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P06686 (AT1A2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sodium/potassium-transporting ATPase subunit alpha-2

Short name=Na(+)/K(+) ATPase alpha-2 subunit
EC=3.6.3.9
Alternative name(s):
Na(+)/K(+) ATPase alpha(+) subunit
Sodium pump subunit alpha-2
Gene names
Name:Atp1a2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1020 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

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 By similarity. Cell membrane; Multi-pass membrane protein By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processIon transport
Potassium transport
Sodium transport
Sodium/potassium transport
Transport
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Potassium
Sodium
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP biosynthetic process

Inferred from electronic annotation. Source: InterPro

ATP hydrolysis coupled proton transport

Inferred from mutant phenotype PubMed 12529322. Source: RGD

adult locomotory behavior

Inferred from electronic annotation. Source: Ensembl

cellular response to mechanical stimulus

Inferred from direct assay PubMed 17458903. Source: RGD

energy coupled proton transmembrane transport, against electrochemical gradient

Traceable author statement PubMed 11950769. Source: RGD

locomotion

Inferred from electronic annotation. Source: Ensembl

negative regulation of cytosolic calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

negative regulation of heart contraction

Inferred from electronic annotation. Source: Ensembl

negative regulation of striated muscle contraction

Inferred from electronic annotation. Source: Ensembl

neurotransmitter uptake

Inferred from electronic annotation. Source: Ensembl

potassium ion transport

Inferred from direct assay PubMed 12093728PubMed 16624992. Source: RGD

regulation of blood pressure

Inferred from electronic annotation. Source: Ensembl

regulation of cardiac muscle cell contraction

Inferred from mutant phenotype PubMed 17442282. Source: RGD

regulation of respiratory gaseous exchange by neurological system process

Inferred from electronic annotation. Source: Ensembl

regulation of smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

regulation of the force of heart contraction

Inferred from electronic annotation. Source: Ensembl

regulation of vasoconstriction

Inferred from electronic annotation. Source: Ensembl

response to nicotine

Inferred from direct assay PubMed 22442718. Source: RGD

sodium ion transmembrane transport

Inferred from direct assay PubMed 16624992. Source: GOC

sodium ion transport

Inferred from direct assay PubMed 12093728PubMed 16624992. Source: RGD

visual learning

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentT-tubule

Inferred from direct assay PubMed 17442282. Source: RGD

caveola

Inferred from direct assay PubMed 16624992. Source: RGD

dendritic spine

Inferred from direct assay PubMed 11950769. Source: RGD

endosome

Inferred from direct assay PubMed 16893515. Source: RGD

neuron projection

Inferred from direct assay PubMed 11950769. Source: RGD

sarcolemma

Inferred from direct assay PubMed 17442282. Source: RGD

sodium:potassium-exchanging ATPase complex

Inferred from direct assay PubMed 12093728PubMed 16624992. Source: RGD

synapse

Inferred from direct assay PubMed 11950769. Source: RGD

   Molecular_functionATP binding

Inferred from mutant phenotype PubMed 12529322. Source: RGD

cation-transporting ATPase activity

Inferred from mutant phenotype PubMed 12529322. Source: RGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 12093728. Source: RGD

sodium:potassium-exchanging ATPase activity

Inferred from direct assay PubMed 16624992. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 55
PRO_0000002507
Chain6 – 10201015Sodium/potassium-transporting ATPase subunit alpha-2
PRO_0000002508

Regions

Topological domain6 – 8580Cytoplasmic Potential
Transmembrane86 – 10621Helical; Potential
Topological domain107 – 12923Extracellular Potential
Transmembrane130 – 15021Helical; Potential
Topological domain151 – 286136Cytoplasmic Potential
Transmembrane287 – 30620Helical; Potential
Topological domain307 – 31812Extracellular Potential
Transmembrane319 – 33618Helical; Potential
Topological domain337 – 769433Cytoplasmic Potential
Transmembrane770 – 78920Helical; Potential
Topological domain790 – 79910Extracellular Potential
Transmembrane800 – 82021Helical; Potential
Topological domain821 – 84020Cytoplasmic Potential
Transmembrane841 – 86323Helical; Potential
Topological domain864 – 91552Extracellular Potential
Transmembrane916 – 93520Helical; Potential
Topological domain936 – 94813Cytoplasmic Potential
Transmembrane949 – 96719Helical; Potential
Topological domain968 – 98215Extracellular Potential
Transmembrane983 – 100321Helical; Potential
Topological domain1004 – 102017Cytoplasmic Potential
Region80 – 823Interaction with phosphoinositide-3 kinase By similarity

Sites

Active site37414-aspartylphosphate intermediate By similarity
Metal binding7141Magnesium By similarity
Metal binding7181Magnesium By similarity

Amino acid modifications

Modified residue5701Phosphothreonine By similarity
Modified residue5871Phosphoserine By similarity
Modified residue9401Phosphoserine; by PKA By similarity

Sequences

Sequence LengthMass (Da)Tools
P06686 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 5436E795BD5B4CFA

