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P13607

- ATNA_DROME

UniProt

P13607 - ATNA_DROME

Protein

Sodium/potassium-transporting ATPase subunit alpha

Gene

Atpalpha

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 158 (01 Oct 2014)
      Sequence version 3 (20 Jun 2001)
      Previous versions | rss
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    Functioni

    This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.3 Publications

    Catalytic activityi

    ATP + H2O + Na+(In) + K+(Out) = ADP + phosphate + Na+(Out) + K+(In).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei394 – 39414-aspartylphosphate intermediateCurated
    Binding sitei526 – 5261ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: InterPro
    3. sodium:potassium-exchanging ATPase activity Source: FlyBase

    GO - Biological processi

    1. adult locomotory behavior Source: FlyBase
    2. ATP biosynthetic process Source: InterPro
    3. cation transport Source: FlyBase
    4. determination of adult lifespan Source: FlyBase
    5. embryonic development via the syncytial blastoderm Source: FlyBase
    6. jump response Source: FlyBase
    7. locomotory behavior Source: FlyBase
    8. neuromuscular process Source: FlyBase
    9. regulation of cell shape Source: FlyBase
    10. regulation of tube architecture, open tracheal system Source: FlyBase
    11. regulation of tube diameter, open tracheal system Source: FlyBase
    12. regulation of tube length, open tracheal system Source: FlyBase
    13. response to mechanical stimulus Source: FlyBase
    14. response to temperature stimulus Source: FlyBase
    15. sensory perception of sound Source: FlyBase
    16. septate junction assembly Source: FlyBase
    17. sodium ion transmembrane transport Source: GOC
    18. synaptic growth at neuromuscular junction Source: FlyBase
    19. synaptic transmission Source: FlyBase
    20. tissue homeostasis Source: FlyBase
    21. trachea morphogenesis Source: FlyBase

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Ion transport, Potassium transport, Sodium transport, Sodium/potassium transport, Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, Potassium, Sodium

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sodium/potassium-transporting ATPase subunit alpha (EC:3.6.3.9)
    Short name:
    Na(+)/K(+) ATPase alpha subunit
    Alternative name(s):
    Sodium pump subunit alpha
    Gene namesi
    Name:Atpalpha
    Synonyms:Na-p
    ORF Names:CG5670
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0002921. Atpalpha.

    Subcellular locationi

    GO - Cellular componenti

    1. basolateral plasma membrane Source: FlyBase
    2. nucleus Source: FlyBase
    3. plasma membrane Source: FlyBase
    4. septate junction Source: FlyBase
    5. sodium:potassium-exchanging ATPase complex Source: FlyBase

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1020 – 10201D → N in allele ATP-alpha-dts2; homozygous lethal and temperature dependent bang sensitive paralysis, shortened life span and neurodegeneration when heterozygous. 1 Publication
    Mutagenesisi1021 – 10211E → K in allele ATP-alpha-dts1; homozygous lethal and temperature dependent bang sensitive paralysis, shortened life span and neurodegeneration when heterozygous. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10411041Sodium/potassium-transporting ATPase subunit alphaPRO_0000046309Add
    BLAST

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP13607.
    PRIDEiP13607.

    Expressioni

    Tissue specificityi

    High levels are found in some adult tissues: Malpighian tubules, indirect flight muscles, tubular leg muscles and throughout the nervous system (brain, optic lobes, retina and ventral thoracic neuromere). Lower levels are detected at the posterior end where the reproductive organs and rectum are located.2 Publications

    Gene expression databases

    BgeeiP13607.

    Interactioni

    Subunit structurei

    Composed of three subunits: alpha (catalytic), beta and gamma.

    Protein-protein interaction databases

    BioGridi71866. 51 interactions.
    DIPiDIP-19649N.
    IntActiP13607. 2 interactions.
    STRINGi7227.FBpp0088502.

    Structurei

    3D structure databases

    ProteinModelPortaliP13607.
    SMRiP13607. Positions 49-1041.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei115 – 13521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei147 – 16721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei312 – 33221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei338 – 35821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei808 – 82821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei870 – 89021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei935 – 95521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei970 – 99021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0474.
    GeneTreeiENSGT00560000076866.
    InParanoidiP13607.
    KOiK01539.
    OMAiFQTHPEN.
    OrthoDBiEOG7327N0.
    PhylomeDBiP13607.

