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P13607 (ATNA_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sodium/potassium-transporting ATPase subunit alpha

Short name=Na(+)/K(+) ATPase alpha subunit
EC=3.6.3.9
Alternative name(s):
Sodium pump subunit alpha
Gene names
Name:Atpalpha
Synonyms:Na-p
ORF Names:CG5670
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1041 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.6

Catalytic activity

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

Subunit structure

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

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

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. Ref.1 Ref.2

Miscellaneous

Ouabain-sensitive electrogenic ion pump.

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily. [View classification]

RNA editing

Edited at position 429.
Partially edited. Target of Adar. Ref.5 Ref.9

Ontologies

Keywords
   Biological processIon transport
Potassium transport
Sodium transport
Sodium/potassium transport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
RNA editing
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
Potassium
Sodium
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP biosynthetic process

Inferred from electronic annotation. Source: InterPro

adult locomotory behavior

Inferred from mutant phenotype Ref.6PubMed 19455355. Source: FlyBase

cation transport

Inferred from direct assay Ref.2Ref.7. Source: FlyBase

determination of adult lifespan

Inferred from mutant phenotype Ref.6PubMed 16272407PubMed 19455355. Source: FlyBase

embryonic development via the syncytial blastoderm

Inferred from mutant phenotype PubMed 8978055. Source: FlyBase

jump response

Inferred from mutant phenotype PubMed 19455355. Source: FlyBase

locomotory behavior

Inferred from mutant phenotype PubMed 11691629. Source: FlyBase

neuromuscular process

Inferred from mutant phenotype Ref.6. Source: FlyBase

regulation of cell shape

Inferred from mutant phenotype PubMed 12466193. Source: FlyBase

regulation of tube architecture, open tracheal system

Traceable author statement PubMed 14570584. Source: FlyBase

regulation of tube diameter, open tracheal system

Inferred from mutant phenotype PubMed 12466193PubMed 12930776. Source: FlyBase

regulation of tube length, open tracheal system

Inferred from mutant phenotype PubMed 12466193PubMed 12930776. Source: FlyBase

response to mechanical stimulus

Inferred from mutant phenotype PubMed 11691629Ref.6PubMed 8110464. Source: FlyBase

response to temperature stimulus

Inferred from mutant phenotype Ref.6Ref.7. Source: FlyBase

sensory perception of sound

Inferred from mutant phenotype PubMed 23248276. Source: FlyBase

septate junction assembly

Inferred from mutant phenotype PubMed 12930776. Source: FlyBase

sodium ion transmembrane transport

Inferred from mutant phenotype PubMed 8110464Ref.2Ref.7. Source: GOC

synaptic growth at neuromuscular junction

Inferred from mutant phenotype PubMed 15281071. Source: FlyBase

synaptic transmission

Inferred from direct assay PubMed 15281071. Source: FlyBase

tissue homeostasis

Inferred from mutant phenotype Ref.6. Source: FlyBase

trachea morphogenesis

Inferred from mutant phenotype PubMed 19455355. Source: FlyBase

   Cellular_componentbasolateral plasma membrane

Inferred from direct assay PubMed 22417167. Source: FlyBase

nucleus

Inferred from direct assay PubMed 8110464. Source: FlyBase

plasma membrane

Inferred from direct assay PubMed 14668392PubMed 20462449PubMed 23248276PubMed 8110464. Source: FlyBase

septate junction

Inferred from direct assay PubMed 12782686PubMed 12930776. Source: FlyBase

sodium:potassium-exchanging ATPase complex

Inferred by curator Ref.2. Source: FlyBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: InterPro

sodium:potassium-exchanging ATPase activity

Inferred from mutant phenotype PubMed 8110464Ref.7. Source: FlyBase

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Note: Exon 6 has 4 mutually exclusive forms (6a, 6b, 6c and 6d). Additional isoforms may exist.
Isoform 1 (identifier: P13607-1)

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.
Isoform 2 (identifier: P13607-2)

Also known as: B; C; E;

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.
Isoform 3 (identifier: P13607-3)

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.
Isoform 4 (identifier: P13607-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MALRSDYE → MSAQ
Isoform 5 (identifier: P13607-5)

The sequence of this isoform differs from the canonical sequence as follows:
     835-865: VPAISLAYEHAEADIMKRPPRDPFNDKLVNS → IPAISLAYEGPEADIMKRRPRNPEIDNLVNE
Isoform 6 (identifier: P13607-6)

Also known as: F; H;

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.
     844-865: HAEADIMKRPPRDPFNDKLVNS → TAESDIMKRQPRNPFQDKLVNE
Isoform 7 (identifier: P13607-7)

Also known as: G;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10411041Sodium/potassium-transporting ATPase subunit alpha
PRO_0000046309