FASTA1,020112,217
        10         20         30         40         50         60 
MGRGAGREYS PAATTAENGG GKKKQKEKEL DELKKEVAMD DHKLSLDELG RKYQVDLSKG 

        70         80         90        100        110        120 
LTNQRAQDIL ARDGPNALTP PPTTPEWVKF CRQLFGGFSI LLWIGALLCF LAYGILAAME 

       130        140        150        160        170        180 
DEPSNDNLYL GIVLAAVVIV TGCFSYYQEA KSSKIMDSFK NMVPQQALVI REGEKMQINA 

       190        200        210        220        230        240 
EEVVVGDLVE VKGGDRVPAD LRIISSHGCK VDNSSLTGES EPQTRSPEFT HENPLETRNI 

       250        260        270        280        290        300 
CFFSTNCVEG TARGIVIATG DRTVMGRIAT LASGLEVGQT PIAMEIEHFI QLITGVAVFL 

       310        320        330        340        350        360 
GVSFFVLSLI LGYSWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA RKNCLVKNLE 

       370        380        390        400        410        420 
AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIHEADT TEDQSGATFD KRSPTWTALS 

       430        440        450        460        470        480 
RIAGLCNRAV FKAGQENISV SKRDTAGDAS ESALLKCIEL SCGSVRKMRD RNPKVAEIPF 

       490        500        510        520        530        540 
NSTNKYQLSI HEREDSPQSH VLVMKGAPER ILDRCSTILV QGKEIPLDKE MQDAFQNAYM 

       550        560        570        580        590        600 
ELGGLGERVL GFCQLNLPSG KFPRGFKFDT DELNFPTEKL CFVGLMSMID PPRAAVPDAV 

       610        620        630        640        650        660 
GKCRSAGIKV IMVTGDHPIT AKAIAKGVGI ISEGNETVED IAARLNIPVS QVNPREAKAC 

       670        680        690        700        710        720 
VVHGSDLKDM TSEQLDEILR DHTEIVFART SPQQKLIIVE GCQRQGAIVA VTGDGVNDSP 

       730        740        750        760        770        780 
ALKKADIGIA MGISGSDVSK QAADMILLDD NFASIVTGVE EGRLIFDNLK KSIAYTLTSN 

       790        800        810        820        830        840 
IPEITPFLLF IIANIPLPLG TVTILCIDLG TDMVPAISLA YEAAESDIMK RQPRNSQTDK 

       850        860        870        880        890        900 
LVNERLISMA YGQIGMIQAL GGFFTYFVIL AENGFLPSRL LGIRLDWDDR TTNDLEDSYG 

       910        920        930        940        950        960 
QEWTYEQRKV VEFTCHTAFF ASIVVVQWAD LIICKTRRNS VFQQGMKNKI LIFGLLEETA 

       970        980        990       1000       1010       1020 
LAAFLSYCPG MGVALRMYPL KVTWWFCAFP YSLLIFIYDE VRKLILRRYP GGWVEKETYY 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of three distinct forms of the Na+,K+-ATPase alpha-subunit from rat brain."
Shull G.E., Greeb J., Lingrel J.B.
Biochemistry 25:8125-8132(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart.
[3]"Regulation of Na+,K(+)-ATPases. I. Cloning and analysis of the 5'-flanking region of the rat NKAA2 gene encoding the alpha 2 subunit."
Kawakami K., Yagawa Y., Nagano K.
Gene 91:267-270(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
[4]Lubec G., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 594-602; 645-655; 659-668 AND 741-770, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14512 mRNA. Translation: AAA40776.1.
BC085764 mRNA. Translation: AAH85764.1.
D90049 Genomic DNA. Translation: BAA14102.1.
PIRB24639.
I54059.
RefSeqNP_036637.1. NM_012505.2.
UniGeneRn.1042.
Rn.214222.

3D structure databases

ProteinModelPortalP06686.
SMRP06686. Positions 28-1020.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246400. 7 interactions.
IntActP06686. 1 interaction.
STRING10116.ENSRNOP00000054947.

PTM databases

PhosphoSiteP06686.

Proteomic databases

PaxDbP06686.
PRIDEP06686.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000058143; ENSRNOP00000054947; ENSRNOG00000007290.
GeneID24212.
KEGGrno:24212.
UCSCRGD:2168. rat.

Organism-specific databases

CTD477.
RGD2168. Atp1a2.

Phylogenomic databases

eggNOGCOG0474.
GeneTreeENSGT00560000076866.
HOGENOMHOG000265622.
HOVERGENHBG004298.
KOK01539.
OMAIINIPLP.
OrthoDBEOG7327N0.
PhylomeDBP06686.
TreeFamTF312838.

Enzyme and pathway databases

SABIO-RKP06686.

Gene expression databases

GenevestigatorP06686.

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. 2 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

NextBio602621.

Entry information

Entry nameAT1A2_RAT
AccessionPrimary (citable) accession number: P06686
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: June 11, 2014
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families