    Family and domain databases

    Gene3Di1.20.1110.10. 2 hits.
    2.70.150.10. 2 hits.
    3.40.1110.10. 1 hit.
    InterProiIPR006068. ATPase_P-typ_cation-transptr_C.
    IPR004014. ATPase_P-typ_cation-transptr_N.
    IPR023299. ATPase_P-typ_cyto_domN.
    IPR005775. ATPase_P-typ_Na/K_IIC.
    IPR018303. ATPase_P-typ_P_site.
    IPR023298. ATPase_P-typ_TM_dom.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    [Graphical view]
    PfamiPF00689. Cation_ATPase_C. 1 hit.
    PF00690. Cation_ATPase_N. 1 hit.
    PF00122. E1-E2_ATPase. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view]
    PRINTSiPR00119. CATATPASE.
    SMARTiSM00831. Cation_ATPase_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 3 hits.
    SSF81660. SSF81660. 1 hit.
    TIGRFAMsiTIGR01106. ATPase-IIC_X-K. 1 hit.
    TIGR01494. ATPase_P-type. 2 hits.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Note: Exon 6 has 4 mutually exclusive forms (6a, 6b, 6c and 6d). Additional isoforms may exist.

    Isoform 1 (identifier: P13607-1) [UniParc]FASTAAdd to Basket

    Also known as: A

    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

    MALRSDYEHG RADSYRVATV IATDDDNRTA DGQYKSRRKM PAKVNKKENL     50
    DDLKQELDID FHKISPEELY QRFQTHPENG LSHAKAKENL ERDGPNALTP 100
    PKQTPEWVKF CKNLFGGFAM LLWIGAILCF VAYSIQASTS EEPADDNLYL 150
    GIVLSAVVIV TGIFSYYQES KSSKIMESFK NMVPQFATVI REGEKLTLRA 200
    EDLVLGDVVE VKFGDRIPAD IRIIEARNFK VDNSSLTGES EPQSRGAEFT 250
    HENPLETKNL AFFSTNAVEG TAKGVVISCG DHTVMGRIAG LASGLDTGET 300
    PIAKEIHHFI HLITGVAVFL GVTFFVIAFI LGYHWLDAVI FLIGIIVANV 350
    PEGLLATVTV CLTLTAKRMA SKNCLVKNLE AVETLGSTST ICSDKTGTLT 400
    QNRMTVAHMW FDNQIIEADT TEDQSGVQYD RTSPGFKALS RIATLCNRAE 450
    FKGGQDGVPI LKKEVSGDAS EAALLKCMEL ALGDVMNIRK RNKKIAEVPF 500
    NSTNKYQVSI HETEDTNDPR YLLVMKGAPE RILERCSTIF INGKEKVLDE 550
    EMKEAFNNAY MELGGLGERV LGFCDFMLPS DKYPNGFKFN TDDINFPIDN 600
    LRFVGLMSMI DPPRAAVPDA VAKCRSAGIK VIMVTGDHPI TAKAIAKSVG 650
    IISEGNETVE DIAQRLNIPV SEVNPREAKA AVVHGAELRD VSSDQLDEIL 700
    RYHTEIVFAR TSPQQKLIIV EGCQRMGAIV AVTGDGVNDS PALKKADIGV 750
    AMGIAGSDVS KQAADMILLD DNFASIVTGV EEGRLIFDNL KKSIAYTLTS 800
    NIPEISPFLA FILCDIPLPL GTVTILCIDL GTDMVPAISL AYEHAEADIM 850
    KRPPRDPFND KLVNSRLISM AYGQIGMIQA AAGFFVYFVI MAENGFLPKK 900
    LFGIRKMWDS KAVNDLTDSY GQEWTYRDRK TLEYTCHTAF FISIVVVQWA 950
    DLIICKTRRN SIFQQGMRNW ALNFGLVFET VLAAFLSYCP GMEKGLRMYP 1000
    LKLVWWFPAI PFALAIFIYD ETRRFYLRRN PGGWLEQETY Y 1041
    Length:1,041
    Mass (Da):115,605
    Last modified:June 20, 2001 - v3
    Checksum:iB2DD36B2E9029F43
    GO
    Isoform 2 (identifier: P13607-2) [UniParc]FASTAAdd to Basket

    Also known as: B, C, E

    The sequence of this isoform differs from the canonical sequence as follows:
         1-39: Missing.

