:April 3, 2006 - v3
Checksum:i5833E3052C9D19B3
GO
Isoform Alpha (identifier: P08510-2) [UniParc]FASTAAdd to basket

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

Show »
Length:616
Mass (Da):70,281
Checksum:iB6453435442CB513
GO
Isoform Beta (identifier: P08510-3) [UniParc]FASTAAdd to basket

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

Show »
Length:643
Mass (Da):72,501
Checksum:iE1F358B5555496D2
GO
Isoform Delta (identifier: P08510-5) [UniParc]FASTAAdd to basket

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.

Show »
Length:304
Mass (Da):34,946
Checksum:i05898ADD605604B5
GO
Isoform Epsilon (identifier: P08510-6) [UniParc]FASTAAdd to basket

Also known as: Larval, F

The sequence of this isoform differs from the canonical sequence as follows:
     349-349: D → V
     350-655: Missing.

Show »
Length:349
Mass (Da):40,493
Checksum:iB509504C2D3EE550
GO
Isoform D (identifier: P08510-7) [UniParc]FASTAAdd to basket

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.

Show »
Length:571
Mass (Da):64,734
Checksum:i7CFF19956D54D599
GO
Isoform N (identifier: P08510-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     407-655: VVLFSSAVYF...ALAVSIETDV → KFHTVNKKKK...IKTTTKDTYI

Note: No experimental confirmation available.

Show »
Length:505
Mass (Da):58,751
Checksum:i5F0D4BCB5FA4F23D
GO
Isoform L (identifier: P08510-9) [UniParc]FASTAAdd to basket

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.

Show »
Length:644
Mass (Da):72,600
Checksum:iA9B6FD52794B82C3
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti563 – 5631Q → QQ in CAA29917 (PubMed:2448635).Curated
Sequence conflicti583 – 5842QL → HV in CAA29917 (PubMed:2448635).Curated

RNA editingi

Edited at positions 178, 360, 464, 489 and 491.1 Publication
Partially edited.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti178 – 1781K → E in RNA edited version.
Natural varianti178 – 1781K → G in RNA edited version.
Natural varianti178 – 1781K → R in RNA edited version.
Natural varianti360 – 3601I → M in RNA edited version.
Natural varianti464 – 4641I → V in RNA edited version.
Natural varianti489 – 4891T → A in RNA edited version.
Natural varianti491 – 4911Q → R in RNA edited version.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6161MAAVA…LDGYG → MTMWQSGGMGGHGSQNNPWM KLMGIVHKERRHTENVQSQS GSNERNLNQ in isoform Beta and isoform L. 3 PublicationsVSP_000954Add
BLAST
Alternative sequencei1 – 6161MAAVA…LDGYG → MAHITTTHGSLSQATR in isoform Delta and isoform D. 4 PublicationsVSP_000956Add
BLAST
Alternative sequencei349 – 3491D → V in isoform Delta and isoform Epsilon. 2 PublicationsVSP_000957
Alternative sequencei350 – 655306Missing in isoform Delta and isoform Epsilon. 2 PublicationsVSP_000958Add
BLAST
Alternative sequencei407 – 655249VVLFS…IETDV → KFHTVNKKKKNNIPHLLIDL RVLFKQHQKQKRNTAKRLRP SRQTYPRYPAPSKDIFSTTS HCPKVLIHILTVNRSKTTYN YSGIVQRSRIKTTTKDTYI in isoform N. CuratedVSP_054719Add
BLAST
Alternative sequencei453 – 46311VWGKIVGSLCA → FWGKIVGSLCV in isoform Alpha and isoform D. 5 PublicationsVSP_017889Add
BLAST
Alternative sequencei506 – 655150PYLPG…IETDV → SYLPGALGQHLKKSSLSESS SDIMDLDDGIDATTPGLTDH TGRHMVPFLRTQQSFEKQQL QLQLQLQQQSQSPHGQQMTQ QQQLGQNGLRSTNSLQLRHN NAMAVSIETDV in isoform Alpha and isoform D. 5 PublicationsVSP_000959Add
BLAST
Alternative sequencei512 – 5121L → LV in isoform L. CuratedVSP_054720

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA27159.
JH0193.
S00480.
S02284.
RefSeqiNP_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]
UniGeneiDm.7088.

Genome annotation databases

EnsemblMetazoaiFBtr0089657; FBpp0088599; FBgn0003380. [P08510-1]
GeneIDi32780.
KEGGidme:Dmel_CG12348.

Keywords - Coding sequence diversityi

Alternative splicing, RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA27159.
JH0193.
S00480.
S02284.
RefSeqiNP_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]
UniGeneiDm.7088.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HO2NMR-A378-397[»]
1HO7NMR-A378-397[»]
DisProtiDP00267.
ProteinModelPortaliP08510.
SMRiP08510. Positions 96-489.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59101. 10 interactions.
DIPiDIP-41151N.
IntActiP08510. 5 interactions.
MINTiMINT-317832.

Protein family/group databases

TCDBi1.A.1.2.6. the voltage-gated ion channel (vic) superfamily.

Proteomic databases

PaxDbiP08510.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0089657; FBpp0088599; FBgn0003380. [P08510-1]
GeneIDi32780.
KEGGidme:Dmel_CG12348.

Organism-specific databases

CTDi32780.
FlyBaseiFBgn0003380. Sh.

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118846.
InParanoidiP08510.
KOiK05318.
OMAiEQECCER.
OrthoDBiEOG7M0NRD.
PhylomeDBiP08510.

Enzyme and pathway databases

ReactomeiREACT_332720. Voltage gated Potassium channels.

Miscellaneous databases

ChiTaRSiSh. fly.
EvolutionaryTraceiP08510.
GenomeRNAii32780.
NextBioi780331.

Gene expression databases

BgeeiP08510.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
InterProiIPR000210. 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]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1986) [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(1986) [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(1987) [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(1987) [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(1987)
  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.
    , 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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  7. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  8. 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 (OCT-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(1986) [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(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 450-534.
    Strain: H4.
  12. "Expression of functional potassium channels from Shaker cDNA in Xenopus oocytes."
    Timpe L.C., Schwarz T.L., Tempel B.L., Papazian D.M., Jan Y.N., Jan L.Y.
    Nature 331:143-145(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. "Nervous system targets of RNA editing identified by comparative genomics."
    Hoopengardner B., Bhalla T., Staber C., Reenan R.
    Science 301:832-836(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA EDITING.
  14. Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF THR-248.
  15. "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(2006) [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.
  16. "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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 378-397.

Entry informationi

Entry nameiKCNAS_DROME
AccessioniPrimary (citable) accession number: P08510
Secondary accession number(s): A4V4Q2
, B6IDJ2, M9MSC0, M9NEM4, M9PF21, P08511, P08512, P08513, Q24277, Q24521, Q7KUW5, Q8IQY9, Q8MT41, Q9VWZ5, Q9VWZ9, Q9VX00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1988
Last sequence update: April 3, 2006
Last modified: March 31, 2015
This is version 176 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.