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Protein

Sodium/potassium-transporting ATPase subunit alpha

Gene

Atpalpha

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

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

  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: InterPro
  • sodium:potassium-exchanging ATPase activity Source: FlyBase

GO - Biological processi

  • adult locomotory behavior Source: FlyBase
  • cation transmembrane transport Source: GOC
  • cation transport Source: FlyBase
  • determination of adult lifespan Source: FlyBase
  • embryonic development via the syncytial blastoderm Source: FlyBase
  • jump response Source: FlyBase
  • locomotory behavior Source: FlyBase
  • neuromuscular process Source: FlyBase
  • regulation of cell shape Source: FlyBase
  • regulation of tube architecture, open tracheal system Source: FlyBase
  • regulation of tube diameter, open tracheal system Source: FlyBase
  • regulation of tube length, open tracheal system Source: FlyBase
  • response to mechanical stimulus Source: FlyBase
  • response to temperature stimulus Source: FlyBase
  • sensory perception of sound Source: FlyBase
  • septate junction assembly Source: FlyBase
  • sodium ion transmembrane transport Source: GOC
  • synaptic growth at neuromuscular junction Source: FlyBase
  • synaptic transmission Source: FlyBase
  • tissue homeostasis Source: FlyBase
  • trachea morphogenesis Source: FlyBase
Complete GO annotation...

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 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0002921. Atpalpha.

Subcellular locationi

Topology

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

GO - Cellular componenti

  • basolateral plasma membrane Source: FlyBase
  • cytoplasm Source: FlyBase
  • nucleus Source: FlyBase
  • plasma membrane Source: FlyBase
  • septate junction Source: FlyBase
  • sodium:potassium-exchanging ATPase complex Source: FlyBase
Complete GO annotation...

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.
ExpressionAtlasiP13607. differential.
GenevisibleiP13607. DM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi71866. 51 interactions.
DIPiDIP-19649N.
IntActiP13607. 36 interactions.
STRINGi7227.FBpp0088502.

Structurei

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00800000124052.
InParanoidiP13607.
OMAiFCDFMLP.
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.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR005775. P-type_ATPase_IIC.
IPR001757. P_typ_ATPase.
[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. AlignAdd to basket

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

        10         20         30         40         50
MALRSDYEHG RADSYRVATV IATDDDNRTA DGQYKSRRKM PAKVNKKENL
60 70 80 90 100
DDLKQELDID FHKISPEELY QRFQTHPENG LSHAKAKENL ERDGPNALTP
110 120 130 140 150
PKQTPEWVKF CKNLFGGFAM LLWIGAILCF VAYSIQASTS EEPADDNLYL
160 170 180 190 200
GIVLSAVVIV TGIFSYYQES KSSKIMESFK NMVPQFATVI REGEKLTLRA
210 220 230 240 250
EDLVLGDVVE VKFGDRIPAD IRIIEARNFK VDNSSLTGES EPQSRGAEFT
260 270 280 290 300
HENPLETKNL AFFSTNAVEG TAKGVVISCG DHTVMGRIAG LASGLDTGET
310 320 330 340 350
PIAKEIHHFI HLITGVAVFL GVTFFVIAFI LGYHWLDAVI FLIGIIVANV
360 370 380 390 400
PEGLLATVTV CLTLTAKRMA SKNCLVKNLE AVETLGSTST ICSDKTGTLT
410 420 430 440 450
QNRMTVAHMW FDNQIIEADT TEDQSGVQYD RTSPGFKALS RIATLCNRAE
460 470 480 490 500
FKGGQDGVPI LKKEVSGDAS EAALLKCMEL ALGDVMNIRK RNKKIAEVPF
510 520 530 540 550
NSTNKYQVSI HETEDTNDPR YLLVMKGAPE RILERCSTIF INGKEKVLDE
560 570 580 590 600
EMKEAFNNAY MELGGLGERV LGFCDFMLPS DKYPNGFKFN TDDINFPIDN
610 620 630 640 650
LRFVGLMSMI DPPRAAVPDA VAKCRSAGIK VIMVTGDHPI TAKAIAKSVG
660 670 680 690 700
IISEGNETVE DIAQRLNIPV SEVNPREAKA AVVHGAELRD VSSDQLDEIL
710 720 730 740 750
RYHTEIVFAR TSPQQKLIIV EGCQRMGAIV AVTGDGVNDS PALKKADIGV
760 770 780 790 800
AMGIAGSDVS KQAADMILLD DNFASIVTGV EEGRLIFDNL KKSIAYTLTS
810 820 830 840 850
NIPEISPFLA FILCDIPLPL GTVTILCIDL GTDMVPAISL AYEHAEADIM
860 870 880 890 900
KRPPRDPFND KLVNSRLISM AYGQIGMIQA AAGFFVYFVI MAENGFLPKK
910 920 930 940 950
LFGIRKMWDS KAVNDLTDSY GQEWTYRDRK TLEYTCHTAF FISIVVVQWA
960 970 980 990 1000
DLIICKTRRN SIFQQGMRNW ALNFGLVFET VLAAFLSYCP GMEKGLRMYP
1010 1020 1030 1040
LKLVWWFPAI PFALAIFIYD ETRRFYLRRN PGGWLEQETY Y
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

Edited at position 429.2 Publications
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:
EMBLi
GenBanki
DDBJi
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_001275862.2. [P13607-2]
NP_732572.1. NM_169936.3. [P13607-1]
NP_732573.1. NM_169937.3. [P13607-2]
NP_732574.1. NM_169938.3. [P13607-2]
NP_732575.1. NM_169939.2. [P13607-3]
NP_996247.1. NM_206525.3. [P13607-6]
NP_996248.1. NM_206526.3. [P13607-7]
NP_996249.1. NM_206527.3. [P13607-6]
NP_996250.1. NM_206528.3. [P13607-2]
UniGeneiDm.6725.

Genome annotation databases

EnsemblMetazoaiFBtr0089510; FBpp0088502; FBgn0002921. [P13607-1]
GeneIDi48971.

Keywords - Coding sequence diversityi

Alternative splicing, RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001275862.2. [P13607-2]
NP_732572.1. NM_169936.3. [P13607-1]
NP_732573.1. NM_169937.3. [P13607-2]
NP_732574.1. NM_169938.3. [P13607-2]
NP_732575.1. NM_169939.2. [P13607-3]
NP_996247.1. NM_206525.3. [P13607-6]
NP_996248.1. NM_206526.3. [P13607-7]
NP_996249.1. NM_206527.3. [P13607-6]
NP_996250.1. NM_206528.3. [P13607-2]
UniGeneiDm.6725.

3D structure databases

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

Protein-protein interaction databases

BioGridi71866. 51 interactions.
DIPiDIP-19649N.
IntActiP13607. 36 interactions.
STRINGi7227.FBpp0088502.

Proteomic databases

PaxDbiP13607.
PRIDEiP13607.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0089510; FBpp0088502; FBgn0002921. [P13607-1]
GeneIDi48971.

Organism-specific databases

CTDi48971.
FlyBaseiFBgn0002921. Atpalpha.

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00800000124052.
InParanoidiP13607.
OMAiFCDFMLP.
OrthoDBiEOG7327N0.
PhylomeDBiP13607.

Miscellaneous databases

ChiTaRSiAtpalpha. fly.
GenomeRNAii48971.
NextBioi839577.
PROiP13607.

Gene expression databases

BgeeiP13607.
ExpressionAtlasiP13607. differential.
GenevisibleiP13607. DM.

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.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR005775. P-type_ATPase_IIC.
IPR001757. P_typ_ATPase.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 166 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

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.