    Show »
    Length:1,002
    Mass (Da):111,133
    Checksum:iCA77B36B10EB23E2
    GO
    Isoform 3 (identifier: P13607-3) [UniParc]FASTAAdd to Basket

    Also known as: D

    The sequence of this isoform differs from the canonical sequence as follows:
         1-39: Missing.
         836-878: PAISLAYEHA...SMAYGQIGMI → SLDLCPKPKL...CSPSQLIVKN
         879-1041: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:839
    Mass (Da):91,981
    Checksum:iD8D38F5B5BE2CD37
    GO
    Isoform 4 (identifier: P13607-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-8: MALRSDYE → MSAQ

    Show »
    Length:1,037
    Mass (Da):115,056
    Checksum:i62722EDBA74BBC88
    GO
    Isoform 5 (identifier: P13607-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         835-865: VPAISLAYEHAEADIMKRPPRDPFNDKLVNS → IPAISLAYEGPEADIMKRRPRNPEIDNLVNE

    Show »
    Length:1,041
    Mass (Da):115,632
    Checksum:iD6084967A87F4FAD
    GO
    Isoform 6 (identifier: P13607-6) [UniParc]FASTAAdd to Basket

    Also known as: F, H

    The sequence of this isoform differs from the canonical sequence as follows:
         1-39: Missing.
         844-865: HAEADIMKRPPRDPFNDKLVNS → TAESDIMKRQPRNPFQDKLVNE

    Show »
    Length:1,002
    Mass (Da):111,199
    Checksum:i4146F52C60C4114A
    GO
    Isoform 7 (identifier: P13607-7) [UniParc]FASTAAdd to Basket

    Also known as: G

    The sequence of this isoform differs from the canonical sequence as follows:
         1-39: Missing.
         835-865: VPAISLAYEHAEADIMKRPPRDPFNDKLVNS → IPAISLAYEQAESDIMKRQPRDPYRDNLVNR

    Show »
    Length:1,002
    Mass (Da):111,298
    Checksum:i9762610EA4A85D45
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti69 – 691L → M in CAA32638. (PubMed:2540956)Curated
    Sequence conflicti85 – 851K → R in CAA32638. (PubMed:2540956)Curated
    Sequence conflicti97 – 971Missing in CAA32638. (PubMed:2540956)Curated
    Sequence conflicti112 – 1132KN → ED in CAA32638. (PubMed:2540956)Curated
    Sequence conflicti117 – 1182GF → V in CAA32638. (PubMed:2540956)Curated
    Sequence conflicti163 – 1631I → V in CAA32638. (PubMed:2540956)Curated
    Sequence conflicti192 – 1921E → G in AAC05260. (PubMed:9648860)Curated
    Sequence conflicti196 – 1972LT → PS in CAA32638. (PubMed:2540956)Curated
    Sequence conflicti207 – 2082DV → VL in CAA32638. (PubMed:2540956)Curated
    Sequence conflicti211 – 2122VK → LE in CAA32638. (PubMed:2540956)Curated
    Sequence conflicti216 – 2216RIPADI → LIPLVY in CAA32638. (PubMed:2540956)Curated
    Sequence conflicti228 – 2281N → D in CAA32638. (PubMed:2540956)Curated
    Sequence conflicti270 – 2723GTA → ALP in CAA32638. (PubMed:2540956)Curated
    Sequence conflicti290 – 2901G → A in CAA32638. (PubMed:2540956)Curated
    Sequence conflicti299 – 2991Missing in CAA32638. (PubMed:2540956)Curated
    Sequence conflicti402 – 4021N → T in CAA35504. (PubMed:2557235)Curated
    Sequence conflicti488 – 4881I → N in CAA35504. (PubMed:2557235)Curated
    Sequence conflicti811 – 8111F → S in CAA32638. (PubMed:2540956)Curated
    Sequence conflicti843 – 8431E → D in CAA32638. (PubMed:2540956)Curated