Regions

Transmembrane115 – 13521Helical; Potential
Transmembrane147 – 16721Helical; Potential
Transmembrane312 – 33221Helical; Potential
Transmembrane338 – 35821Helical; Potential
Transmembrane808 – 82821Helical; Potential
Transmembrane870 – 89021Helical; Potential
Transmembrane935 – 95521Helical; Potential
Transmembrane970 – 99021Helical; Potential

Sites

Active site39414-aspartylphosphate intermediate Probable
Binding site5261ATP By similarity

Natural variations

Alternative sequence1 – 3939Missing in isoform 2, isoform 3, isoform 6 and isoform 7.
VSP_000417
Alternative sequence1 – 88MALRSDYE → MSAQ in isoform 4.
VSP_008074
Alternative sequence835 – 86531VPAIS…KLVNS → IPAISLAYEGPEADIMKRRP RNPEIDNLVNE in isoform 5.
VSP_008075
Alternative sequence835 – 86531VPAIS…KLVNS → IPAISLAYEQAESDIMKRQP RDPYRDNLVNR in isoform 7.
VSP_008076
Alternative sequence836 – 87843PAISL…QIGMI → SLDLCPKPKLHRRLKLKLLL SQYHSSKLYSYTSCSPSQLI VKN in isoform 3.
VSP_008077
Alternative sequence844 – 86522HAEAD…KLVNS → TAESDIMKRQPRNPFQDKLV NE in isoform 6.
VSP_000418
Alternative sequence879 – 1041163Missing in isoform 3.
VSP_008078
Natural variant4291Y → C in RNA edited version.

Experimental info

Mutagenesis10201D → N in allele ATP-alpha-dts2; homozygous lethal and temperature dependent bang sensitive paralysis, shortened life span and neurodegeneration when heterozygous. Ref.6
Mutagenesis10211E → K in allele ATP-alpha-dts1; homozygous lethal and temperature dependent bang sensitive paralysis, shortened life span and neurodegeneration when heterozygous. Ref.6
Sequence conflict691L → M in CAA32638. Ref.1
Sequence conflict851K → R in CAA32638. Ref.1
Sequence conflict971Missing in CAA32638. Ref.1
Sequence conflict112 – 1132KN → ED in CAA32638. Ref.1
Sequence conflict117 – 1182GF → V in CAA32638. Ref.1
Sequence conflict1631I → V in CAA32638. Ref.1
Sequence conflict1921E → G in AAC05260. Ref.2
Sequence conflict196 – 1972LT → PS in CAA32638. Ref.1
Sequence conflict207 – 2082DV → VL in CAA32638. Ref.1
Sequence conflict211 – 2122VK → LE in CAA32638. Ref.1
Sequence conflict216 – 2216RIPADI → LIPLVY in CAA32638. Ref.1
Sequence conflict2281N → D in CAA32638. Ref.1
Sequence conflict270 – 2723GTA → ALP in CAA32638. Ref.1
Sequence conflict2901G → A in CAA32638. Ref.1
Sequence conflict2991Missing in CAA32638. Ref.1
Sequence conflict4021N → T in CAA35504. Ref.8
Sequence conflict4881I → N in CAA35504. Ref.8
Sequence conflict8111F → S in CAA32638. Ref.1
Sequence conflict8431E → D in CAA32638. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A) [UniParc].

Last modified June 20, 2001. Version 3.
Checksum: B2DD36B2E9029F43

FASTA1,041115,605
        10         20         30         40         50         60 
MALRSDYEHG RADSYRVATV IATDDDNRTA DGQYKSRRKM PAKVNKKENL DDLKQELDID 

        70         80         90        100        110        120 
FHKISPEELY QRFQTHPENG LSHAKAKENL ERDGPNALTP PKQTPEWVKF CKNLFGGFAM 

       130        140        150        160        170        180 
LLWIGAILCF VAYSIQASTS EEPADDNLYL GIVLSAVVIV TGIFSYYQES KSSKIMESFK 

       190        200        210        220        230        240 
NMVPQFATVI REGEKLTLRA EDLVLGDVVE VKFGDRIPAD IRIIEARNFK VDNSSLTGES 

       250        260        270        280        290        300 
EPQSRGAEFT HENPLETKNL AFFSTNAVEG TAKGVVISCG DHTVMGRIAG LASGLDTGET 

       310        320        330        340        350        360 
PIAKEIHHFI HLITGVAVFL GVTFFVIAFI LGYHWLDAVI FLIGIIVANV PEGLLATVTV 

       370        380        390        400        410        420 
CLTLTAKRMA SKNCLVKNLE AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIIEADT 

