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P08510

- KCNAS_DROME

UniProt

P08510 - KCNAS_DROME

Protein

Potassium voltage-gated channel protein Shaker

Gene

Sh

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 170 (01 Oct 2014)
      Sequence version 3 (04 Apr 2006)
      Previous versions | rss
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    Functioni

    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.1 Publication

    GO - Molecular functioni

    1. delayed rectifier potassium channel activity Source: RefGenome
    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 transport Source: FlyBase
    11. proboscis extension reflex Source: FlyBase
    12. protein homooligomerization Source: InterPro
    13. regulation of circadian sleep/wake cycle, sleep Source: FlyBase
    14. regulation of synaptic activity Source: FlyBase
    15. sensory perception of taste Source: FlyBase
    16. sleep Source: FlyBase

    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_180793. 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: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0003380. Sh.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    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

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

    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 – 39415

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP08510.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 227227CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini247 – 27832ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini301 – 31111CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini333 – 36028ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini381 – 39515CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini479 – 616138CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei228 – 24619Helical; Name=Segment S1Add
    BLAST
    Transmembranei279 – 30022Helical; Name=Segment S2Add
    BLAST
    Transmembranei312 – 33221Helical; Name=Segment S3Add
    BLAST
    Transmembranei361 – 38020Helical; Voltage-sensor; Name=Segment S4Add
    BLAST
    Transmembranei396 – 41520Helical; Name=Segment S5Add
    BLAST
    Transmembranei457 – 47822Helical; Name=Segment S6Add
    BLAST

    Family & Domainsi

    Motif

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

    Compositional bias

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

    Domaini

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

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1226.
    GeneTreeiENSGT00740000115291.
    InParanoidiP08510.
    KOiK05318.
    OMAiCVSADAN.
    OrthoDBiEOG7M0NRD.
    PhylomeDBiP08510.

    Family and domain databases

    Gene3Di1.20.120.350. 1 hit.
    3.30.710.10. 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. Align

    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

    MAAVAGLYGL GEDRQHRKKQ QQQQQHQKEQ LEQKEEQKKI AERKLQLREQ    50
    QLQRNSLDGY GSLPKLSSQD EEGGAGHGFG GGPQHFEPIP HDHDFCERVV 100
    INVSGLRFET QLRTLNQFPD TLLGDPARRL RYFDPLRNEY FFDRSRPSFD 150
    AILYYYQSGG RLRRPVNVPL DVFSEEIKFY ELGDQAINKF REDEGFIKEE 200
    ERPLPDNEKQ RKVWLLFEYP ESSQAARVVA IISVFVILLS IVIFCLETLP 250
    EFKHYKVFNT TTNGTKIEED EVPDITDPFF LIETLCIIWF TFELTVRFLA 300
    CPNKLNFCRD VMNVIDIIAI IPYFITLATV VAEEEDTLNL PKAPVSPQDK 350
    SSNQAMSLAI LRVIRLVRVF RIFKLSRHSK GLQILGRTLK ASMRELGLLI 400
    FFLFIGVVLF SSAVYFAEAG SENSFFKSIP DAFWWAVVTM TTVGYGDMTP 450
    VGVWGKIVGS LCAIAGVLTI ALPVPVIVSN FNYFYHRETD QEEMQSQNFN 500
    HVTSCPYLPG TLGQHMKKSS LSESSSDMMD LDDGVESTPG LTETHPGRSA 550
    VAPFLGAQQQ QQQPVASSLS MSIDKQLQHP LQQLTQTQLY QQQQQQQQQQ 600
    QNGFKQQQQQ TQQQLQQQQS HTINASAAAA TSGSGSSGLT MRHNNALAVS 650
    IETDV 655
    Length:655
    Mass (Da):74,193
    Last modified:April 4, 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.

    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

    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:
    EMBL
    GenBank
    DDBJ
    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]
    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]
    GeneIDi32780.
    KEGGidme:Dmel_CG12348.

    Keywords - Coding sequence diversityi

    Alternative splicing, RNA editing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi A27159.
    JH0193.
    S00480.
    S02284.
    RefSeqi NP_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 ]
    UniGenei Dm.7088.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HO2 NMR - A 378-397 [» ]
    1HO7 NMR - A 378-397 [» ]
    DisProti DP00267.
    ProteinModelPortali P08510.
    SMRi P08510. Positions 96-489.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 59101. 10 interactions.
    DIPi DIP-41151N.
    IntActi P08510. 5 interactions.
    MINTi MINT-317832.

    Protein family/group databases

    TCDBi 1.A.1.2.6. the voltage-gated ion channel (vic) superfamily.

    Proteomic databases

    PaxDbi P08510.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0089657 ; 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 ]
    GeneIDi 32780.
    KEGGi dme:Dmel_CG12348.

    Organism-specific databases

    CTDi 32780.
    FlyBasei FBgn0003380. Sh.

    Phylogenomic databases

    eggNOGi COG1226.
    GeneTreei ENSGT00740000115291.
    InParanoidi P08510.
    KOi K05318.
    OMAi CVSADAN.
    OrthoDBi EOG7M0NRD.
    PhylomeDBi P08510.

    Enzyme and pathway databases

    Reactomei REACT_180793. Voltage gated Potassium channels.

    Miscellaneous databases

    ChiTaRSi Sh. drosophila.
    EvolutionaryTracei P08510.
    GenomeRNAii 32780.
    NextBioi 780331.

    Gene expression databases

    Bgeei P08510.

    Family and domain databases

    Gene3Di 1.20.120.350. 1 hit.
    3.30.710.10. 1 hit.
    InterProi IPR000210. 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 ]
    PANTHERi PTHR11537. PTHR11537. 1 hit.
    Pfami PF02214. BTB_2. 1 hit.
    PF00520. Ion_trans. 1 hit.
    [Graphical view ]
    PRINTSi PR00169. KCHANNEL.
    PR01491. KVCHANNEL.
    PR01496. SHAKERCHANEL.
    SMARTi SM00225. BTB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54695. SSF54695. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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 (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. 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.

    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: August 1, 1988
    Last sequence update: April 4, 2006
    Last modified: October 1, 2014
    This is version 170 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