    RNA editingi

    Partially edited. Target of Adar.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti429 – 4291Y → C in RNA edited version.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3939Missing in isoform 2, isoform 3, isoform 6 and isoform 7. 2 PublicationsVSP_000417Add
    BLAST
    Alternative sequencei1 – 88MALRSDYE → MSAQ in isoform 4. CuratedVSP_008074
    Alternative sequencei835 – 86531VPAIS…KLVNS → IPAISLAYEGPEADIMKRRP RNPEIDNLVNE in isoform 5. CuratedVSP_008075Add
    BLAST
    Alternative sequencei835 – 86531VPAIS…KLVNS → IPAISLAYEQAESDIMKRQP RDPYRDNLVNR in isoform 7. CuratedVSP_008076Add
    BLAST
    Alternative sequencei836 – 87843PAISL…QIGMI → SLDLCPKPKLHRRLKLKLLL SQYHSSKLYSYTSCSPSQLI VKN in isoform 3. 1 PublicationVSP_008077Add
    BLAST
    Alternative sequencei844 – 86522HAEAD…KLVNS → TAESDIMKRQPRNPFQDKLV NE in isoform 6. CuratedVSP_000418Add
    BLAST
    Alternative sequencei879 – 1041163Missing in isoform 3. 1 PublicationVSP_008078Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14476 mRNA. Translation: CAA32638.1.
    AF044974 mRNA. Translation: AAC05260.1.
    AE014297 Genomic DNA. Translation: AAF55825.3.
    AE014297 Genomic DNA. Translation: AAF55826.2.
    AE014297 Genomic DNA. Translation: AAF55828.1.
    AE014297 Genomic DNA. Translation: AAS65183.1.
    AE014297 Genomic DNA. Translation: AAS65184.1.
    AE014297 Genomic DNA. Translation: AAS65185.1.
    AE014297 Genomic DNA. Translation: AAS65186.1.
    AY069184 mRNA. Translation: AAL39329.1.
    AY174097 Genomic DNA. Translation: AAO33930.1.
    AY174097 Genomic DNA. Translation: AAO33931.1.
    AY174097 Genomic DNA. Translation: AAO33932.1.
    AY174097 Genomic DNA. Translation: AAO33933.1.
    AY174098 Genomic DNA. Translation: AAO33929.1.
    U55767 Genomic DNA. Translation: AAB01189.1.
    X17471 mRNA. Translation: CAA35504.1.
    PIRiS03632.
    RefSeqiNP_001262790.1. NM_001275861.1. [P13607-2]
    NP_001262791.1. NM_001275862.1. [P13607-2]
    NP_732572.1. NM_169936.2. [P13607-1]
    NP_732573.1. NM_169937.2. [P13607-2]
    NP_732574.1. NM_169938.2. [P13607-2]
    NP_732575.1. NM_169939.2. [P13607-3]
    NP_996247.1. NM_206525.2. [P13607-6]
    NP_996248.1. NM_206526.2. [P13607-7]
    NP_996249.1. NM_206527.2. [P13607-6]
    NP_996250.1. NM_206528.2. [P13607-2]
    UniGeneiDm.6725.

    Genome annotation databases

    EnsemblMetazoaiFBtr0089510; FBpp0088502; FBgn0002921. [P13607-1]
    GeneIDi48971.
    KEGGidme:Dmel_CG5670.

    Keywords - Coding sequence diversityi

    Alternative splicing, RNA editing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14476 mRNA. Translation: CAA32638.1 .
    AF044974 mRNA. Translation: AAC05260.1 .
    AE014297 Genomic DNA. Translation: AAF55825.3 .
    AE014297 Genomic DNA. Translation: AAF55826.2 .
    AE014297 Genomic DNA. Translation: AAF55828.1 .
    AE014297 Genomic DNA. Translation: AAS65183.1 .
    AE014297 Genomic DNA. Translation: AAS65184.1 .
    AE014297 Genomic DNA. Translation: AAS65185.1 .
    AE014297 Genomic DNA. Translation: AAS65186.1 .
    AY069184 mRNA. Translation: AAL39329.1 .
    AY174097 Genomic DNA. Translation: AAO33930.1 .
    AY174097 Genomic DNA. Translation: AAO33931.1 .
    AY174097 Genomic DNA. Translation: AAO33932.1 .
    AY174097 Genomic DNA. Translation: AAO33933.1 .
    AY174098 Genomic DNA. Translation: AAO33929.1 .
    U55767 Genomic DNA. Translation: AAB01189.1 .
    X17471 mRNA. Translation: CAA35504.1 .
    PIRi S03632.
    RefSeqi NP_001262790.1. NM_001275861.1. [P13607-2 ]
    NP_001262791.1. NM_001275862.1. [P13607-2 ]
    NP_732572.1. NM_169936.2. [P13607-1 ]
    NP_732573.1. NM_169937.2. [P13607-2 ]
    NP_732574.1. NM_169938.2. [P13607-2 ]
    NP_732575.1. NM_169939.2. [P13607-3 ]
    NP_996247.1. NM_206525.2. [P13607-6 ]
    NP_996248.1. NM_206526.2. [P13607-7 ]
    NP_996249.1. NM_206527.2. [P13607-6 ]
    NP_996250.1. NM_206528.2. [P13607-2 ]
    UniGenei Dm.6725.

    3D structure databases

    ProteinModelPortali P13607.
    SMRi P13607. Positions 49-1041.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 71866. 51 interactions.
    DIPi DIP-19649N.
    IntActi P13607. 2 interactions.
    STRINGi 7227.FBpp0088502.