       430        440        450        460        470        480 
TEDQSGVQYD RTSPGFKALS RIATLCNRAE FKGGQDGVPI LKKEVSGDAS EAALLKCMEL 

       490        500        510        520        530        540 
ALGDVMNIRK RNKKIAEVPF NSTNKYQVSI HETEDTNDPR YLLVMKGAPE RILERCSTIF 

       550        560        570        580        590        600 
INGKEKVLDE EMKEAFNNAY MELGGLGERV LGFCDFMLPS DKYPNGFKFN TDDINFPIDN 

       610        620        630        640        650        660 
LRFVGLMSMI DPPRAAVPDA VAKCRSAGIK VIMVTGDHPI TAKAIAKSVG IISEGNETVE 

       670        680        690        700        710        720 
DIAQRLNIPV SEVNPREAKA AVVHGAELRD VSSDQLDEIL RYHTEIVFAR TSPQQKLIIV 

       730        740        750        760        770        780 
EGCQRMGAIV AVTGDGVNDS PALKKADIGV AMGIAGSDVS KQAADMILLD DNFASIVTGV 

       790        800        810        820        830        840 
EEGRLIFDNL KKSIAYTLTS NIPEISPFLA FILCDIPLPL GTVTILCIDL GTDMVPAISL 

       850        860        870        880        890        900 
AYEHAEADIM KRPPRDPFND KLVNSRLISM AYGQIGMIQA AAGFFVYFVI MAENGFLPKK 

       910        920        930        940        950        960 
LFGIRKMWDS KAVNDLTDSY GQEWTYRDRK TLEYTCHTAF FISIVVVQWA DLIICKTRRN 

       970        980        990       1000       1010       1020 
SIFQQGMRNW ALNFGLVFET VLAAFLSYCP GMEKGLRMYP LKLVWWFPAI PFALAIFIYD 

      1030       1040 
ETRRFYLRRN PGGWLEQETY Y 

« Hide

Isoform 2 (B) (C) (E) [UniParc].

Checksum: CA77B36B10EB23E2
Show »

FASTA1,002111,133
Isoform 3 (D) [UniParc].

Checksum: D8D38F5B5BE2CD37
Show »

FASTA83991,981
Isoform 4 [UniParc].

Checksum: 62722EDBA74BBC88
Show »

FASTA1,037115,056
Isoform 5 [UniParc].

Checksum: D6084967A87F4FAD
Show »

FASTA1,041115,632
Isoform 6 (F) (H) [UniParc].

Checksum: 4146F52C60C4114A
Show »

FASTA1,002111,199
Isoform 7 (G) [UniParc].

Checksum: 9762610EA4A85D45
Show »

FASTA1,002111,298

References

« Hide 'large scale' references
[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. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS03632.
RefSeqNP_001262790.1. NM_001275861.1.
NP_001262791.1. NM_001275862.1.
NP_732572.1. NM_169936.2.
NP_732573.1. NM_169937.2.
NP_732574.1. NM_169938.2.
NP_732575.1. NM_169939.2.
NP_996247.1. NM_206525.2.
NP_996248.1. NM_206526.2.
NP_996249.1. NM_206527.2.
NP_996250.1. NM_206528.2.
UniGeneDm.6725.

3D structure databases

ProteinModelPortalP13607.
SMRP13607. Positions 49-1041.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid71866. 50 interactions.
DIPDIP-19649N.
IntActP13607. 2 interactions.
STRING7227.FBpp0088502.

Proteomic databases

PaxDbP13607.
PRIDEP13607.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0089510; FBpp0088502; FBgn0002921. [P13607-1]
GeneID48971.
KEGGdme:Dmel_CG5670.

Organism-specific databases

CTD48971.
FlyBaseFBgn0002921. Atpalpha.

Phylogenomic databases

eggNOGCOG0474.
GeneTreeENSGT00560000076866.
InParanoidP13607.
KOK01539.
OMAFQTHPEN.
OrthoDBEOG7327N0.
PhylomeDBP13607.

Gene expression databases

BgeeP13607.

Family and domain databases

Gene3D1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProIPR006068. 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]
PfamPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsTIGR01106. ATPase-IIC_X-K. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAtpalpha. drosophila.
GenomeRNAi48971.
NextBio839577.

Entry information

Entry nameATNA_DROME
AccessionPrimary (citable) accession number: P13607
Secondary accession number(s): A4V366 expand/collapse secondary AC list , A4V367, O61494, Q0KI37, Q7KS94, Q7KS95, Q86MY6, Q86MY7, Q86MY8, Q86MY9, Q86MZ0, Q8IN40, Q8T0L8, Q9VDG6, Q9VDG7, Q9VDG8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: June 20, 2001
Last modified: April 16, 2014
This is version 154 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

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