    Proteomic databases

    PaxDbi P13607.
    PRIDEi P13607.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0089510 ; FBpp0088502 ; FBgn0002921 . [P13607-1 ]
    GeneIDi 48971.
    KEGGi dme:Dmel_CG5670.

    Organism-specific databases

    CTDi 48971.
    FlyBasei FBgn0002921. Atpalpha.

    Phylogenomic databases

    eggNOGi COG0474.
    GeneTreei ENSGT00560000076866.
    InParanoidi P13607.
    KOi K01539.
    OMAi FQTHPEN.
    OrthoDBi EOG7327N0.
    PhylomeDBi P13607.

    Miscellaneous databases

    ChiTaRSi Atpalpha. drosophila.
    GenomeRNAii 48971.
    NextBioi 839577.

    Gene expression databases

    Bgeei P13607.

    Family and domain databases

    Gene3Di 1.20.1110.10. 2 hits.
    2.70.150.10. 2 hits.
    3.40.1110.10. 1 hit.
    InterProi IPR006068. ATPase_P-typ_cation-transptr_C.
    IPR004014. ATPase_P-typ_cation-transptr_N.
    IPR023299. ATPase_P-typ_cyto_domN.
    IPR005775. ATPase_P-typ_Na/K_IIC.
    IPR018303. ATPase_P-typ_P_site.
    IPR023298. ATPase_P-typ_TM_dom.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    [Graphical view ]
    Pfami PF00689. Cation_ATPase_C. 1 hit.
    PF00690. Cation_ATPase_N. 1 hit.
    PF00122. E1-E2_ATPase. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view ]
    PRINTSi PR00119. CATATPASE.
    SMARTi SM00831. Cation_ATPase_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 3 hits.
    SSF81660. SSF81660. 1 hit.
    TIGRFAMsi TIGR01106. ATPase-IIC_X-K. 1 hit.
    TIGR01494. ATPase_P-type. 2 hits.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization and expression of the (Na+ + K+)-ATPase alpha-subunit in Drosophila melanogaster."
      Lebovitz R.M., Takeyasu K., Fambrough D.M.
      EMBO J. 8:193-202(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Strain: Canton-S and Oregon-R.
      Tissue: Embryo, Head and Pupae.
    2. "Functional analysis and tissue-specific expression of Drosophila Na+,K+-ATPase subunits."
      Sun B., Wang W., Salvaterra P.M.
      J. Neurochem. 71:142-151(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Head.
    3. "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.
    4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), RNA EDITING OF POSITION 429.
      Strain: Berkeley.
      Tissue: Head.
    6. "Neural dysfunction and neurodegeneration in Drosophila Na+/K+ ATPase alpha subunit mutants."
      Palladino M.J., Bower J.E., Kreber R., Ganetzky B.
      J. Neurosci. 23:1276-1286(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35 (ISOFORM 4), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 835-865 (ISOFORMS 1; 5; 6 AND 7), FUNCTION, MUTAGENESIS OF ASP-1020 AND GLU-1021.
    7. "The Drosophila Na,K-ATPase alpha-subunit gene: gene structure, promoter function and analysis of a cold-sensitive recessive-lethal mutation."
      Feng Y., Huynh L., Takeyasu K., Fambrough D.M.
      Genes Funct. 1:99-117(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
    8. "Amplification of the phosphorylation site-ATP-binding site cDNA fragment of the Na+,K(+)-ATPase and the Ca2(+)-ATPase of Drosophila melanogaster by polymerase chain reaction."
      Varadi A., Gilmore-Heber M., Benz E.J. Jr.
      FEBS Lett. 258:203-207(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 400-524.
    9. "RNA editing in Drosophila melanogaster: new targets and functional consequences."
      Stapleton M., Carlson J.W., Celniker S.E.
      RNA 12:1922-1932(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA EDITING OF POSITION 429.

    Entry informationi

    Entry nameiATNA_DROME
    AccessioniPrimary (citable) accession number: P13607
    Secondary accession number(s): A4V366
    , A4V367, O61494, Q0KI37, Q7KS94, Q7KS95, Q86MY6, Q86MY7, Q86MY8, Q86MY9, Q86MZ0, Q8IN40, Q8T0L8, Q9VDG6, Q9VDG7, Q9VDG8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: June 20, 2001
    Last modified: October 1, 2014
    This is version 158 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Miscellaneous

    Ouabain-sensitive electrogenic ion pump.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3